Dap-1626 Goat Anti-SEPT2 Antibody-PDF.Pdf

Total Page:16

File Type:pdf, Size:1020Kb

Dap-1626 Goat Anti-SEPT2 Antibody-PDF.Pdf DATA SHEET Goat anti-SEPT2 Antibody Item Number dAP-1626 Target Molecule Principle Name: SEPT2; Official Symbol: SEPT2; All Names and Symbols: SEPT2; septin 2; DIFF6; KI- AA0158; NEDD5; Pnutl3; hNedd5; neural precursor cell expressed, developmentally down-regulated 5; Accession Number (s): NP_001008491.1; Human Gene ID(s): 4735; Non-Human GeneID(s): 18000 (mouse) 117515 (rat) Immunogen SKQQPTQFINPET, is from N terminus Reported variants represent identical protein: NP_001008492.1, NP_006146.1, NP_004395.1, NP_001008491.1. Applications Pep ELISA, WB, IHC Species Tested: Human Purification Purified from goat serum by ammonium sulphate precipitation followed by antigen affinity chromatography using the immunizing peptide. Supplied As lyophilized powder of 50ug or 100ug IgG; Reconsititute IgG with 100ul or 200ul sterile DI Water and final product will be formulated as 0.5 mg/ml in Tris saline, 0.02% sodium azide, pH7.3 with 0.5% bovine serum albumin. Aliquot and store at -20°C. Minimize freezing and thawing. Peptide ELISA Peptide ELISA: antibody detection limit dilution 1 to 32000. Western Blot Western Blot: Approx. 40kDa band observed in Human Testis lysates (calculated MW of 41.5kDa accord- ing to NP_001008491.1). Recommended concentration: 0.05-0.2µg/ml. Primary incubation was 1 hour. IHC Immunohistochemistry: Paraffin embedded Human Breast, Tonsil and Brain (Cortex). Recommended con- centration: 2.5µg/ml. Reference Reference(s): Kremer BE, Adang LA, Macara IG. Septins regulate actin organization and cell-cycle arrest through nuclear accumulation of NCK mediated by SOCS7. Cell. 2007 Sep 7;130(5):837-50..PMID: 17803907-> Optimal dilutions should be determined by each laboratory for each application. The listed dilutions are for recommendation only and the final condi- tions should be optimized by the ender users! This product is sold for Research Use Only Angio-Proteomie | 11 Park Drive, Suite 12 Boston, MA 02215, USA | Tel: 001‐617‐549‐2665 | Fax: 001‐480‐247‐4337 | Email: [email protected] .
Recommended publications
  • Atherosclerosis-Susceptible and Atherosclerosis-Resistant Pigeon Aortic Cells Express Different Genes in Vivo
    University of New Hampshire University of New Hampshire Scholars' Repository New Hampshire Agricultural Experiment Station Publications New Hampshire Agricultural Experiment Station 7-1-2013 Atherosclerosis-susceptible and atherosclerosis-resistant pigeon aortic cells express different genes in vivo Janet L. Anderson University of New Hampshire, [email protected] C. M. Ashwell University of New Hampshire - Main Campus S. C. Smith University of New Hampshire - Main Campus R. Shine University of New Hampshire - Main Campus E. C. Smith University of New Hampshire - Main Campus See next page for additional authors Follow this and additional works at: https://scholars.unh.edu/nhaes Part of the Poultry or Avian Science Commons Recommended Citation J. L. Anderson, C. M. Ashwell, S. C. Smith, R. Shine, E. C. Smith and R. L. Taylor, Jr. Atherosclerosis- susceptible and atherosclerosis-resistant pigeon aortic cells express different genes in vivo Poultry Science (2013) 92 (10): 2668-2680 doi:10.3382/ps.2013-03306 This Article is brought to you for free and open access by the New Hampshire Agricultural Experiment Station at University of New Hampshire Scholars' Repository. It has been accepted for inclusion in New Hampshire Agricultural Experiment Station Publications by an authorized administrator of University of New Hampshire Scholars' Repository. For more information, please contact [email protected]. Authors Janet L. Anderson, C. M. Ashwell, S. C. Smith, R. Shine, E. C. Smith, and Robert L. Taylor Jr. This article is available at University of New Hampshire Scholars' Repository: https://scholars.unh.edu/nhaes/207 Atherosclerosis-susceptible and atherosclerosis-resistant pigeon aortic cells express different genes in vivo J.
