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.
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.
PMID1621245.
S2CID20052201.
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.
PMID9819354.
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.
PMID14743216.
S2CID11683986.
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.
PMID15342343.
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.
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.
PMID1621245.
S2CID20052201.
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.
PMID9819354.
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.
PMID14743216.
S2CID11683986.
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.
PMID15342343.