Developmental Expression Profiles of Celsr (Flamingo) Genes in the Mouse

Total Page:16

File Type:pdf, Size:1020Kb

Developmental Expression Profiles of Celsr (Flamingo) Genes in the Mouse Mechanisms of Development 112 (2002) 157–160 www.elsevier.com/locate/modo Gene expression pattern Developmental expression profiles of Celsr (Flamingo) genes in the mouse F. Tissir1, O. De-Backer, A.M. Goffinet1, C. Lambert de Rouvroit* Neurobiology Unit 2853, FUNDP School of Medicine, B5000 Namur, Belgium Received 10 October 2001; received in revised form 8 November 2001; accepted 8 November 2001 Abstract Celsr, also called Flamingo (Fmi) genes encode proteins of the cadherin superfamily. Celsr cadherins are seven-pass transmembrane proteins with nine cadherin repeats in the extracellular domain, and an anonymous intracellular C-terminus. The Drosophila Fmi gene regulates epithelial planar cell polarity and dendritic field deployment. The three Flamingo gene orthologs in man and rodents are named, respectively, CELSR1–3 and Celsr1–3. Celsr1 and 2 are expressed during early development, in the brain and epithelia. In this report, we characterized further Celsr genes in the mouse, and examined their developmental pattern of expression. Each Celsr is expressed prominently in the developing brain following a specific pattern, suggesting that they serve distinct functions. q 2002 Elsevier Science Ireland Ltd. All rights reserved. Keywords: Brain development; Cerebral cortex; Cadherin; In situ hybridization; Genomic structure; Frizzled; Flamingo; G-protein coupled receptor 1. Results and discussion developing brain following a specific pattern, suggesting that they serve distinct functions. Celsr, also called Flamingo (Fmi) genes encode proteins The Celsr3 cDNA was reconstituted by alignment of the of the cadherin superfamily (Nollet et al., 2000; Redies, human CELSR3 cDNA with mouse genomic and expressed 2000; Takeichi et al., 2000; Tepass et al., 2000). Celsr sequence tag (EST) sequences, and verified by reverse tran- proteins have nine N-terminal cadherin repeats, followed scriptase polymerase chain reaction (RT-PCR) and sequen- by six EGF-like domains, seven putative transmembrane cing. Like its two homologs Celsr1 and 2 (Wu and Maniatis, segments and an intracellular C-terminus. The Drosophila 2000), it is encoded by 35 exons (Fig. 1). The first exon is Fmi gene regulates planar cell polarity and dendritic field longer than 4000 nucleotides (nt) and encodes the nine deployment (Chae et al., 1999; Usui et al., 1999; Gao et al., cadherin repeats. Other exons range in size from 79 to 2000). The three Flamingo gene orthologs in man and 1660 nt and are separated by small introns (range: 94– rodents are named, respectively, CELSR1–3 and Celsr1–3 1831). The three Celsr protein sequences are more than (Table 1; Hadjantonakis et al., 1997; Nakayama et al., 1998; 50% identical in their extracellular and transmembrane Usui et al., 1999; Vincent et al., 2000; Wu and Maniatis, segments but differ in their cytoplasmic portions. 2000). Celsr1 and 2 are expressed during early develop- At embryonic day 10 (E10, Fig. 2A–C), Celsr genes were ment, in the brain and epithelia (Hadjantonakis et al., expressed in the embryonic central nervous system (CNS), 1997; Formstone and Little, 2001). However, brain expres- in the emerging dorsal root ganglia (DRG) and cranial gang- sion patterns have not been studied in detail (Shima et al., lia, and to a lower level in epithelia. In the CNS, expression 2001). In this report, we characterized further Celsr genes in of the three genes was uniform along the rostrocaudal axis, the mouse, and examined their developmental pattern of but different in the radial dimension. Celsr1 mRNA was expression. Each Celsr is expressed prominently in the detected in ventricular zones (VZ) but not in marginal zones (MZ), and weakly in other structures. Celsr2 expres- sion was strong in the VZ in all sectors of the brain, and lower in the MZ. As also shown by Formstone and Little * Corresponding author. Tel.: 132-81-72-42-78; fax: 132-81-72-42-80. E-mail address: [email protected] (C. Lambert de Rouv- (2001), Celsr3 expression was almost complementary to roit). that of Celsr1, low in VZ but strong in MZ. At E12 (Fig. 1 Present address: Developmental Genetics Unit, UCL Medical School, 2D–F), Celsr1 was detected at high levels in the VZ in all B1200 Brussels, Belgium. 