A Complete Compendium of Crystal Structures for the Human SEPT3 Subgroup Reveals Functional Plasticity at a Specific Septin Inte
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FK506-Binding Protein 12.6/1B, a Negative Regulator of [Ca2+], Rescues Memory and Restores Genomic Regulation in the Hippocampus of Aging Rats
This Accepted Manuscript has not been copyedited and formatted. The final version may differ from this version. A link to any extended data will be provided when the final version is posted online. Research Articles: Neurobiology of Disease FK506-Binding Protein 12.6/1b, a negative regulator of [Ca2+], rescues memory and restores genomic regulation in the hippocampus of aging rats John C. Gant1, Eric M. Blalock1, Kuey-Chu Chen1, Inga Kadish2, Olivier Thibault1, Nada M. Porter1 and Philip W. Landfield1 1Department of Pharmacology & Nutritional Sciences, University of Kentucky, Lexington, KY 40536 2Department of Cell, Developmental and Integrative Biology, University of Alabama at Birmingham, Birmingham, AL 35294 DOI: 10.1523/JNEUROSCI.2234-17.2017 Received: 7 August 2017 Revised: 10 October 2017 Accepted: 24 November 2017 Published: 18 December 2017 Author contributions: J.C.G. and P.W.L. designed research; J.C.G., E.M.B., K.-c.C., and I.K. performed research; J.C.G., E.M.B., K.-c.C., I.K., and P.W.L. analyzed data; J.C.G., E.M.B., O.T., N.M.P., and P.W.L. wrote the paper. Conflict of Interest: The authors declare no competing financial interests. NIH grants AG004542, AG033649, AG052050, AG037868 and McAlpine Foundation for Neuroscience Research Corresponding author: Philip W. Landfield, [email protected], Department of Pharmacology & Nutritional Sciences, University of Kentucky, 800 Rose Street, UKMC MS 307, Lexington, KY 40536 Cite as: J. Neurosci ; 10.1523/JNEUROSCI.2234-17.2017 Alerts: Sign up at www.jneurosci.org/cgi/alerts to receive customized email alerts when the fully formatted version of this article is published. -
Dissection of Molecular Assembly Dynamics by Tracking Orientation
Dissection of molecular assembly dynamics by tracking PNAS PLUS orientation and position of single molecules in live cells Shalin B. Mehtaa,1, Molly McQuilkenb,c, Patrick J. La Riviered, Patricia Occhipintib,c, Amitabh Vermaa, Rudolf Oldenbourga,e, Amy S. Gladfeltera,b,c, and Tomomi Tania,2 aEugene Bell Center for Regenerative Biology and Tissue Engineering, Marine Biological Laboratory, Woods Hole, MA 02543; bDepartment of Biological Sciences, Dartmouth College, Hanover, NH 03755; cDepartment of Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599; dDepartment of Radiology, University of Chicago, Chicago, IL 60637; and ePhysics Department, Brown University, Providence, RI 02912 Edited by Jennifer Lippincott-Schwartz, National Institutes of Health, Bethesda, MD, and approved August 19, 2016 (received for review May 12, 2016) Regulation of order, such as orientation and conformation, drives excitation (3–5, 14–18) or polarization-resolved detection (1, 2, 19– the function of most molecular assemblies in living cells but 21) has allowed measurement of orientations of fluorophores. remains difficult to measure accurately through space and time. For fluorescent assemblies that exhibit simple geometries, such We built an instantaneous fluorescence polarization microscope, as planar (3), spherical (2), or cylindrical (19) shapes, two or- which simultaneously images position and orientation of fluorophores thogonal polarization-resolved measurements suffice to retrieve in living cells with single-molecule sensitivity and a time resolution fluorophore orientations relative to these geometries. However, of 100 ms. We developed image acquisition and analysis methods unbiased measurement of dipole orientation in a complex as- to track single particles that interact with higher-order assemblies sembly requires exciting or analyzing the fluorescent dipoles using of molecules. -
Anti-SEPT7 Antibody (ARG55299)
