Scinderin (also known as adseverin) is a protein that in humans is encoded by the SCINgene.[5] Scinderin is an actin severing protein belonging to the gelsolin superfamily.[6] It was discovered in Dr. Trifaro's laboratory at the University of Ottawa, Canada. Secretory tissues are rich in scinderin. In these tissues scinderin, a calcium dependent protein, regulates cortical actin networks. Normally secretory vesicles are excluded from release sites on the plasma membrane by the presence of a cortical actin filament network. During cell stimulation, calcium channels open allowing calcium ions to enter the secretory cell. Increase in intracellular calcium activates scinderin with the consequent actin filament severing and local dissociation of actin filament networks. This allows the movement of secretory vesicles to release sites on the plasma membrane.
^Ghoshdastider U, Popp D, Burtnick LD, Robinson RC (2013). "The expanding superfamily of gelsolin homology domain proteins". Cytoskeleton. 70 (11): 775–95. doi:10.1002/cm.21149. PMID 24155256. S2CID 205643538.
Further readingedit
Rodríguez Del Castillo A, Vitale ML, Trifaró JM (1992). "Ca2+ and pH determine the interaction of chromaffin cell scinderin with phosphatidylserine and phosphatidylinositol 4,5,-biphosphate and its cellular distribution during nicotinic-receptor stimulation and protein kinase C activation". J. Cell Biol. 119 (4): 797–810. doi:10.1083/jcb.119.4.797. PMC2289683. PMID 1331119.
Rodríguez Del Castillo A, Vitale ML, Tchakarov L, Trifaró JM (1992). "Human platelets contain scinderin, a Ca(2+)-dependent actin filament-severing protein". Thromb. Haemost. 67 (2): 248–51. doi:10.1055/s-0038-1648420. PMID 1621245. S2CID 20052201.
Lueck A, Brown D, Kwiatkowski DJ (1999). "The actin-binding proteins adseverin and gelsolin are both highly expressed but differentially localized in kidney and intestine". J. Cell Sci. 111. ( Pt 24) (24): 3633–43. doi:10.1242/jcs.111.24.3633. PMID 9819354.
Zunino R, Li Q, Rosé SD, et al. (2001). "Expression of scinderin in megakaryoblastic leukemia cells induces differentiation, maturation, and apoptosis with release of plateletlike particles and inhibits proliferation and tumorigenesis". Blood. 98 (7): 2210–9. doi:10.1182/blood.V98.7.2210. hdl:11336/60914. PMID 11568009.
Nagase T, Kikuno R, Ohara O (2002). "Prediction of the coding sequences of unidentified human genes. XXI. The complete sequences of 60 new cDNA clones from brain which code for large proteins". DNA Res. 8 (4): 179–87. doi:10.1093/dnares/8.4.179. PMID 11572484.
Lejen T, Pene TD, Rosé SD, Trifaró JM (2002). "The role of different Scinderin domains in the control of F-actin cytoskeleton during exocytosis". Ann. N. Y. Acad. Sci. 971 (1): 248–50. Bibcode:2002NYASA.971..248L. doi:10.1111/j.1749-6632.2002.tb04469.x. PMID 12438125. S2CID 19994226.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC139241. PMID 12477932.
Hillier LW, Fulton RS, Fulton LA, et al. (2003). "The DNA sequence of human chromosome 7". Nature. 424 (6945): 157–64. Bibcode:2003Natur.424..157H. doi:10.1038/nature01782. PMID 12853948.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Bouwmeester T, Bauch A, Ruffner H, et al. (2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nat. Cell Biol. 6 (2): 97–105. doi:10.1038/ncb1086. PMID 14743216. S2CID 11683986.
Ehre C, Rossi AH, Abdullah LH, et al. (2005). "Barrier role of actin filaments in regulated mucin secretion from airway goblet cells". Am. J. Physiol., Cell Physiol. 288 (1): C46–56. doi:10.1152/ajpcell.00397.2004. PMID 15342343.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC528928. PMID 15489334.
