SCIN: Difference between revisions

Jump to navigation Jump to search
m (task, added underlinked tag using AWB)
imported>Jmertel23
m (added wikilinks and removed "underlinked" tag)
 
Line 1: Line 1:
{{Underlinked|date=November 2017}}
 
{{Infobox_gene}}
{{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>
'''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>
Line 6: Line 6:
| section_title =  
| section_title =  
| summary_text =  
| summary_text =  
Scinderin is an actin severing protein belonging to the gelsolin superfamily.<ref>{{Cite journal
Scinderin is an [[actin]] severing protein belonging to the [[gelsolin]] superfamily.<ref>{{Cite journal
  | pmid = 24155256
  | pmid = 24155256
| year = 2013
| year = 2013
Line 23: Line 23:
| first4 = R. C.
| first4 = R. C.
| doi = 10.1002/cm.21149
| 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 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 de secretory cell. Increase in intracellualr 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.
}}</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.
}}
}}



Latest revision as of 20:09, 19 February 2018

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

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