    [Show full text]
  • 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.
    [Show full text]
  • 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.
    [Show full text]
  • Supplementary Table 1
    Supplementary Table 1. Large-scale quantitative phosphoproteomic profiling was performed on paired vehicle- and hormone-treated mTAL-enriched suspensions (n=3). A total of 654 unique phosphopeptides corresponding to 374 unique phosphoproteins were identified. The peptide sequence, phosphorylation site(s), and the corresponding protein name, gene symbol, and RefSeq Accession number are reported for each phosphopeptide identified in any one of three experimental pairs. For those 414 phosphopeptides that could be quantified in all three experimental pairs, the mean Hormone:Vehicle abundance ratio and corresponding standard error are also reported. Peptide Sequence column: * = phosphorylated residue Site(s) column: ^ = ambiguously assigned phosphorylation site Log2(H/V) Mean and SE columns: H = hormone-treated, V = vehicle-treated, n/a = peptide not observable in all 3 experimental pairs Sig. column: * = significantly changed Log 2(H/V), p<0.05 Log (H/V) Log (H/V) # Gene Symbol Protein Name Refseq Accession Peptide Sequence Site(s) 2 2 Sig. Mean SE 1 Aak1 AP2-associated protein kinase 1 NP_001166921 VGSLT*PPSS*PK T622^, S626^ 0.24 0.95 PREDICTED: ATP-binding cassette, sub-family A 2 Abca12 (ABC1), member 12 XP_237242 GLVQVLS*FFSQVQQQR S251^ 1.24 2.13 3 Abcc10 multidrug resistance-associated protein 7 NP_001101671 LMT*ELLS*GIRVLK T464, S468 -2.68 2.48 4 Abcf1 ATP-binding cassette sub-family F member 1 NP_001103353 QLSVPAS*DEEDEVPVPVPR S109 n/a n/a 5 Ablim1 actin-binding LIM protein 1 NP_001037859 PGSSIPGS*PGHTIYAK S51 -3.55 1.81 6 Ablim1 actin-binding
    [Show full text]
  • The Role of Sept2 on Neuronal Development
    THE ROLE OF SEPT2 ON NEURONAL DEVELOPMENT by HYUN JONG KIM A Dissertation submitted to the Graduate School-New Brunswick Rutgers, The State University of New Jersey and The Graduate School of Biomedical Sciences University of Medicine and Dentistry of New Jersey in partial fulfillment of the requirements for the degree of Doctor of Philosophy Graduate Program in Cell and Developmental Biology written under the direction of Shu Chan Hsu, Ph. D and approved by ________________________ ________________________ ________________________ ________________________ ________________________ New Brunswick, New Jersey May, 2009 ABSTRACT THE ROLE OF SEPT2 ON NEURONAL DEVELOPMENT By HYUN JONG KIM Dissertation Director: Shu Chan Hsu, Ph D Septins constitute a family of evolutionarily conserved proteins that were first discovered for their involvement in cell division. Recently, they are also found to be increasingly important in various neurodegenerative states, such as Parkinson’s and Alzheimer’s diseases. Molecular mechanisms underlying the function of septin proteins in the nervous system, however, remain largely unknown. Work from this thesis revealed that a member of the septin family, SEPT2, is important for exocytosis underlying neurite outgrowth in PC12 cells. SEPT2 has a similar tissue distribution and developmental expression profile as that of sec15, a subunit of the exocyst complex which has been found to be required for exocytosis. In undifferentiated PC12 cells, SEPT2 exhibited perinuclear enrichment, as observed for exocyst subunits. Upon neuronal differentiation, SEPT2, like exocyst subunits, redistributes from its perinuclear enrichment to the neurites and the growth cones. Knockdown of SEPT2 disrupted the perinuclear enrichment of exocyst subunits, decreased the protein levels of exocyst subunits.