Otsuki T, Ota T, Nishikawa T, et al. (2007). "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries". DNA Res. 12 (2): 117–26. doi:10.1093/dnares/12.2.117. PMID 16303743.
Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC1356129. PMID 16344560.
This article on a gene on human chromosome 7 is a stub. You can help Wikipedia by expanding it.
scin, scinderin, also, known, adseverin, protein, that, humans, encoded, gene, scinderin, actin, severing, protein, belonging, gelsolin, superfamily, discovered, trifaro, laboratory, university, ottawa, canada, secretory, tissues, rich, scinderin, these, tissu. Scinderin also known as adseverin is a protein that in humans is encoded by the SCIN gene 5 Scinderin is an actin severing protein belonging to the gelsolin superfamily 6 It was discovered in Dr Trifaro s laboratory at the University of Ottawa Canada Secretory tissues are rich in scinderin In these tissues scinderin a calcium dependent protein regulates cortical actin networks Normally secretory vesicles are excluded from release sites on the plasma membrane by the presence of a cortical actin filament network During cell stimulation calcium channels open allowing calcium ions to enter the secretory cell Increase in intracellular calcium activates scinderin with the consequent actin filament severing and local dissociation of actin filament networks This allows the movement of secretory vesicles to release sites on the plasma membrane SCINAvailable structuresPDBOrtholog search PDBe RCSBList of PDB id codes3FG6 5A1K 5A1MIdentifiersAliasesSCIN scinderinExternal IDsOMIM 613416 MGI 1306794 HomoloGene 36296 GeneCards SCINGene location Human Chr Chromosome 7 human 1 Band7p21 3Start12 570 577 bp 1 End12 660 182 bp 1 Gene location Mouse Chr Chromosome 12 mouse 2 Band12 12 B1Start40 109 768 bp 2 End40 184 227 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed injejunal mucosatibiarenal medulladuodenumAchilles tendonkidneypalpebral conjunctivaoral cavityright uterine tuberectumTop expressed inleft colonmolarcorneal stromaPaneth cellseminal vesiculajejunummedullary collecting ductconjunctival fornixkidneyduodenumMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functioncalcium ion binding phosphatidylserine binding actin filament binding 1 phosphatidylinositol binding actin binding phosphatidylinositol 4 5 bisphosphate binding metal ion bindingCellular componentcytoplasm cell cortex brush border extracellular exosome cytoskeleton podosome cell junction cell projection plasma membrane protein containing complexBiological processsequestering of actin monomers regulation of chondrocyte differentiation actin nucleation actin filament severing positive regulation of actin nucleation positive regulation of secretion actin filament capping positive regulation of apoptotic process positive regulation of megakaryocyte differentiation negative regulation of cell population proliferation calcium ion regulated exocytosisSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez8547720259EnsemblENSG00000006747ENSMUSG00000002565UniProtQ9Y6U3Q60604RefSeq mRNA NM 001112706NM 033128NM 001146196NM 009132RefSeq protein NP 001106177NP 149119NP 001139668NP 033158Location UCSC Chr 7 12 57 12 66 MbChr 12 40 11 40 18 MbPubMed search 3 4 WikidataView Edit HumanView Edit MouseReferences edit a b c GRCh38 Ensembl release 89 ENSG00000006747 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000002565 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Mouse PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Entrez Gene SCIN scinderin Ghoshdastider U Popp D Burtnick LD Robinson RC 2013 The expanding superfamily of gelsolin homology