0925-4773/02/$ - see front matter q 2002 Elsevier Science Ireland Ltd. All rights reserved. PII: s0925-4773(01)00623-2 158 F. Tissir et al. / Mechanisms of Development 112 (2002) 157–160 Table 1 Nomenclature of Celsr genes Name Others, man Human map Mouse Mouse map Rat CELSR1 FMI2 Chr 22 Celsr1, Fmi2 Chr 15 CELSR2 EGFL2 Chr 1 Celsr2, Fmi1 Chr 3 MEGF3 CELSR3 MEGF2, EGFL1, FMI1 Chr 3 Celsr3 Chr 9 MEGF2 brain areas, and to some extent in epithelia. The signal was and incipient dentate gyrus, cerebellar cortex and pontine negligible in other organs. Celsr2 expression was strong in nuclei. Celsr3 was expressed at highest levels in differen- VZ and lower in MZ, except in the telencephalic MZ where tiating neuronal fields, particularly in the olfactory bulb, the it was prominent. The DRG and cranial ganglia expressed cerebral and hippocampal cortical plate, the external layer low amounts of Celsr2 mRNA, and there was also some of the tectum, pontine nuclei (not shown) and the external weak signal in epithelia, particularly in nasal cavities. granular layer of the cerebellum. At postnatal day 10 (P10, Celsr3 mRNA was expressed in a pattern almost comple- Fig. 2M–O), Celsr1 mRNA expression was weak and mentary to that of Celsr1, with highest levels in MZ, such as confined to germinative zones, namely the residual VZ in the cortical primordium (mainly the preplate) and weaker telencephalon and midbrain, and the external tiers of the signal in the VZ. Celsr3 was expressed in DRG and cranial cerebellar external granule cell layer. Celsr2 mRNA was ganglia. At E15 (Fig. 2G–I), Celsr1 was highly expressed in no longer detected in the VZ, but was found in high concen- the VZ in all brain areas, particularly in the telencephalon. tration in postmigratory fields. In the olfactory bulb, heavy No Celsr1 mRNA was detected in differentiating neuronal expression was associated with the granule cell layer. In the fields. Celsr1 signal was also present in epithelia, including cerebral cortex, high expression at the external and inter- the olfactory epithelium, in the developing lungs and kidney mediate levels was superposed to a diffuse moderate signal. cortex. Celsr2 expression remained prominent in the brain. A high signal was detected in the pyramidal cell layer of the The intensity was highest in all VZ. The signal was less hippocampus and in granule cells of the dentate gyrus. Inner intense in differentiating fields than in VZ, except in the and outer cerebellar granule cells were strongly positive. cerebral hemispheres, and to a lesser extent in the tectum Celsr3 mRNA was expressed in differentiating neuronal and cerebellum. In addition, there was strong Celsr2 expres- fields in all brain areas. There was strong signal in the sion in the kidney cortex, moderate signal in the skin, nasal olfactory bulb, in the cortical plate – with highest intensity pits and developing lungs. The Celsr3-related signal was in its superficial tiers –, in hippocampal pyramidal cells and restricted to the brain and to the olfactory epithelium. In in the dentate gyrus. Expression was high in the external and the brain, it was low in VZ but strong in external fields, inner granule cell layers of the cerebellum; in the external particularly those with ongoing migration, such as the tele- layer, it was associated with postmitotic cells of the inner ncephalic cortical plate, the olfactory bulb, the cerebellum tiers. At P21 (Fig. 2P–R), Celsr1 expression was detected in and the tectum. the remnants of the telencephalic VZ. Celsr2 expression In the newborn and postnatal stages, Celsr-related signals remained strong in pyramidal hippocampal neurons, granule were studied on brain