Gelsolin

GSN
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1C0F, 1C0G, 1D4X, 1DEJ, 1EQY, 1ESV, 1H1V, 1KCQ, 1MDU, 1NLV, 1NM1, 1NMD, 1P8X, 1P8Z, 1SOL, 1T44, 1YAG, 1YVN, 2FF3, 2FF6, 2FH1, 2FH2, 2FH3, 2FH4, 3A5L, 3A5M, 3A5N, 3A5O, 3CI5, 3CIP, 3CJB, 3CJC, 3FFK, 3FFN, 3TU5, 4PKG, 4PKH, 4PKI, 4S10, 4Z94
Identifiers
Aliases	GSN, Gsn, ADF, AGEL, gelsolin
External IDs	OMIM: 137350; MGI: 95851; HomoloGene: 147; GeneCards: GSN; OMA:GSN - orthologs
Gene location (Mouse)
Chr.	Chromosome 2 (mouse)
End	35,197,904 bp
RNA expression pattern
	n/a
	Top expressed in
	skin of external ear; ; subcutaneous adipose tissue; ; right lung; ; white adipose tissue; ; right lung lobe; ; tunica adventitia of aorta; ; stroma of bone marrow; ; left lung; ; superior surface of tongue; ; conjunctival fornix;
	; ;
	More reference expression data
Gene ontology
Molecular function	metal ion binding; protein binding; actin binding; myosin II binding; calcium ion binding; actin filament binding;
Cellular component	cytoplasm; cytosol; blood microparticle; plasma membrane; extracellular region; sarcoplasm; cortical actin cytoskeleton; actin cap; podosome; extracellular exosome; cytoskeleton; nucleus; secretory granule lumen; ficolin-1-rich granule lumen; ruffle; extracellular space; focal adhesion; actin cytoskeleton; lamellipodium; myelin sheath; perinuclear region of cytoplasm; protein-containing complex; phagocytic vesicle;
Biological process	regulation of plasma membrane raft polarization; cilium assembly; sequestering of actin monomers; actin filament reorganization; amyloid fibril formation; positive regulation of keratinocyte apoptotic process; striated muscle atrophy; regulation of establishment of T cell polarity; extracellular matrix disassembly; positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; positive regulation of actin nucleation; regulation of receptor clustering; positive regulation of gene expression; cell projection organization; protein destabilization; actin filament capping; regulation of podosome assembly; renal protein absorption; hepatocyte apoptotic process; neutrophil degranulation; actin nucleation; actin filament severing; barbed-end actin filament capping; phagocytosis, engulfment; apoptotic process; human ageing; actin polymerization or depolymerization; oligodendrocyte development; vesicle-mediated transport; actin filament polymerization; regulation of cell adhesion; wound healing; tissue regeneration; response to ethanol; phosphatidylinositol-mediated signaling; response to folic acid; cellular response to cadmium ion; positive regulation of protein processing in phagocytic vesicle; cellular response to interferon-gamma;
	Sources:Amigo / QuickGO
Orthologs
	2934
	227753
	ENSG00000148180
	ENSMUSG00000026879
	P06396
	P13020
NM_000177; NM_001127662; NM_001127663; NM_001127664; NM_001127665;
	NM_001127666; NM_001127667; NM_001258029; NM_001258030; NM_198252
NM_001206367; NM_001206368; NM_001206369; NM_146120; NM_001362945;
	NM_001362947; NM_001362948
NP_000168; NP_001121134; NP_001121135; NP_001121136; NP_001121137;
	NP_001121138; NP_001121139; NP_001244958; NP_001244959; NP_937895; NP_001339982; NP_001339983; NP_001339984; NP_001339985; NP_001339986; NP_001339987; NP_001339988; NP_001339989; NP_001339990; NP_001339991; NP_001339992; NP_001339993; NP_001339994; NP_001339995; NP_001339996; NP_001339997; NP_001339998; NP_001339999; NP_001340000; NP_001340001; NP_001340002; NP_001340003; NP_001340004; NP_001340005; NP_001340006; NP_001340007
NP_001193296; NP_001193297; NP_001193298; NP_666232; NP_001349874;
	NP_001349876; NP_001349877
	Wikidata
View/Edit Human	View/Edit Mouse

