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{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = Scinderin
| HGNCid = 21695
| Symbol = SCIN
| AltSymbols =; KIAA1905
| OMIM = 
| ECnumber = 
| Homologene = 
| MGIid = 
| GeneAtlas_image1 = PBB_GE_SCIN_222272_x_at_tn.png
| Function = {{GNF_GO|id=GO:0001786 |text = phosphatidylserine binding}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005545 |text = phosphatidylinositol binding}} {{GNF_GO|id=GO:0005546 |text = phosphatidylinositol-4,5-bisphosphate binding}} {{GNF_GO|id=GO:0051015 |text = actin filament binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005856 |text = cytoskeleton}} {{GNF_GO|id=GO:0005938 |text = cell cortex}}
| Process = {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}} {{GNF_GO|id=GO:0017156 |text = calcium ion-dependent exocytosis}} {{GNF_GO|id=GO:0043065 |text = positive regulation of apoptosis}} {{GNF_GO|id=GO:0045010 |text = actin nucleation}} {{GNF_GO|id=GO:0045654 |text = positive regulation of megakaryocyte differentiation}} {{GNF_GO|id=GO:0051014 |text = actin filament severing}} {{GNF_GO|id=GO:0051016 |text = barbed-end actin filament capping}} {{GNF_GO|id=GO:0051047 |text = positive regulation of secretion}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 85477
    | Hs_Ensembl = ENSG00000006747
    | Hs_RefseqProtein = NP_149119
    | Hs_RefseqmRNA = NM_033128
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 7
    | Hs_GenLoc_start = 12576728
    | Hs_GenLoc_end = 12659254
    | Hs_Uniprot = Q9Y6U3
    | Mm_EntrezGene = 
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = 
    | Mm_RefseqProtein = 
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''Scinderin''', also known as '''SCIN''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SCIN scinderin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=85477| accessdate = }}</ref>


{{Infobox_gene}}
'''Scinderin''' (also known as '''adseverin''') is a [[protein]] that in humans is encoded by the ''SCIN'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SCIN scinderin| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=85477| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text =  
| summary_text =  
Scinderin is an [[actin]] severing protein belonging to the [[gelsolin]] superfamily.<ref>{{Cite journal
| pmid = 24155256
| year = 2013
| author1 = Ghoshdastider
| first1 = U
| title = The expanding superfamily of gelsolin homology domain proteins
| journal = Cytoskeleton
| volume = 70
| issue = 11
| pages = 775–95
| last2 = Popp
| first2 = D
| last3 = Burtnick
| first3 = L. D.
| last4 = Robinson
| first4 = R. C.
| doi = 10.1002/cm.21149
}}</ref> 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 [[vesicle (biology and chemistry)|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 consecuent [[actin filament]] severing and local dissociation of actin filament networks. This allows the movement of secretory vesicles to release sites on the plasma membrane.
}}
}}


