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gelsolin; actin-depolymerizing factor; ADF; brevin; AGEL (GSN)
Function:
- Ca+2-triggered actin filament-severing protein
- binds to the plus (or barbed) ends of actin monomers or filaments preventing monomer exchange (end-blocking or capping)
- can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed
- remains tightly bound to barbed end of F-actin after severing filament
- phosphorylation on Tyr-86, Tyr-409, Tyr-465, Tyr-603 & Tyr-651 in vitro is induced in presence of phospholipids
- binds to actin & to fibronectin
Structure:
- belongs to the villin/gelsolin family
- contains 6 gelsolin-like repeats
Compartment:
- isoform 2: cytoplasm, cytoskeleton
- isoform 1: secreted
Alternative initiation:
- named isoforms=2;
- initiator Met-1 may be either removed, or N-acetylated
Expression:
- phagocytic cells, platelets, fibroblasts, nonmuscle cells, smooth muscle & skeletal muscle cells
Pathology:
- defects in GSN are the cause of amyloidosis type 5 (Finnish type amyloidosis)
Interactions
molecular events
General
Ca+2 binding protein
cytoskeletal protein
Properties
SIZE: entity length = 782 aa
MW = 86 kD
COMPARTMENT: cytoplasm
MOTIF: signal sequence {1-27}
Actin-severing {53-176}
MOTIF: Gelsolin-like {76-126}
Tyr phosphorylation site {Y86}
Actin contact {123-126}
binding site
SITE: 162-169
FOR-BINDING-OF: POLYPHOSPHOINOSITIDE
Polyphosphoinositide binding {188-196}
Gelsolin-like {198-238}
MOTIF: cysteine residue {C215}
MODIFICATION: cysteine residue {C228}
cysteine residue {C228}
MODIFICATION: cysteine residue {C215}
Gelsolin-like {314-356}
Tyr phosphorylation site {Y409}
binding site
SITE: 434-782
FOR-BINDING-OF: actin
MOTIF: Gelsolin-like {453-504}
Tyr phosphorylation site {Y465}
Gelsolin-like {576-616}
Tyr phosphorylation site {Y603}
Tyr phosphorylation site {Y651}
Gelsolin-like {679-721}
Database Correlations
OMIM correlations
MORBIDMAP 137350
UniProt P06396
Pfam PF00626
Entrez Gene 2934
Kegg hsa:2934
References
- UniProt :accession P06396
- GeneReviews
https://www.genecards.org/cgi-bin/carddisp.pl?gene=GSN
- Wikipedia; Gelsolin
http://en.wikipedia.org/wiki/Gelsolin
- Molecular Cell Biology (2nd ed) Darnell J; Lodish H
& Baltimore D (eds), Scientific American Books,
WH Freeman, NY 1990, pg 889
- Stossel TP.
On the crawling of animal cells.
Science. 1993 May 21;260(5111):1086-94. Review.
PMID: 8493552