sections. In the newborn (Fig. 2J–L), cells of the dentate gyrus, in the cerebral cortex, olfactory the expression of Celsr1 remained restricted to the VZ. bulb and basal forebrain. Celsr3 mRNA levels were much Celsr2 remained expressed in the VZ as well as in migrating lower than at previous stages, except in cerebellar granule and postmigratory cells throughout the brain. Expression cells and, to a lesser extent, in the dentate gyrus and olfac- was particularly high in the cortical plate, hippocampus tory bulb. Fig. 1. Genomic organization of the mouse Celsr3 gene. Exons are indicated by solid rectangles with the encoded protein shown below; the transcription start site was not mapped. The protein domains were defined used the Pfam database (Bateman et al., 2000). S, signal sequence; E, EGF-like motif; Lam, laminin G domain; LE, laminin-type EGF motif; H, domain present in hormone receptors; GPS, latrophilin-CL1-like G protein coupled receptor proteolytic site; 7TM, seven-pass transmembrane domain (secretin family); P, proline-rich region. Shaded rectangles represent protein domains displaying more than 50% identity with Celsr1 and Celsr2. The Celsr3 sequence has been submitted to Genbank (AF427498). F. Tissir et al. / Mechanisms of Development 112 (2002) 157–160 159 Fig. 2. In situ hybridization studies of Celsr 1–3 mRNA expression during mouse development. [P-33] labeled riboprobes were hybridized to cryostat sections, and the signal was revealed using X-ray films as described (Simmons et al., 1989; Bernier et al., 1999). Primers for probe preparations with RT-PCR were: (i) Celsr1:50-CCACCCCTGAAATCTGACC-30 and 50-CACTCTGTATCCTTGCCATCC-30 (amplifying nucleotides 10162–10608 of sequence GI6753407); (ii) Celsr2:50-TCATCTCTGTAGTGCGCCTG-30 and 50-ATCTCACCGTTCTCTCGTCG-30 (amplifying nucleotides 6506–7121 of sequence GI11995465) ; (iii) Celsr3:50-GCTTGGACACCAGCCTGTCTA-30 and 50 TTAACCCCCACCTGCATAGATGCGA-30 (amplifying nucleotides 8314–9138 of sequence AF427498). Figures are micrographs of autoradiography films. The signals for Celsr1, 2 and 3 are shown, respectively in the left, middle and right series of figures.
Recommended publications
  • Wnt Signaling in Vertebrate Neural Development and Function
    J Neuroimmune Pharmacol (2012) 7:774–787 DOI 10.1007/s11481-012-9404-x INVITED REVIEW Wnt Signaling in Vertebrate Neural Development and Function Kimberly A. Mulligan & Benjamin N. R. Cheyette Received: 18 June 2012 /Accepted: 10 September 2012 /Published online: 27 September 2012 # Springer Science+Business Media, LLC 2012 Abstract Members of the Wnt family of secreted signaling immature neurons migrate to populate different cortical proteins influence many aspects of neural development and layers, nuclei, and ganglia in the forebrain, midbrain, hind- function. Wnts are required from neural induction and axis brain, and spinal cord. Each mature neuron elaborates an formation to axon guidance and synapse development, and axon and numerous dendrites while forming hundreds to even help modulate synapse activity. Wnt proteins activate a thousands of synapses with other neurons, enabling electro- variety of downstream signaling pathways and can induce a chemical communication throughout the nervous system. similar variety of cellular responses, including gene tran- All these developmental processes must be coordinated to scription changes and cytoskeletal rearrangements. This re- ensure proper construction and function of the CNS, and view provides an introduction to Wnt signaling pathways this requires the coordinated developmental activity of a and discusses current research on their roles in vertebrate vast array of genes. neural development and function. Members of the Wnt family of secreted signaling proteins are implicated in every step of neural development men- Keywords Wnt signaling . Neural development . tioned above. Wnt proteins provide positional information CNS patterning . Axon guidance . Dendrite growth . within the embryo for anterior-posterior axis specification of Synapse formation .