==References==
== References ==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Rodríguez Del Castillo A, Vitale ML, Trifaró JM |title=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. |journal=J. Cell Biol. |volume=119 |issue= 4 |pages= 797-810 |year= 1992 |pmid= 1331119 |doi=  }}
*{{cite journal  |author1=Rodríguez Del Castillo A |author2=Vitale ML |author3=Trifaró JM |title=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. |journal=J. Cell Biol. |volume=119 |issue= 4 |pages= 797–810 |year= 1992 |pmid= 1331119 |doi=10.1083/jcb.119.4.797  | pmc=2289683 }}
*{{cite journal  | author=Rodríguez Del Castillo A, Vitale ML, Tchakarov L, Trifaró JM |title=Human platelets contain scinderin, a Ca(2+)-dependent actin filament-severing protein. |journal=Thromb. Haemost. |volume=67 |issue= 2 |pages= 248-51 |year= 1992 |pmid= 1621245 |doi=  }}
*{{cite journal  |author1=Rodríguez Del Castillo A |author2=Vitale ML |author3=Tchakarov L |author4=Trifaró JM |title=Human platelets contain scinderin, a Ca(2+)-dependent actin filament-severing protein. |journal=Thromb. Haemost. |volume=67 |issue= 2 |pages= 248–51 |year= 1992 |pmid= 1621245 |doi=  }}
*{{cite journal  | author=Lueck A, Brown D, Kwiatkowski DJ |title=The actin-binding proteins adseverin and gelsolin are both highly expressed but differentially localized in kidney and intestine. |journal=J. Cell. Sci. |volume=111 ( Pt 24) |issue=  |pages= 3633-43 |year= 1999 |pmid= 9819354 |doi=  }}
*{{cite journal  |author1=Lueck A |author2=Brown D |author3=Kwiatkowski DJ |title=The actin-binding proteins adseverin and gelsolin are both highly expressed but differentially localized in kidney and intestine. | series=111 |journal=J. Cell Sci. |volume=( Pt 24) |issue=  |pages= 3633–43 |year= 1999 |pmid= 9819354 |doi=  }}
*{{cite journal | author=Zunino R, Li Q, Rosé SD, ''et al.'' |title=Expression of scinderin in megakaryoblastic leukemia cells induces differentiation, maturation, and apoptosis with release of plateletlike particles and inhibits proliferation and tumorigenesis. |journal=Blood |volume=98 |issue= 7 |pages= 2210-9 |year= 2001 |pmid= 11568009 |doi=  }}
*{{cite journal   |vauthors=Zunino R, Li Q, Rosé SD, etal |title=Expression of scinderin in megakaryoblastic leukemia cells induces differentiation, maturation, and apoptosis with release of plateletlike particles and inhibits proliferation and tumorigenesis. |journal=Blood |volume=98 |issue= 7 |pages= 2210–9 |year= 2001 |pmid= 11568009 |doi=10.1182/blood.V98.7.2210 }}
*{{cite journal  | author=Nagase T, Kikuno R, Ohara O |title=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. |journal=DNA Res. |volume=8 |issue= 4 |pages= 179-87 |year= 2002 |pmid= 11572484 |doi=  }}
*{{cite journal  |author1=Nagase T |author2=Kikuno R |author3=Ohara O |title=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. |journal=DNA Res. |volume=8 |issue= 4 |pages= 179–87 |year= 2002 |pmid= 11572484 |doi=10.1093/dnares/8.4.179 }}
*{{cite journal  | author=Lejen T, Pene TD, Rosé SD, Trifaró JM |title=The role of different Scinderin domains in the control of F-actin cytoskeleton during exocytosis. |journal=Ann. N. Y. Acad. Sci. |volume=971 |issue=  |pages= 248-50 |year= 2002 |pmid= 12438125 |doi=  }}
*{{cite journal  |author1=Lejen T |author2=Pene TD |author3=Rosé SD |author4=Trifaró JM |title=The role of different Scinderin domains in the control of F-actin cytoskeleton during exocytosis. |journal=Ann. N. Y. Acad. Sci. |volume=971 |issue=  1|pages= 248–50 |year= 2002 |pmid= 12438125 |doi=10.1111/j.1749-6632.2002.tb04469.x }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }}
*{{cite journal | author=Hillier LW, Fulton RS, Fulton LA, ''et al.'' |title=The DNA sequence of human chromosome 7. |journal=Nature |volume=424 |issue= 6945 |pages= 157-64 |year= 2003 |pmid= 12853948 |doi= 10.1038/nature01782 }}
*{{cite journal   |vauthors=Hillier LW, Fulton RS, Fulton LA, etal |title=The DNA sequence of human chromosome 7. |journal=Nature |volume=424 |issue= 6945 |pages= 157–64 |year= 2003 |pmid= 12853948 |doi= 10.1038/nature01782 }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal   |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal | author=Bouwmeester T, Bauch A, Ruffner H, ''et al.'' |title=A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway. |journal=Nat. Cell Biol. |volume=6 |issue= 2 |pages= 97-105 |year= 2004 |pmid= 14743216 |doi= 10.1038/ncb1086 }}
*{{cite journal   |vauthors=Bouwmeester T, Bauch A, Ruffner H, etal |title=A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway. |journal=Nat. Cell Biol. |volume=6 |issue= 2 |pages= 97–105 |year= 2004 |pmid= 14743216 |doi= 10.1038/ncb1086 }}
*{{cite journal | author=Ehre C, Rossi AH, Abdullah LH, ''et al.'' |title=Barrier role of actin filaments in regulated mucin secretion from airway goblet cells. |journal=Am. J. Physiol., Cell Physiol. |volume=288 |issue= 1 |pages= C46-56 |year= 2005 |pmid= 15342343 |doi= 10.1152/ajpcell.00397.2004 }}
*{{cite journal   |vauthors=Ehre C, Rossi AH, Abdullah LH, etal |title=Barrier role of actin filaments in regulated mucin secretion from airway goblet cells. |journal=Am. J. Physiol., Cell Physiol. |volume=288 |issue= 1 |pages= C46–56 |year= 2005 |pmid= 15342343 |doi= 10.1152/ajpcell.00397.2004 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }}
*{{cite journal | author=Otsuki T, Ota T, Nishikawa T, ''et al.'' |title=Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. |journal=DNA Res. |volume=12 |issue= 2 |pages= 117-26 |year= 2007 |pmid= 16303743 |doi= 10.1093/dnares/12.2.117 }}
*{{cite journal   |vauthors=Otsuki T, Ota T, Nishikawa T, etal |title=Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. |journal=DNA Res. |volume=12 |issue= 2 |pages= 117–26 |year= 2007 |pmid= 16303743 |doi= 10.1093/dnares/12.2.117 }}
*{{cite journal | author=Kimura K, Wakamatsu A, Suzuki Y, ''et al.'' |title=Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes. |journal=Genome Res. |volume=16 |issue= 1 |pages= 55-65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406 }}
*{{cite journal   |vauthors=Kimura K, Wakamatsu A, Suzuki Y, etal |title=Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes. |journal=Genome Res. |volume=16 |issue= 1 |pages= 55–65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406 | pmc=1356129 }}
}}
}}
{{refend}}
{{refend}}


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Latest revision as of 20:09, 19 February 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Scinderin (also known as adseverin) is a protein that in humans is encoded by the SCIN gene.[1] Scinderin is an actin severing protein belonging to the gelsolin superfamily.[2] 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 consecuent actin filament severing and local dissociation of actin filament networks. This allows the movement of secretory vesicles to release sites on the plasma membrane.

References

  1. ↑ "Entrez Gene: SCIN scinderin".
  2. ↑ Ghoshdastider, U; Popp, D; Burtnick, L. D.; Robinson, R. C. (2013). "The expanding superfamily of gelsolin homology domain proteins". Cytoskeleton. 70 (11): 775–95. doi:10.1002/cm.21149. PMID 24155256.

Further reading



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