Product datasheet [email protected] ARG55299 Package: 100 μl anti-SEPT7 antibody Store at: -20°C Summary Product Description Rabbit Polyclonal antibody recognizes 7-Sep Tested Reactivity Hu, Ms, Rat Tested Application ICC/IF, WB Host Rabbit Clonality Polyclonal Isotype IgG Target Name SEPT7 Antigen Species Human Immunogen Recombinant protein of Human SEPT7 Conjugation Un-conjugated Alternate Names Septin-7; CDC10; CDC10 protein homolog; NBLA02942; SEPT7A; CDC3 Application Instructions Application table Application Dilution ICC/IF 1:50 - 1:100 WB 1:500 - 1:2000 Application Note * The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist. Positive Control HepG2 Calculated Mw 51 kDa Properties Form Liquid Purification Affinity purification with immunogen. Buffer PBS (pH 7.3), 0.02% Sodium azide and 50% Glycerol Preservative 0.02% Sodium azide Stabilizer 50% Glycerol Storage instruction For continuous use, store undiluted antibody at 2-8°C for up to a week. For long-term storage, aliquot and store at -20°C. Storage in frost free freezers is not recommended. Avoid repeated freeze/thaw cycles. Suggest spin the vial prior to opening. The antibody solution should be gently mixed before use. Note For laboratory research only, not for drug, diagnostic or other use. www.arigobio.com 1/2 Bioinformation Gene Symbol 42254 Gene Full Name septin 7 Background This gene encodes a protein that is highly similar to the CDC10 protein of Saccharomyces cerevisiae. The protein also shares similarity with Diff 6 of Drosophila and with H5 of mouse. Each of these similar proteins, including the yeast CDC10, contains a GTP-binding motif. -
Protein Kinase A-Mediated Septin7 Phosphorylation Disrupts Septin Filaments and Ciliogenesis
cells Article Protein Kinase A-Mediated Septin7 Phosphorylation Disrupts Septin Filaments and Ciliogenesis Han-Yu Wang 1,2, Chun-Hsiang Lin 1, Yi-Ru Shen 1, Ting-Yu Chen 2,3, Chia-Yih Wang 2,3,* and Pao-Lin Kuo 1,2,4,* 1 Department of Obstetrics and Gynecology, College of Medicine, National Cheng Kung University, Tainan 701, Taiwan; [email protected] (H.-Y.W.); [email protected] (C.-H.L.); [email protected] (Y.-R.S.) 2 Institute of Basic Medical Sciences, College of Medicine, National Cheng Kung University, Tainan 701, Taiwan; [email protected] 3 Department of Cell Biology and Anatomy, College of Medicine, National Cheng Kung University, Tainan 701, Taiwan 4 Department of Obstetrics and Gynecology, National Cheng-Kung University Hospital, Tainan 704, Taiwan * Correspondence: [email protected] (C.-Y.W.); [email protected] (P.-L.K.); Tel.: +886-6-2353535 (ext. 5338); (C.-Y.W.)+886-6-2353535 (ext. 5262) (P.-L.K.) Abstract: Septins are GTP-binding proteins that form heteromeric filaments for proper cell growth and migration. Among the septins, septin7 (SEPT7) is an important component of all septin filaments. Here we show that protein kinase A (PKA) phosphorylates SEPT7 at Thr197, thus disrupting septin filament dynamics and ciliogenesis. The Thr197 residue of SEPT7, a PKA phosphorylating site, was conserved among different species. Treatment with cAMP or overexpression of PKA catalytic subunit (PKACA2) induced SEPT7 phosphorylation, followed by disruption of septin filament formation. Constitutive phosphorylation of SEPT7 at Thr197 reduced SEPT7-SEPT7 interaction, but did not affect SEPT7-SEPT6-SEPT2 or SEPT4 interaction. -
Myopia in African Americans Is Significantly Linked to Chromosome 7P15.2-14.2
Genetics Myopia in African Americans Is Significantly Linked to Chromosome 7p15.2-14.2 Claire L. Simpson,1,2,* Anthony M. Musolf,2,* Roberto Y. Cordero,1 Jennifer B. Cordero,1 Laura Portas,2 Federico Murgia,2 Deyana D. Lewis,2 Candace D. Middlebrooks,2 Elise B. Ciner,3 Joan E. Bailey-Wilson,1,† and Dwight Stambolian4,† 1Department of Genetics, Genomics and Informatics and Department of Ophthalmology, University of Tennessee Health Science Center, Memphis, Tennessee, United States 2Computational and Statistical Genomics Branch, National Human Genome Research Institute, National Institutes of Health, Baltimore, Maryland, United States 3The Pennsylvania College of Optometry at Salus University, Elkins Park, Pennsylvania, United States 4Department of Ophthalmology, University of Pennsylvania, Philadelphia, Pennsylvania, United States Correspondence: Joan E. PURPOSE. The purpose of this study was to perform genetic linkage analysis and associ- Bailey-Wilson, NIH/NHGRI, 333 ation analysis on exome genotyping from highly aggregated African American families Cassell Drive, Suite 1200, Baltimore, with nonpathogenic myopia. African Americans are a particularly understudied popula- MD 21131, USA; tion with respect to myopia. [email protected]. METHODS. One hundred six African American families from the Philadelphia area with a CLS and AMM contributed equally to family history of myopia were genotyped using an Illumina ExomePlus array and merged this work and should be considered co-first authors. with previous microsatellite data. Myopia was initially measured in mean spherical equiv- JEB-W and DS contributed equally alent (MSE) and converted to a binary phenotype where individuals were identified as to this work and should be affected, unaffected, or unknown. -