    [Show full text]
  • Glial Insulin Regulates Cooperative Or Antagonistic Golden Goal/Flamingo
    RESEARCH ARTICLE Glial insulin regulates cooperative or antagonistic Golden goal/Flamingo interactions during photoreceptor axon guidance Hiroki Takechi1, Satoko Hakeda-Suzuki1*, Yohei Nitta2,3, Yuichi Ishiwata1, Riku Iwanaga1, Makoto Sato4,5, Atsushi Sugie2,3, Takashi Suzuki1* 1Graduate School of Life Science and Technology, Tokyo Institute of Technology, Yokohama, Japan; 2Center for Transdisciplinary Research, Niigata University, Niigata, Japan; 3Brain Research Institute, Niigata University, Niigata, Japan; 4Mathematical Neuroscience Unit, Institute for Frontier Science Initiative, Kanazawa University, Kanazawa, Japan; 5Laboratory of Developmental Neurobiology, Graduate School of Medical Sciences, Kanazawa University, Kanazawa, Japan Abstract Transmembrane protein Golden goal (Gogo) interacts with atypical cadherin Flamingo (Fmi) to direct R8 photoreceptor axons in the Drosophila visual system. However, the precise mechanisms underlying Gogo regulation during columnar- and layer-specific R8 axon targeting are unknown. Our studies demonstrated that the insulin secreted from surface and cortex glia switches the phosphorylation status of Gogo, thereby regulating its two distinct functions. Non- phosphorylated Gogo mediates the initial recognition of the glial protrusion in the center of the medulla column, whereas phosphorylated Gogo suppresses radial filopodia extension by counteracting Flamingo to maintain a one axon-to-one column ratio. Later, Gogo expression ceases during the midpupal stage, thus allowing R8 filopodia to extend vertically into the M3 layer. These *For correspondence: results demonstrate that the long- and short-range signaling between the glia and R8 axon growth [email protected] (SH-S); cones regulates growth cone dynamics in a stepwise manner, and thus shapes the entire [email protected] (TS) organization of the visual system. Competing interests: The authors declare that no competing interests exist.
    [Show full text]
  • Inaugural – Dissertation
    INAUGURAL – DISSERTATION zur Erlangung der Doktorwürde der Naturwissenschaftlich-Mathematischen Gesamtfakultät der Ruprecht - Karls - Universität Heidelberg vorgelegt von Diplom-Biochemikerin Nadine Stephanie Kirsch geboren in Heidelberg Tag der mündlichen Prüfung: ……………………………………………. Analysis of novel Wnt pathway components acting at the receptor level Gutachter: Prof. Dr. Christof Niehrs Prof. Dr. Thomas Holstein Table of Contents Table of Contents 1. Summary .......................................................................................................................... 1 2. Zusammenfassung ........................................................................................................... 2 3. Introduction ..................................................................................................................... 3 3.1 Wnt signaling transduction cascades ......................................................................... 3 3.1.1 Wnt/β-catenin signaling ...................................................................................... 4 3.1.2 Wnt/PCP signaling ............................................................................................... 6 3.2 Wnt/β-catenin signaling regulation at the receptor level ......................................... 8 3.2.1 Wnt receptors ...................................................................................................... 8 3.2.2 Extracellular modifiers ......................................................................................
    [Show full text]
  • A Role for Atypical Cadherincelsr3in Hippocampal Maturation And
    The Journal of Neuroscience, October 3, 2012 • 32(40):13729–13743 • 13729 Development/Plasticity/Repair A Role for Atypical Cadherin Celsr3 in Hippocampal Maturation and Connectivity Jia Feng,1 Ying Xu,1 Meizhi Wang,1 Yiwen Ruan,1 Kwok-Fai So,1,2 Fadel Tissir,3 Andre Goffinet,3 and Libing Zhou1 1Joint Laboratory for Brain Function and Health, Jinan University and the University of Hong Kong, Medical School of Jinan University, Guangzhou 510632, People’s Republic of China, 2Department of Anatomy, the University of Hong Kong, Pokfulam, Hong Kong SAR, People’s Republic of China, and 3Institute of Neuroscience, Universite´ Catholique de Louvain, B1200 Brussels, Belgium Atypical cadherin Celsr3, a regulator of planar cell polarity, is critical for the development of the axonal blueprint. We previously showed that expression of Celsr3 is necessary to establish forebrain connections such as the anterior commissure and thalamocortical and corticospinal tracts. The requirement for Celsr3 during hippocampal wiring and its action in the hippocampus remain largely unex- plored. Here, we compared the connectivity and maturation of the hippocampal formation in Celsr3͉Foxg1 and Celsr3͉Dlx mice. Celsr3 is inactivated in the whole telencephalon, including the hippocampal primordium, in Celsr3͉Foxg1 mice, and in the early basal telenceph- alon, including ganglionic eminences and ventral diencephalon, in Celsr3͉Dlx mice. Behavioral tests showed that both mutants were hyperactive and had impaired learning and memory. Abnormal cytoarchitecture of CA1, CA3, and dentate gyrus was found in the Celsr3͉Foxg1 mutant, in which afferent and efferent hippocampal pathways, as well as intrinsic connections, were dramatically disrupted. In Celsr3͉Dlx mutant mice, hippocampal cytoarchitecture was mildly affected and extrinsic and intrinsic connectivity moderately dis- turbed.