domain proteins Cytoskeleton 70 11 775 95 doi 10 1002 cm 21149 PMID 24155256 S2CID 205643538 Further reading editRodriguez Del Castillo A Vitale ML Trifaro JM 1992 Ca2 and pH determine the interaction of chromaffin cell scinderin with phosphatidylserine and phosphatidylinositol 4 5 biphosphate and its cellular distribution during nicotinic receptor stimulation and protein kinase C activation J Cell Biol 119 4 797 810 doi 10 1083 jcb 119 4 797 PMC 2289683 PMID 1331119 Rodriguez Del Castillo A Vitale ML Tchakarov L Trifaro JM 1992 Human platelets contain scinderin a Ca 2 dependent actin filament severing protein Thromb Haemost 67 2 248 51 doi 10 1055 s 0038 1648420 PMID 1621245 S2CID 20052201 Lueck A Brown D Kwiatkowski DJ 1999 The actin binding proteins adseverin and gelsolin are both highly expressed but differentially localized in kidney and intestine J Cell Sci 111 Pt 24 24 3633 43 doi 10 1242 jcs 111 24 3633 PMID 9819354 Zunino R Li Q Rose SD et al 2001 Expression of scinderin in megakaryoblastic leukemia cells induces differentiation maturation and apoptosis with release of plateletlike particles and inhibits proliferation and tumorigenesis Blood 98 7 2210 9 doi 10 1182 blood V98 7 2210 hdl 11336 60914 PMID 11568009 Nagase T Kikuno R Ohara O 2002 Prediction of the coding sequences of unidentified human genes XXI The complete sequences of 60 new cDNA clones from brain which code for large proteins DNA Res 8 4 179 87 doi 10 1093 dnares 8 4 179 PMID 11572484 Lejen T Pene TD Rose SD Trifaro JM 2002 The role of different Scinderin domains in the control of F actin cytoskeleton during exocytosis Ann N Y Acad Sci 971 1 248 50 Bibcode 2002NYASA 971 248L doi 10 1111 j 1749 6632 2002 tb04469 x PMID 12438125 S2CID 19994226 Strausberg RL Feingold EA Grouse LH et al 2003 Generation and initial analysis of more than 15 000 full length human and mouse cDNA sequences Proc Natl Acad Sci U S A 99 26 16899 903 Bibcode 2002PNAS 9916899M doi 10 1073 pnas 242603899 PMC 139241 PMID 12477932 Hillier LW Fulton RS Fulton LA et al 2003 The DNA sequence of human chromosome 7 Nature 424 6945 157 64 Bibcode 2003Natur 424 157H doi 10 1038 nature01782 PMID 12853948 Ota T Suzuki Y Nishikawa T et al 2004 Complete sequencing and characterization of 21 243 full length human cDNAs Nat Genet 36 1 40 5 doi 10 1038 ng1285 PMID 14702039 Bouwmeester T Bauch A Ruffner H et al 2004 A physical and functional map of the human TNF alpha NF kappa B signal transduction pathway Nat Cell Biol 6 2 97 105 doi 10 1038 ncb1086 PMID 14743216 S2CID 11683986 Ehre C Rossi AH Abdullah LH et al 2005 Barrier role of actin filaments in regulated mucin secretion from airway goblet cells Am J Physiol Cell Physiol 288 1 C46 56 doi 10 1152 ajpcell 00397 2004 PMID 15342343 Gerhard DS Wagner L Feingold EA et al 2004 The status quality and expansion of the NIH full length cDNA project the Mammalian Gene Collection MGC Genome Res 14 10B 2121 7 doi 10 1101 gr 2596504 PMC 528928 PMID 15489334 Otsuki T Ota T Nishikawa T et al 2007 Signal sequence and keyword trap in silico for selection of full length human cDNAs encoding secretion or membrane proteins from oligo capped cDNA libraries DNA Res 12 2 117 26 doi 10 1093 dnares 12 2 117 PMID 16303743 Kimura K Wakamatsu A Suzuki Y et al 2006 Diversification of transcriptional modulation large scale identification and characterization of putative alternative promoters of human genes Genome Res 16 1 55 65 doi 10 1101 gr 4039406 PMC 1356129 PMID 16344560 nbsp This article on a gene on human chromosome 7 is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title SCIN amp oldid 1193125491, wikipedia, wiki, book, books, library,