Development and Applications of Superfolder and Split Fluorescent Protein Detection Systems in Biology
International Journal of Molecular Sciences Review Development and Applications of Superfolder and Split Fluorescent Protein Detection Systems in Biology Jean-Denis Pedelacq 1,* and Stéphanie Cabantous 2,* 1 Institut de Pharmacologie et de Biologie Structurale, IPBS, Université de Toulouse, CNRS, UPS, 31077 Toulouse, France 2 Centre de Recherche en Cancérologie de Toulouse (CRCT), Inserm, Université Paul Sabatier-Toulouse III, CNRS, 31037 Toulouse, France * Correspondence: [email protected] (J.-D.P.); [email protected] (S.C.) Received: 15 June 2019; Accepted: 8 July 2019; Published: 15 July 2019 Abstract: Molecular engineering of the green fluorescent protein (GFP) into a robust and stable variant named Superfolder GFP (sfGFP) has revolutionized the field of biosensor development and the use of fluorescent markers in diverse area of biology. sfGFP-based self-associating bipartite split-FP systems have been widely exploited to monitor soluble expression in vitro, localization, and trafficking of proteins in cellulo. A more recent class of split-FP variants, named « tripartite » split-FP,that rely on the self-assembly of three GFP fragments, is particularly well suited for the detection of protein–protein interactions. In this review, we describe the different steps and evolutions that have led to the diversification of superfolder and split-FP reporter systems, and we report an update of their applications in various areas of biology, from structural biology to cell biology. Keywords: fluorescent protein; superfolder; split-GFP; bipartite; tripartite; folding; PPI 1. Superfolder Fluorescent Proteins: Progenitor of Split Fluorescent Protein (FP) Systems Previously described mutations that improve the physical properties and expression of green fluorescent protein (GFP) color variants in the host organism have already been the subject of several reviews [1–4] and will not be described here. -
Proteomic Profiling of the Oncogenic Septin 9 Reveals Isoform-Specific
bioRxiv preprint doi: https://doi.org/10.1101/566513; this version posted March 5, 2019. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. Proteomic profiling of the oncogenic septin 9 reveals isoform-specific interactions in breast cancer cells Louis Devlina,b, George Perkinsb, Jonathan R. Bowena, Cristina Montagnac and Elias T. Spiliotisa* aDepartment of Biology, Drexel University, Philadelphia, PA 19095, USA bSanofi Pasteur, Swiftwater, PA 18370, USA cDepartments of Genetics and Pathology, Albert Einstein College of Medicine, Yeshiva University, Bronx, NY 10461, USA *Corresponding author: Elias T. Spiliotis, Department of Biology, Drexel University, PISB 423, 3245 Chestnut St, Philadelphia, PA 19104, USA E-mail: [email protected] Phone: 215-571-3552 Fax: 215-895-1273 Key words: septins, SEPT9 isoforms, breast cancer, septin interactome 1 bioRxiv preprint doi: https://doi.org/10.1101/566513; this version posted March 5, 2019. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. Abstract Septins are a family of multimeric GTP-binding proteins, which are abnormally expressed in cancer. Septin 9 (SEPT9) is an essential and ubiquitously expressed septin with multiple isoforms, which have differential expression patterns and effects in breast cancer cells. It is unknown, however, if SEPT9 isoforms associate with different molecular networks and functions. Here, we performed a proteomic screen in MCF-7 breast cancer cells to identify the interactome of GFP-SEPT9 isoforms 1, 4 and 5, which vary significantly in their N-terminal extensions. -
The Requirement of SEPT2 and SEPT7 for Migration and Invasion in Human Breast Cancer Via MEK/ERK Activation