    [Show full text]
  • The Cytoplasmic LIM Domain Protein Espinas Contributes to Photoreceptor Layer Selection in the Visual System
    biology Article The Cytoplasmic LIM Domain Protein Espinas Contributes to Photoreceptor Layer Selection in the Visual System 1,2, 1,2, 1 Alejandra Fernández-Pineda y , Martí Monge-Asensio y , Martín Rios and Marta Morey 1,2,* 1 Departament de Genètica, Microbiologia i Estadística, Facultat de Biologia, Universitat de Barcelona, 08028 Barcelona, Spain; [email protected] (A.F.-P.); [email protected] (M.M.-A.); [email protected] (M.R.) 2 Institut de Biomedicina (IBUB), Universitat de Barcelona, 08028 Barcelona, Spain * Correspondence: [email protected] Equal contribution. y Received: 27 November 2020; Accepted: 12 December 2020; Published: 14 December 2020 Simple Summary: One of the central questions in neurobiology is how neurons discriminate between one another during circuit assembly. A common strategy of many nervous systems is the organization of brain regions in layers, to facilitate that neurons encounter a limited repertoire of synaptic partners. The fly visual system, which is structured in layers like many regions of the vertebrate brain, is used to identify cell surface molecules that mediate recognition between neurons and allow them to extend to specific layers. However, little is known about the intracellular pathways that link cell surface molecules to the cytoskeleton to determine whether or not to stabilize in a layer. Flamingo and its vertebrate homologs CELSR1/2 are cell surface molecules with widespread roles in neurite growth. In the fly visual system in particular, Flamingo regulates layer selection of a particular neuronal type. Our data suggests that in this context, Flamingo signals to the cytoskeleton through the conserved cytoplasmic molecule Espinas/PRICKLE2. Given that Flamingo and Espinas, as well as their respective vertebrate homologs, are broadly expressed in the nervous system, elucidating the interactions between them can reveal conserved mechanisms and provide valuable insights into the assembly of neural circuits.
    [Show full text]
  • 7 X 11.5 Long Title.P65
    Cambridge University Press 978-0-521-11208-6 - G Protein-Coupled Receptors: Structure, Signaling, and Physiology Edited by Sandra Siehler and Graeme Milligan Index More information Index Α 2A-adrenoceptor D1 receptor interactions, 93 activation kinetics, 148 time-limiting steps, 152–153 allosteric modulators, 257 TR-FRET analysis, 76–78, 84 effector systems, 152 Adenosine-A2, 257 function studies, 55–56 Adenosine-A2A receptor/G protein interaction, activation kinetics, 148, 149 149–150, 151 β/γ complex in adenylyl cyclase signal time-limiting steps, 152–153 modulation, 207–208 -1 adrenoceptors receptors dopamine receptor interactions, 93–94 allosteric modulators, 257 Golf mediation of, 131 cardiovascular regulation role, 291–292 in Parkinson’s disease, 335–338 TR-FRET analysis, 76–78 receptor/G protein interaction, 149–150 2-andrenoceptors receptors schizophrenia, D2R-A2AR heteromeric β 1-adrenoceptors receptor complexes in, 94 polymorphisms in heart failure, Adenylyl cyclases regulation 304–305 as assay, 235 conformational selection in, 275 crystal structures, 203 α 1B-adrenoceptor-G 11 function studies, expression patterns, 191–192, 203–204 57–58 GPCR interactions, direct, 205, 206, ABC294640, 392 217–218 ABC747080, 392 Gq/G11 family, 135–136 ABP688, 257, 260 group I, 195–196 AC-42, 257 group II, 196–197 Acebutol, 298 group III, 197–198 ACPD group IV, 198–199 1S,3R-ACPD, 339 Gz, 131 trans-ACPD, 327, 328 heterologous sensitization, 192, 199–202 in cognitive disorders, 346–348 history, 192–194 in epilepsy, 338, 339, 352–353, 354, isoforms,
    [Show full text]