    [Show full text]
  • The Human Gene Connectome As a Map of Short Cuts for Morbid Allele Discovery
    The human gene connectome as a map of short cuts for morbid allele discovery Yuval Itana,1, Shen-Ying Zhanga,b, Guillaume Vogta,b, Avinash Abhyankara, Melina Hermana, Patrick Nitschkec, Dror Friedd, Lluis Quintana-Murcie, Laurent Abela,b, and Jean-Laurent Casanovaa,b,f aSt. Giles Laboratory of Human Genetics of Infectious Diseases, Rockefeller Branch, The Rockefeller University, New York, NY 10065; bLaboratory of Human Genetics of Infectious Diseases, Necker Branch, Paris Descartes University, Institut National de la Santé et de la Recherche Médicale U980, Necker Medical School, 75015 Paris, France; cPlateforme Bioinformatique, Université Paris Descartes, 75116 Paris, France; dDepartment of Computer Science, Ben-Gurion University of the Negev, Beer-Sheva 84105, Israel; eUnit of Human Evolutionary Genetics, Centre National de la Recherche Scientifique, Unité de Recherche Associée 3012, Institut Pasteur, F-75015 Paris, France; and fPediatric Immunology-Hematology Unit, Necker Hospital for Sick Children, 75015 Paris, France Edited* by Bruce Beutler, University of Texas Southwestern Medical Center, Dallas, TX, and approved February 15, 2013 (received for review October 19, 2012) High-throughput genomic data reveal thousands of gene variants to detect a single mutated gene, with the other polymorphic genes per patient, and it is often difficult to determine which of these being of less interest. This goes some way to explaining why, variants underlies disease in a given individual. However, at the despite the abundance of NGS data, the discovery of disease- population level, there may be some degree of phenotypic homo- causing alleles from such data remains somewhat limited. geneity, with alterations of specific physiological pathways under- We developed the human gene connectome (HGC) to over- come this problem.
    [Show full text]
  • A Homozygous Genome-Edited Sept2-EGFP Fibroblast Cell Line
    bioRxiv preprint doi: https://doi.org/10.1101/570622; this version posted March 7, 2019. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC-ND 4.0 International license. A homozygous genome-edited Sept2-EGFP fibroblast cell line Monika Banko2,3, Iwona Mucha-Kruczynska1,2, Christoph Weise1, Florian Heyd1 and Helge Ewers1,2,3* 1Institut für Chemie und Biochemie, Freie Universität Berlin, Thielallee 63, 14195 Berlin, Germany 2Randall Divison of Cell and Molecular Biophysics, King’s College London, London SE1 1UL, United Kingdom 3Institut für Biochemie, ETH Zürich, Switzerland *Corresponding author: Helge Ewers Institut für Biochemie Freie Universität Berlin Thielallee 63 14195 Berlin Germany Tel: +49 30 838 60644 Email: [email protected] Running Head: Genome-edited Sept2-EGFP cell line 1 bioRxiv preprint doi: https://doi.org/10.1101/570622; this version posted March 7, 2019. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC-ND 4.0 International license. Abstract Septins are a conserved, essential family of GTPases that interact with actin, microtubules and membranes and form scaffolds and diffusion barriers in cells. Several of the 13 known mammalian septins assemble into nonpolar, multimeric complexes that can further polymerize into filamentous structures. While some GFP-coupled septins have been described, overexpression of GFP-tagged septins often leads to artifacts in localization and function.
    [Show full text]
  • Septins Guide Microtubules
    RESEARCH HIGHLIGHTS Akt-ing to control lipid LTsc1KO hepatocytes with constitutively active grew. Knockdown of SEPT2 resulted in a loss metabolism Akt2, and showed that in hepatocytes Akt2 of microtubule directionality and the microtu- represses INSIG2, an inhibitor of SREBP1c bules ended up becoming entangled. Further- The liver responds to insulin by blocking gluco- induction. These data uncover an mTORC1- more, SEPT2 knockdown increased micro- neogenesis and stimulating lipogenesis. Insulin- independent mechanism for Akt-mediated tubule shrinkage, suggesting septins inhibit induced lipid synthesis requires induction of the regulation of liver lipogenesis. AIZ microtubule depolymerization and thus main- transcription factor SREBP1c, which is mediated tain persistent microtubule growth. by the activation of mTORC1 (mammalian tar- Hence, septin control of microtubule growth get of rapamycin complex 1), through the Akt- and directionality seems to allow for correct dependent inhibition of the TSC1–TSC2 (tuber- This way up: Septins guide organization of microtubules in establishing a ous sclerosis protein 1 and 2) complex. Yecies microtubules polarized epithelial cell. GD et al. now identify an mTORC1-independent pathway that induces SREBP1c to promote lipo- Formation of a polarized epithelial cell requires genesis in the liver (Cell Metab. 14, 21–32; 2011). rearrangement of the cell’s microtubules. As the To elucidate the role of mTORC1 in the flat cell rises up into a column, the microtubules SNARE proteins regulate regulation of hepatic lipid metabolism, Yecies are formed into a complex network consisting autophagosome biogenesis et al. genetically ablated Tsc1 to generate a of bundles aligned from the top to the bottom liver-specific, insulin-independent mTORC1 of the cell, and a meshwork of shorter filaments Pre-autophagosomal structures mature into gain-of-function model (LTsc1KO).