Gelsolin is an actin-binding protein that is a key regulator of actin filament assembly and disassembly. Gelsolin is one of the most potent members of the actin-severing gelsolin/villin superfamily, as it severs with nearly 100% efficiency.^[4]^[5]

Cellular gelsolin, found within the cytosol and mitochondria,^[6] has a closely related secreted form, Plasma gelsolin, that contains an additional 24 AA N-terminal extension.^[7]^[8] Plasma gelsolin's ability to sever actin filaments helps the body recover from disease and injury that leaks cellular actin into the blood. Additionally it plays important roles in host innate immunity, activating macrophages and localizing of inflammation.

^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000026879 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Ghoshdastider U, Popp D, Burtnick LD, Robinson RC (November 2013). "The expanding superfamily of gelsolin homology domain proteins". Cytoskeleton. 70 (11): 775–95. doi:10.1002/cm.21149. PMID 24155256. S2CID 205643538.
^ Sun HQ, Yamamoto M, Mejillano M, Yin HL (November 1999). "Gelsolin, a multifunctional actin regulatory protein". The Journal of Biological Chemistry. 274 (47): 33179–82. doi:10.1074/jbc.274.47.33179. PMID 10559185.
^ Koya RC, Fujita H, Shimizu S, Ohtsu M, Takimoto M, Tsujimoto Y, Kuzumaki N (May 2000). "Gelsolin inhibits apoptosis by blocking mitochondrial membrane potential loss and cytochrome c release". The Journal of Biological Chemistry. 275 (20): 15343–9. doi:10.1074/jbc.275.20.15343. hdl:2115/718. PMID 10809769.
^ Kwiatkowski DJ, Stossel TP, Orkin SH, Mole JE, Colten HR, Yin HL (1986-10-02). "Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain". Nature. 323 (6087): 455–8. Bibcode:1986Natur.323..455K. doi:10.1038/323455a0. PMID 3020431. S2CID 4356162.
^ Nag S, Larsson M, Robinson RC, Burtnick LD (July 2013). "Gelsolin: the tail of a molecular gymnast". Cytoskeleton. 70 (7): 360–84. doi:10.1002/cm.21117. PMID 23749648. S2CID 23646422.

[refGRCm38Ensembl-1] GRCm38: Ensembl release 89: ENSMUSG00000026879 – Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[3] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid24155256-4] Ghoshdastider U, Popp D, Burtnick LD, Robinson RC (November 2013). "The expanding superfamily of gelsolin homology domain proteins". Cytoskeleton. 70 (11): 775–95. doi:10.1002/cm.21149. PMID 24155256. S2CID 205643538.

[Sun-5] Sun HQ, Yamamoto M, Mejillano M, Yin HL (November 1999). "Gelsolin, a multifunctional actin regulatory protein". The Journal of Biological Chemistry. 274 (47): 33179–82. doi:10.1074/jbc.274.47.33179. PMID 10559185.

[Koya-6] Koya RC, Fujita H, Shimizu S, Ohtsu M, Takimoto M, Tsujimoto Y, Kuzumaki N (May 2000). "Gelsolin inhibits apoptosis by blocking mitochondrial membrane potential loss and cytochrome c release". The Journal of Biological Chemistry. 275 (20): 15343–9. doi:10.1074/jbc.275.20.15343. hdl:2115/718. PMID 10809769.

[Kwiatkowski1986-7] Kwiatkowski DJ, Stossel TP, Orkin SH, Mole JE, Colten HR, Yin HL (1986-10-02). "Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain". Nature. 323 (6087): 455–8. Bibcode:1986Natur.323..455K. doi:10.1038/323455a0. PMID 3020431. S2CID 4356162.

[Nag2013Gymnast-8] Nag S, Larsson M, Robinson RC, Burtnick LD (July 2013). "Gelsolin: the tail of a molecular gymnast". Cytoskeleton. 70 (7): 360–84. doi:10.1002/cm.21117. PMID 23749648. S2CID 23646422.

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