  • Supplemental Table S1. Primers for Sybrgreen Quantitative RT-PCR Assays
    Supplemental Table S1. Primers for SYBRGreen quantitative RT-PCR assays. Gene Accession Primer Sequence Length Start Stop Tm GC% GAPDH NM_002046.3 GAPDH F TCCTGTTCGACAGTCAGCCGCA 22 39 60 60.43 59.09 GAPDH R GCGCCCAATACGACCAAATCCGT 23 150 128 60.12 56.52 Exon junction 131/132 (reverse primer) on template NM_002046.3 DNAH6 NM_001370.1 DNAH6 F GGGCCTGGTGCTGCTTTGATGA 22 4690 4711 59.66 59.09% DNAH6 R TAGAGAGCTTTGCCGCTTTGGCG 23 4797 4775 60.06 56.52% Exon junction 4790/4791 (reverse primer) on template NM_001370.1 DNAH7 NM_018897.2 DNAH7 F TGCTGCATGAGCGGGCGATTA 21 9973 9993 59.25 57.14% DNAH7 R AGGAAGCCATGTACAAAGGTTGGCA 25 10073 10049 58.85 48.00% Exon junction 9989/9990 (forward primer) on template NM_018897.2 DNAI1 NM_012144.2 DNAI1 F AACAGATGTGCCTGCAGCTGGG 22 673 694 59.67 59.09 DNAI1 R TCTCGATCCCGGACAGGGTTGT 22 822 801 59.07 59.09 Exon junction 814/815 (reverse primer) on template NM_012144.2 RPGRIP1L NM_015272.2 RPGRIP1L F TCCCAAGGTTTCACAAGAAGGCAGT 25 3118 3142 58.5 48.00% RPGRIP1L R TGCCAAGCTTTGTTCTGCAAGCTGA 25 3238 3214 60.06 48.00% Exon junction 3124/3125 (forward primer) on template NM_015272.2 Supplemental Table S2. Transcripts that differentiate IPF/UIP from controls at 5%FDR Fold- p-value Change Transcript Gene p-value p-value p-value (IPF/UIP (IPF/UIP Cluster ID RefSeq Symbol gene_assignment (Age) (Gender) (Smoking) vs. C) vs. C) NM_001178008 // CBS // cystathionine-beta- 8070632 NM_001178008 CBS synthase // 21q22.3 // 875 /// NM_0000 0.456642 0.314761 0.418564 4.83E-36 -2.23 NM_003013 // SFRP2 // secreted frizzled- 8103254 NM_003013
    [Show full text]
  • Targeted Molecular Profiling of Rare Olfactory Sensory Neurons Identifies
    RESEARCH ARTICLE Targeted molecular profiling of rare olfactory sensory neurons identifies fate, wiring, and functional determinants J Roman Arguello1,2,3‡, Liliane Abuin1‡, Jan Armida1†, Kaan Mika1†, Phing Chian Chai1, Richard Benton1* 1Center for Integrative Genomics Faculty of Biology and Medicine University of Lausanne, Lausanne, Switzerland; 2Department of Ecology and Evolution Faculty of Biology and Medicine University of Lausanne, Lausanne, Switzerland; 3Swiss Institute of Bioinformatics, Lausanne, Switzerland Abstract Determining the molecular properties of neurons is essential to understand their development, function and evolution. Using Targeted DamID (TaDa), we characterize RNA polymerase II occupancy and chromatin accessibility in selected Ionotropic receptor (Ir)-expressing olfactory sensory neurons in Drosophila. Although individual populations represent a minute fraction of cells, TaDa is sufficiently sensitive and specific to identify the expected receptor genes. Unique Ir expression is not consistently associated with differences in chromatin accessibility, but rather to distinct transcription factor profiles. Genes that are heterogeneously expressed across populations are enriched for neurodevelopmental factors, and we identify functions for the POU- domain protein Pdm3 as a genetic switch of Ir neuron fate, and the atypical cadherin Flamingo in segregation of neurons into discrete glomeruli. Together this study reveals the effectiveness of *For correspondence: TaDa in profiling rare neural populations, identifies new roles for a transcription factor and a [email protected] neuronal guidance molecule, and provides valuable datasets for future exploration. †These authors also contributed equally to this work ‡These authors also contributed equally to this work Introduction Competing interests: The Nervous systems are composed of vast numbers of neuron classes with specific structural and func- authors declare that no tional characteristics.
