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Gene Review

SCIN  -  scinderin

Bos taurus

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Disease relevance of SCIN


High impact information on SCIN


Biological context of SCIN

  • The observation strongly suggested that adseverin is not involved in secretory processes in general but is specifically involved in exocytosis [1].
  • A new member of the gelsolin/villin family of actin regulatory proteins was initially identified by screening an adult murine brain cDNA library with a probe for bovine adseverin [6].
  • Sc domain role in secretion was studied by co-transfection of human growth hormone (hGH) reporter gene and green fluorescent protein (GFP)-fusion Sc constructs [7].
  • In addition, scinderin antisense treatment did not alter the expression of proteins involved in vesicle-plasma membrane fusion, such as synaptophysin, synaptotagmin or syntaxin, indicating a lack of effects on the fusion machinery components [8].
  • In view of the wide tissue distribution of gelsolin, another actin filament-severing protein, experiments were performed to determine the tissue expression of scinderin [9].

Anatomical context of SCIN


Associations of SCIN with chemical compounds

  • The NH2 termini of native adseverin and the Mr 42,000 fragment were confirmed to be blocked by amino acid sequencing [10].
  • Ca2(+)-dependent binding of adseverin to PS liposomes but not to PC or PE liposomes was observed by a centrifugation assay [11].
  • A 74-kDa protein (adseverin) derived from adrenal medulla severs actin filaments and nucleates actin polymerization in a Ca2(+)-dependent manner but does not form an EGTA-resistant complex with actin monomers, which is different from the gelsolin-actin interaction [11].
  • Histamine evoked similar patterns of distribution of scinderin and filamentous actin [12].
  • The trigger for the release of Ca2+ was inositol 1,4,5-trisphosphate because U-73122, a phospholipase C inhibitor, but not its inactive isomer (U-73343), inhibited the increases in IP3 and intracellular Ca2+ levels, scinderin redistribution, cortical F-actin disassembly, and catecholamine release in response to histamine [12].

Regulatory relationships of SCIN

  • Here we report that histamine-H1 receptor activation induces redistribution of scinderin, a Ca(2+)-dependent F-actin severing protein, cortical F-actin disassembly, and catecholamine release [12].

Other interactions of SCIN


Analytical, diagnostic and therapeutic context of SCIN


  1. Differential expression of bovine adseverin in adrenal gland revealed by in situ hybridization. Cloning of a cDNA for adseverin. Nakamura, S., Sakurai, T., Nonomura, Y. J. Biol. Chem. (1994) [Pubmed]
  2. Selective acylation of plasma membrane proteins of Mycoplasma mycoides subsp. mycoides SC, the contagious bovine pleuropneumonia agent. Jan, G., Fontenelle, C., Verrier, F., Le Hénaff, M., Wróblewski, H. Curr. Microbiol. (1996) [Pubmed]
  3. Recombinant scinderin enhances exocytosis, an effect blocked by two scinderin-derived actin-binding peptides and PIP2. Zhang, L., Marcu, M.G., Nau-Staudt, K., Trifaró, J.M. Neuron (1996) [Pubmed]
  4. Cortical filamentous actin disassembly and scinderin redistribution during chromaffin cell stimulation precede exocytosis, a phenomenon not exhibited by gelsolin. Vitale, M.L., Rodríguez Del Castillo, A., Tchakarov, L., Trifaró, J.M. J. Cell Biol. (1991) [Pubmed]
  5. Chromaffin cell scinderin, a novel calcium-dependent actin filament-severing protein. Rodriguez Del Castillo, A., Lemaire, S., Tchakarov, L., Jeyapragasan, M., Doucet, J.P., Vitale, M.L., Trifaró, J.M. EMBO J. (1990) [Pubmed]
  6. Advillin (p92): a new member of the gelsolin/villin family of actin regulatory proteins. Marks, P.W., Arai, M., Bandura, J.L., Kwiatkowski, D.J. J. Cell. Sci. (1998) [Pubmed]
  7. Expression of various scinderin domains in chromaffin cells indicates that this protein acts as a molecular switch in the control of actin filament dynamics and exocytosis. Dumitrescu Pene, T., Rosé, S.D., Lejen, T., Marcu, M.G., Trifaró, J.M. J. Neurochem. (2005) [Pubmed]
  8. An antisense oligodeoxynucleotide targeted to chromaffin cell scinderin gene decreased scinderin levels and inhibited depolarization-induced cortical F-actin disassembly and exocytosis. Lejen, T., Skolnik, K., Rosé, S.D., Marcu, M.G., Elzagallaai, A., Trifaró, J.M. J. Neurochem. (2001) [Pubmed]
  9. Expression of scinderin, an actin filament-severing protein, in different tissues. Tchakarov, L., Vitale, M.L., Jeyapragasan, M., Rodriguez Del Castillo, A., Trifaró, J.M. FEBS Lett. (1990) [Pubmed]
  10. The Ca2(+)-dependent actin filament-severing activity of 74-kDa protein (adseverin) resides in its NH2-terminal half. Sakurai, T., Kurokawa, H., Nonomura, Y. J. Biol. Chem. (1991) [Pubmed]
  11. Inhibition of actin regulatory activity of the 74-kDa protein from bovine adrenal medulla (adseverin) by some phospholipids. Maekawa, S., Sakai, H. J. Biol. Chem. (1990) [Pubmed]
  12. Histamine-evoked chromaffin cell scinderin redistribution, F-actin disassembly, and secretion: in the absence of cortical F-actin disassembly, an increase in intracellular Ca2+ fails to trigger exocytosis. Zhang, L., Rodríguez Del Castillo, A., Trifaró, J.M. J. Neurochem. (1995) [Pubmed]
  13. Molecular cloning and functional expression of chromaffin cell scinderin indicates that it belongs to the family of Ca(2+)-dependent F-actin severing proteins. Marcu, M.G., Rodríguez del Castillo, A., Vitale, M.L., Trifaró, J.M. Mol. Cell. Biochem. (1994) [Pubmed]
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