www.impactjournals.com/oncotarget/ Oncotarget, Vol. 7, No. 38 Research Paper The requirement of SEPT2 and SEPT7 for migration and invasion in human breast cancer via MEK/ERK activation Nianzhu Zhang1,*, Lu Liu2,*, Ning Fan2, Qian Zhang1, Weijie Wang1, Mingnan Zheng3, Lingfei Ma4, Yan Li2, Lei Shi1,5 1Institute of Cancer Stem Cell, Cancer Center, Dalian Medical University, Dalian, 116044, Liaoning, P.R.China 2College of Basic Medical Sciences, Dalian Medical University, Dalian, 116044 Liaoning, P.R.China 3Department of Gynecology and Obstetrics, Dalian Municipal Central Hospital Affiliated to Dalian Medical University, Dalian, 116033, Liaoning, P.R.China 4The First Affiliated Hospital of Dalian Medical University, Dalian, 116011, Liaoning, P.R.China 5State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, 201203, P.R.China *These authors contributed equally to this work Correspondence to: Lei Shi, email: [email protected] Yan Li, email: [email protected] Lingfei Ma, email: [email protected] Keywords: septin, forchlorfenuron, breast cancer, invasion, MAPK Received: April 24, 2016 Accepted: July 28, 2016 Published: August 19, 2016 ABSTRACT Septins are a novel class of GTP-binding cytoskeletal proteins evolutionarily conserved from yeast to mammals and have now been found to play a contributing role in a broad range of tumor types. However, their functional importance in breast cancer remains largely unclear. Here, we demonstrated that pharmaceutical inhibition of global septin dynamics would greatly suppress proliferation, migration and invasiveness in breast cancer cell lines. We then examined the expression and subcellular distribution of the selected septins SEPT2 and SEPT7 in breast cancer cells, revealing a rather variable localization of the two proteins with cell cycle progression. -
Bioinformatics Analysis for the Identification of Differentially Expressed Genes and Related Signaling Pathways in H
Bioinformatics analysis for the identification of differentially expressed genes and related signaling pathways in H. pylori-CagA transfected gastric cancer cells Dingyu Chen*, Chao Li, Yan Zhao, Jianjiang Zhou, Qinrong Wang and Yuan Xie* Key Laboratory of Endemic and Ethnic Diseases , Ministry of Education, Guizhou Medical University, Guiyang, China * These authors contributed equally to this work. ABSTRACT Aim. Helicobacter pylori cytotoxin-associated protein A (CagA) is an important vir- ulence factor known to induce gastric cancer development. However, the cause and the underlying molecular events of CagA induction remain unclear. Here, we applied integrated bioinformatics to identify the key genes involved in the process of CagA- induced gastric epithelial cell inflammation and can ceration to comprehend the potential molecular mechanisms involved. Materials and Methods. AGS cells were transected with pcDNA3.1 and pcDNA3.1::CagA for 24 h. The transfected cells were subjected to transcriptome sequencing to obtain the expressed genes. Differentially expressed genes (DEG) with adjusted P value < 0.05, | logFC |> 2 were screened, and the R package was applied for gene ontology (GO) enrichment and the Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway analysis. The differential gene protein–protein interaction (PPI) network was constructed using the STRING Cytoscape application, which conducted visual analysis to create the key function networks and identify the key genes. Next, the Submitted 20 August 2020 Kaplan–Meier plotter survival analysis tool was employed to analyze the survival of the Accepted 11 March 2021 key genes derived from the PPI network. Further analysis of the key gene expressions Published 15 April 2021 in gastric cancer and normal tissues were performed based on The Cancer Genome Corresponding author Atlas (TCGA) database and RT-qPCR verification. -
Actin, Microtubule, Septin and ESCRT Filament Remodeling During Late Steps of Cytokinesis Cyril Addi, Jian Bai, Arnaud Echard