    [Show full text]
  • Supplementary Table 1
    Supplementary Table 1. 492 genes are unique to 0 h post-heat timepoint. The name, p-value, fold change, location and family of each gene are indicated. Genes were filtered for an absolute value log2 ration 1.5 and a significance value of p ≤ 0.05. Symbol p-value Log Gene Name Location Family Ratio ABCA13 1.87E-02 3.292 ATP-binding cassette, sub-family unknown transporter A (ABC1), member 13 ABCB1 1.93E-02 −1.819 ATP-binding cassette, sub-family Plasma transporter B (MDR/TAP), member 1 Membrane ABCC3 2.83E-02 2.016 ATP-binding cassette, sub-family Plasma transporter C (CFTR/MRP), member 3 Membrane ABHD6 7.79E-03 −2.717 abhydrolase domain containing 6 Cytoplasm enzyme ACAT1 4.10E-02 3.009 acetyl-CoA acetyltransferase 1 Cytoplasm enzyme ACBD4 2.66E-03 1.722 acyl-CoA binding domain unknown other containing 4 ACSL5 1.86E-02 −2.876 acyl-CoA synthetase long-chain Cytoplasm enzyme family member 5 ADAM23 3.33E-02 −3.008 ADAM metallopeptidase domain Plasma peptidase 23 Membrane ADAM29 5.58E-03 3.463 ADAM metallopeptidase domain Plasma peptidase 29 Membrane ADAMTS17 2.67E-04 3.051 ADAM metallopeptidase with Extracellular other thrombospondin type 1 motif, 17 Space ADCYAP1R1 1.20E-02 1.848 adenylate cyclase activating Plasma G-protein polypeptide 1 (pituitary) receptor Membrane coupled type I receptor ADH6 (includes 4.02E-02 −1.845 alcohol dehydrogenase 6 (class Cytoplasm enzyme EG:130) V) AHSA2 1.54E-04 −1.6 AHA1, activator of heat shock unknown other 90kDa protein ATPase homolog 2 (yeast) AK5 3.32E-02 1.658 adenylate kinase 5 Cytoplasm kinase AK7
    [Show full text]
  • Wiring Visual Systems: Common and Divergent Mechanisms and Principles
    Available online at www.sciencedirect.com ScienceDirect Wiring visual systems: common and divergent mechanisms and principles 1 2 Alex L Kolodkin and P Robin Hiesinger The study of visual systems has a rich history, leading to the upstream of RGCs in the vertebrate retina are comparable discovery and understanding of basic principles underlying the to brain neuropils downstream of R cells in the fly optic elaboration of neuronal connectivity. Recent work in model lobe (Figure 1B): the vertebrate retina outer plexiform organisms such as fly, fish and mouse has yielded a wealth of layer (OPL) to the fly lamina, and the inner plexiform new insights into visual system wiring. Here, we consider how layer (IPL) to the fly distal medulla [1]. These compar- axonal and dendritic patterning in columns and laminae isons make sense in terms of circuit connectivity and influence synaptic partner selection in these model organisms. function, but the actual structures and cell types are not We highlight similarities and differences among disparate visual analogous. For example, a subset of RGCs that are systems with the goal of identifying common and divergent intrinsically photosensitive reveal that RGCs may share principles for visual system wiring. evolutionary origins with invertebrate photoreceptor neu- rons [2,3]; vertebrates may have evolved modern retinal Addresses connectivity subsequent to development of the first pho- 1 The Solomon H. Snyder Department of Neuroscience and Howard tosensitive cells, while connectivity in the fly lamina and Hughes Medical Institute, The Johns Hopkins University School of medulla may have evolved independently and down- Medicine, Baltimore, MD 21205, USA 2 stream of retinal output (Figure 1A,B).