    [Show full text]
  • SEPT2 Is a New Fusion Partner of MLL in Acute Myeloid Leukemia with T (2
    Oncogene (2006) 25, 6147–6152 & 2006 Nature Publishing Group All rights reserved 0950-9232/06 $30.00 www.nature.com/onc ONCOGENOMICS SEPT2 is a new fusion partner of MLL in acute myeloid leukemia with t(2;11)(q37;q23) N Cerveira1, C Correia1, S Bizarro1, C Pinto1, S Lisboa1, JM Mariz2, M Marques2 and MR Teixeira1 1Department of Genetics, Portuguese Oncology Institute, Porto, Portugal and 2Department of Onco-Hematology, Portuguese Oncology Institute, Porto, Portugal We have identified a new mixed lineage leukemia (MLL) hematopoietic stem cells or progenitors (Daser and gene fusion partner in a patient with treatment-related Rabbitts, 2005; Li et al., 2005; Slany, 2005). Normally, acute myeloid leukemia (AML)presenting a HOX expression is high in hematopoietic stem cells and t(2;11)(q37;q23) as the only cytogenetic abnormality. becomes gradually extinguished during differentiation Fluorescence in situ hybridization demonstrated a re- (Grier et al., 2005). A failure to downregulate HOX arrangement of the MLL gene and molecular genetic expression inhibits hematopoietic maturation and can analyses identified a septin family gene, SEPT2, located lead to leukemia (Grier et al., 2005). on chromosome 2q37, as the fusion partner of MLL.RNA Abnormalities of 11q23 involving the MLL gene are and DNA analyses showed the existence of an in-frame found in several hematological malignancies, including fusion of MLL exon 7 with SEPT2 exon 3, with the acute lymphoblastic leukemia (ALL)and acute myeloid genomic breakpoints located in intron 7 and 2 of MLL leukemia (AML)(Huret, 2005).The overall incidence of and SEPT2, respectively. Search for DNA sequence MLL-associated leukemia is around 3 and 8–10% for motifs revealed the existence of two sequences with AML and ALL, respectively (Daser and Rabbitts, 94.4% homology with the topoisomerase II consensus 2005).
    [Show full text]
  • Septins 2, 7 and 9 and MAP4 Colocalize Along the Axoneme in the Primary Cilium and Control Ciliary Length
    Research Article 2583 Septins 2, 7 and 9 and MAP4 colocalize along the axoneme in the primary cilium and control ciliary length Rania Ghossoub1,2,3, Qicong Hu4, Marion Failler1,2,3,5, Marie-Christine Rouyez1,2,3, Benjamin Spitzbarth6, Serge Mostowy7,8,9,*, Uwe Wolfrum6, Sophie Saunier3,5, Pascale Cossart7,8,9, W. James Nelson4,10,`,§ and Alexandre Benmerah1,2,3,5,`,§ 1INSERM U1016, Insitut Cochin, Paris, France 2CNRS UMR8104, Paris, France 3Universite´ Paris Descartes, Sorbonne Paris Cite´, Institut Imagine, Paris, France 4Department of Biology, Stanford University, Stanford, CA, USA 5INSERM, U983, Hoˆpital Necker-Enfants Malades, Paris, France 6Department of Cell and Matrix Biology, Institute of Zoology, Johannes Gutenberg University, Mainz, Germany 7Institut Pasteur, Unite´ des Interactions Bacte´ries-Cellules, De´partement de Biologie Cellulaire et Infection, Paris, France 8INSERM, U604, Paris, France 9INRA, USC2020, Paris, France 10Department of Molecular and Cellular Physiology, Stanford University, Stanford, CA, USA *Present address: Section of Microbiology, MRC Centre for Molecular Bacteriology and Infection, Imperial College London, London, UK `These authors contributed equally to this work §Authors for correspondence ([email protected]; [email protected]) Accepted 20 March 2013 Journal of Cell Science 126, 2583–2594 ß 2013. Published by The Company of Biologists Ltd doi: 10.1242/jcs.111377 Summary Septins are a large, evolutionarily conserved family of GTPases that form hetero-oligomers and interact with the actin-based cytoskeleton and microtubules. They are involved in scaffolding functions, and form diffusion barriers in budding yeast, the sperm flagellum and the base of primary cilia of kidney epithelial cells. We investigated the role of septins in the primary cilium of retinal pigmented epithelial (RPE) cells, and found that SEPT2 forms a 1:1:1 complex with SEPT7 and SEPT9 and that the three members of this complex colocalize along the length of the axoneme.