Actin, microtubule, septin and ESCRT filament remodeling during late steps of cytokinesis Cyril Addi, Jian Bai, Arnaud Echard To cite this version: Cyril Addi, Jian Bai, Arnaud Echard. Actin, microtubule, septin and ESCRT filament remodel- ing during late steps of cytokinesis. Current Opinion in Cell Biology, Elsevier, 2018, 50, pp.27-34. 10.1016/j.ceb.2018.01.007. hal-02114062 HAL Id: hal-02114062 https://hal.archives-ouvertes.fr/hal-02114062 Submitted on 29 Apr 2019 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. Distributed under a Creative Commons Attribution - NonCommercial| 4.0 International License Actin, microtubule, septin and ESCRT filament remodeling during late steps of cytokinesis Cyril Addi1,2,3,#, Jian Bai1,2,3,# and Arnaud Echard1,2 1 Membrane Traffic and Cell Division Lab, Cell Biology and Infection department Institut Pasteur, 25–28 rue du Dr Roux, 75724 Paris cedex 15, France 2 Centre National de la Recherche Scientifique CNRS UMR3691, 75015 Paris, France 3 Sorbonne Universités, Université Pierre et Marie Curie, Université Paris 06, Institut de formation doctorale, 75252 Paris, France # equal contribution, alphabetical order correspondence: [email protected] 1 ABSTRACT Cytokinesis is the process by which a mother cell is physically cleaved into two daughter cells. -
Septins Are Involved at the Early Stages of Macroautophagy in S
© 2018. Published by The Company of Biologists Ltd | Journal of Cell Science (2018) 131, jcs209098. doi:10.1242/jcs.209098 RESEARCH ARTICLE Septins are involved at the early stages of macroautophagy in S. cerevisiae Gaurav Barve1, Shreyas Sridhar1, Amol Aher1, Mayurbhai H. Sahani1, Sarika Chinchwadkar1, Sunaina Singh1, Lakshmeesha K. N.1, Michael A. McMurray2 and Ravi Manjithaya1,* ABSTRACT blocks, such as amino acids, back to the cytoplasm. The biogenesis Autophagy is a conserved cellular degradation pathway wherein of autophagosomes remains incompletely understood. double-membrane vesicles called autophagosomes capture long-lived In budding yeast cells, the site of autophagosome formation proteins, and damaged or superfluous organelles, and deliver them to is known as the pre-autophagosomal structure (PAS) and is the lysosome for degradation. Septins are conserved GTP-binding perivacuolarly located. Recent work has shown that the PAS proteins involved in many cellular processes, including phagocytosis is tethered to endoplasmic reticulum (ER) exit sites where multiple and the autophagy of intracellular bacteria, but no role in general autophagy proteins colocalize in a hierarchical sequence (Graef autophagy was known. In budding yeast, septins polymerize into ring- et al., 2013; Suzuki et al., 2007). The membrane source for the shaped arrays of filaments required for cytokinesis. In an unbiased developing autophagosome is contributed by the trafficking of Atg9 – – – – genetic screen and in subsequent targeted analysis, we found along with its transport complex (Atg1 Atg11 Atg13 Atg23 – – – autophagy defects in septin mutants. Upon autophagy induction, Atg27 Atg2 Atg18 TRAPIII) to help build the initial cup-shaped pre-assembled septin complexes relocalized to the pre- structure, the phagophore (Legakis et al., 2007; Reggiori et al., 2004; – – autophagosomal structure (PAS) where they formed non-canonical Tucker et al., 2003). -
1 Septin Roles and Mechanisms in Organization Of
bioRxiv preprint doi: https://doi.org/10.1101/2020.03.04.977199; this version posted March 5, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. Septin Roles and Mechanisms in Organization of Endothelial Cell Junctions Authors: Joanna Kim, Ph.D.* and John A. Cooper, M.D., Ph.D.* Department of Biochemistry & Molecular Biophysics* Washington University School of Medicine, Saint Louis, MO, USA. Corresponding author: John A. Cooper Campus Box 8231 660 S. Euclid Ave. Saint Louis, MO 63110-1093 E-mail: [email protected] Phone: (314) 362-3964 Fax: (314) 362-7183 Short title: Septin and endothelial cell junctions Abstract Septins play an important role in regulating the barrier function of the endothelial monolayer of the microvasculature. Depletion of septin 2 protein alters the organization of vascular endothelial (VE)-cadherin at cell-cell adherens junctions as well as the dynamics of membrane protrusions at endothelial cell-cell contact sites. Here, we report the discovery that localization of septin 2 at endothelial cell junctions is important for the distribution of a number of other junctional molecules. We also found that treatment of microvascular endothelial cells with the inflammatory mediator TNF-a led to sequestration of septin 2 away from cell junctions and into the cytoplasm, without an effect on the overall level of septin 2 protein. Interestingly, TNF-a treatment of endothelial monolayers produced effects similar to those of depletion of septin 2 on various molecular components of adherens junctions (AJs) and tight 1 bioRxiv preprint doi: https://doi.org/10.1101/2020.03.04.977199; this version posted March 5, 2020.