    [Show full text]
  • Strand Breaks for P53 Exon 6 and 8 Among Different Time Course of Folate Depletion Or Repletion in the Rectosigmoid Mucosa
    SUPPLEMENTAL FIGURE COLON p53 EXONIC STRAND BREAKS DURING FOLATE DEPLETION-REPLETION INTERVENTION Supplemental Figure Legend Strand breaks for p53 exon 6 and 8 among different time course of folate depletion or repletion in the rectosigmoid mucosa. The input of DNA was controlled by GAPDH. The data is shown as ΔCt after normalized to GAPDH. The higher ΔCt the more strand breaks. The P value is shown in the figure. SUPPLEMENT S1 Genes that were significantly UPREGULATED after folate intervention (by unadjusted paired t-test), list is sorted by P value Gene Symbol Nucleotide P VALUE Description OLFM4 NM_006418 0.0000 Homo sapiens differentially expressed in hematopoietic lineages (GW112) mRNA. FMR1NB NM_152578 0.0000 Homo sapiens hypothetical protein FLJ25736 (FLJ25736) mRNA. IFI6 NM_002038 0.0001 Homo sapiens interferon alpha-inducible protein (clone IFI-6-16) (G1P3) transcript variant 1 mRNA. Homo sapiens UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 15 GALNTL5 NM_145292 0.0001 (GALNT15) mRNA. STIM2 NM_020860 0.0001 Homo sapiens stromal interaction molecule 2 (STIM2) mRNA. ZNF645 NM_152577 0.0002 Homo sapiens hypothetical protein FLJ25735 (FLJ25735) mRNA. ATP12A NM_001676 0.0002 Homo sapiens ATPase H+/K+ transporting nongastric alpha polypeptide (ATP12A) mRNA. U1SNRNPBP NM_007020 0.0003 Homo sapiens U1-snRNP binding protein homolog (U1SNRNPBP) transcript variant 1 mRNA. RNF125 NM_017831 0.0004 Homo sapiens ring finger protein 125 (RNF125) mRNA. FMNL1 NM_005892 0.0004 Homo sapiens formin-like (FMNL) mRNA. ISG15 NM_005101 0.0005 Homo sapiens interferon alpha-inducible protein (clone IFI-15K) (G1P2) mRNA. SLC6A14 NM_007231 0.0005 Homo sapiens solute carrier family 6 (neurotransmitter transporter) member 14 (SLC6A14) mRNA.
    [Show full text]
  • Family-B G-Protein-Coupled Receptors
    Edinburgh Research Explorer Family-B G-protein-coupled receptors Citation for published version: Harmar, AJ 2001, 'Family-B G-protein-coupled receptors', Genome Biology, vol. 2, no. 12, 3013.1, pp. -. https://doi.org/10.1186/gb-2001-2-12-reviews3013 Digital Object Identifier (DOI): 10.1186/gb-2001-2-12-reviews3013 Link: Link to publication record in Edinburgh Research Explorer Document Version: Publisher's PDF, also known as Version of record Published In: Genome Biology Publisher Rights Statement: © 2001 BioMed Central Ltd General rights Copyright for the publications made accessible via the Edinburgh Research Explorer is retained by the author(s) and / or other copyright owners and it is a condition of accessing these publications that users recognise and abide by the legal requirements associated with these rights. Take down policy The University of Edinburgh has made every reasonable effort to ensure that Edinburgh Research Explorer content complies with UK legislation. If you believe that the public display of this file breaches copyright please contact [email protected] providing details, and we will remove access to the work immediately and investigate your claim. Download date: 28. Sep. 2021 http://genomebiology.com/2001/2/12/reviews/3013.1 Protein family review Family-B G-protein-coupled receptors comment Anthony J Harmar Address: Department of Neuroscience, University of Edinburgh, 1 George Square, Edinburgh EH8 9JZ, UK. E-mail: [email protected] Published: 23 November 2001 Genome Biology 2001, 2(12):reviews3013.1–3013.10
    [Show full text]