    [Show full text]
  • Structural Insight Into Filament Formation by Mammalian Septins
    doi:10.1038/nature06052 ARTICLES Structural insight into filament formation by mammalian septins Minhajuddin Sirajuddin1, Marian Farkasovsky1{, Florian Hauer2, Dorothee Ku¨hlmann1, Ian G. Macara3, Michael Weyand1, Holger Stark2 & Alfred Wittinghofer1 Septins are GTP-binding proteins that assemble into homo- and hetero-oligomers and filaments. Although they have key roles in various cellular processes, little is known concerning the structure of septin subunits or the organization and polarity of septin complexes. Here we present the structures of the human SEPT2 G domain and the heterotrimeric human SEPT2–SEPT6–SEPT7 complex. The structures reveal a universal bipolar polymer building block, composed of an extended G domain, which forms oligomers and filaments by conserved interactions between adjacent nucleotide-binding sites and/or the amino- and carboxy-terminal extensions. Unexpectedly, X-ray crystallography and electron microscopy showed that the predicted coiled coils are not involved in or required for complex and/or filament formation. The asymmetrical heterotrimers associate head-to-head to form a hexameric unit that is nonpolarized along the filament axis but is rotationally asymmetrical. The architecture of septin filaments differs fundamentally from that of other cytoskeletal structures. Septins are conserved GTP-binding proteins discovered in the bud- The SEPT2 G domain ding yeast Saccharomyces cerevisiae, where they organize into a ring at Human SEPT2 lacking 46 residues of the predicted C-terminal coiled the bud neck1–4. A parallel array of filaments is formed from hetero- coil (SEPT2-315) was isolated as recombinant protein from oligomers of four septins, which interact asymmetrically with other Escherichia coli. It contains 50% bound GDP and elutes in several proteins during cell division5,6.
    [Show full text]
  • Revised Subunit Order of Mammalian Septin Complexes Explains Their in Vitro Polymerization Properties Forooz Soroor1, 2, Moshe S
    bioRxiv preprint doi: https://doi.org/10.1101/569871; this version posted March 7, 2019. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC-ND 4.0 International license. Revised subunit order of mammalian septin complexes explains their in vitro polymerization properties Forooz Soroor1, 2, Moshe S. Kim1.2, Oliva Palander1, 2, Yadu Balachandran1, Richard Collins1, Samir Benlekbir3, John Rubinstein2,3 and William S. Trimble1,2,4,5 1Cell Biology Program, Hospital for Sick Children, Toronto, Ontario, Canada, M5G 1X8 2 Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada, M5G 1A8 3Molecular Medicine Program, Hospital for Sick Children, Toronto, Ontario, Canada, M5G 1X8 4Department of Physiology, University of Toronto, Toronto, Ontario, Canada, M5G 1A8 5Corresponding author ABSTRACT Septins are conserved GTP-binding cytoskeletal proteins that polymerize into filaments by end-to-end joining of heterooligomeric complexes. In human cells, both hexamers and octamers exist, and crystallography studies predicted the order of the hexamers to be SEPT7-SEPT6-SEPT2-SEPT2-SEPT6-SEPT7, while octamers are thought to have the same core, but with SEPT9 at the ends. However, based on this septin organization, octamers and hexamers would not be expected to co-polymerize due to incompatible ends. Here we isolated hexamers and octamers of specific composition from human cells and show that hexamers and octamers polymerize individually and, surprisingly, with each other. Binding of Borg3 results in distinctive clustering of each filament type.
    [Show full text]