Filamine A

FLNA
Structures disponibles
PDB	Recherche d'orthologue : PDBe RCSB
Identifiants PDB
	2AAV, 2BP3, 2BRQ, 2J3S, 2JF1, 2K3T, 2K7P, 2MTP, 2W0P, 2WFN, 3CNK, 3HOC, 3HOP, 3HOR, 3ISW, 3RGH, 4M9P, 4P3W
Identifiants
Alias	FLNA
IDs externes	OMIM: 300017 MGI: 95556 HomoloGene: 1119 GeneCards: FLNA
Position du gène (humain)
Chr.	Chromosome X
Fin	154,374,634 bp
Position du gène (souris)
Chr.	X chromosome (souris)
Fin	73,293,426 bp
Expression génique
	Fortement exprimé dans
	artère coronaire droite; ; artère poplitée; ; Tibial arteries; ; aorte ascendante; ; Descending thoracic aorta; ; body of uterus; ; Veine saphène; ; muqueuse gastrique; ; artère coronaire gauche; ; muscle layer of sigmoid colon;
	Fortement exprimé dans
	tunica media of zone of aorta; ; granulocyte; ; aorte ascendante; ; utérus; ; col de l'utérus; ; cordon ombilical; ; artère carotide externe; ; valve aortique; ; artère carotide interne; ; tail of embryo;
	Plus de données d'expression de référence
	; ; ; ;
	Plus de données d'expression de référence
Gene Ontology
Fonction moléculaire	protein homodimerization activity; liaison de complexe macromoléculaire; transcription factor binding; mu-type opioid receptor binding; signal transducer activity; actin filament binding; small GTPase binding; liaison de kinase; actin binding; SMAD binding; Fc-gamma receptor I complex binding; G protein-coupled receptor binding; liaison de GTPase; liaison ARN; potassium channel regulator activity; transmembrane transporter binding; cadherin binding; liaison protéique;
Composant cellulaire	cytoplasme; membrane; focal adhesion; cortical cytoskeleton; membrane plasmique; Myb complex; dendritic shaft; région extracellulaire; soma; cortex cellulaire; nucléole; filament d'actine; actin cytosquelette; perinuclear region of cytoplasm; exosome; cytosquelette; noyau; apical dendrite; filamentous actin; matrice extracellulaire; jonction cellule-cellule; cytosol; Z discdkac;
Processus biologique	actin cytoskeleton reorganization; negative regulation of transcription by RNA polymerase I; negative regulation of protein catabolic process; establishment of protein localization; protein stabilization; platelet degranulation; mRNA transcription by RNA polymerase II; negative regulation of apoptotic process; receptor clustering; negative regulation of DNA-binding transcription factor activity; cytoplasmic sequestering of protein; platelet activation; mitotic spindle assembly; positive regulation of substrate adhesion-dependent cell spreading; protein localization to cell surface; organisation de la projection de cellules; adenylate cyclase-inhibiting dopamine receptor signaling pathway; actin crosslink formation; positive regulation of I-kappaB kinase/NF-kappaB signaling; positive regulation of integrin-mediated signaling pathway; Agrégation plaquettaire; cell junction assembly; regulation of cell migration; wound healing, spreading of cells; semaphorin-plexin signaling pathway; formation of radial glial scaffolds; développement du cortex cérébral; cilium assembly; protein localization to plasma membrane; positive regulation of potassium ion transmembrane transport; regulation of membrane repolarization during atrial cardiac muscle cell action potential; regulation of membrane repolarization during cardiac muscle cell action potential; positive regulation of neural precursor cell proliferation; positive regulation of neuron migration;
	Sources:Amigo / QuickGO
Orthologues
	2316
	192176
	ENSG00000196924
	ENSMUSG00000031328
	P21333
	Q8BTM8
	NM_001110556; NM_001456
	NM_001290421; NM_010227
	NP_001104026; NP_001447
	NP_001277350; NP_034357; NP_001390993
	Wikidata
Voir/Editer Humain	Voir/Editer Souris

La filamine A est la principale isoforme des filamines, protéines se fixant sur l'actine et stabilisant la structure tridimensionnelle de cette dernière. Son gène est le FLNA situé sur le chromosome X humain.

Rôles

Outre son rôle de stabilisation de l'actine, elle intervient dans les jonctions intercellulaires et dans la fonction endothéliale.

Elle interagit avec le HIF-1α (« hypoxia-inducible factor-1α ») en cas d'hypoxie.

Génétique

La mutation de son gène est retrouvée dans plusieurs syndromes malformatifs :

le syndrome oto-palato-digital de type I et II ;
la dysplasie frontométaphysaire ;
le syndrome de Melnick-Needles ;
l'hétérotopie nodulaire héréditaire liée à l'X.

Elle peut également causer une valvulopathie cardiaque ou une thrombopénie isolée.

Notes et références

1 2 3 GRCh38: Ensembl release 89: ENSG00000196924 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000031328 - Ensembl, May 2017
↑ « Publications PubMed pour l'Homme », sur National Center for Biotechnology Information, U.S. National Library of Medicine
↑ « Publications PubMed pour la Souris », sur National Center for Biotechnology Information, U.S. National Library of Medicine
↑ Feng YY, Chen MH, Moskowitz IP et al. Filamin A (flna) is required for cell-cell contact in vascular development and cardiac morphogenesis, Proc Natl Acad Sci USA, 2006;103:19836-19841
↑ Bandaru S, Grönros J, Redfors B et al. Deficiency of filamin A in endothelial cells impairs left ventricular remodelling after myocardial infarction, Cardiovasc Res, 2015;105:151-159
↑ Zheng X, Zhou X, Rouhi P et al. Hypoxia-induced and calpain-dependent cleavage of filamin A regulates the hypoxic response, Proc Natl Acad Sci USA, 2014;111:2560-2565
↑ Robertson SP, Twigg SR, Sutherland-Smith AJ et al. Localized mutations in the gene encoding the cytoskeletal protein filamin A cause diverse malformations in humans, Nature Gen, 2003;33:487-491
↑ Kyndt F, Gueffet JP, Probst V et el. Mutations in the gene encoding filamin A as a cause for familial cardiac valvular dystrophy, Circulation, 2007;115:40-49
↑ Nurden P, Debili N, Coupry I et al. Thrombocytopenia resulting from mutations in filamin A can be expressed as an isolated syndrome, Blood, 2011;118:5928–5937

Portail de la médecine

Portail de la biologie cellulaire et moléculaire

[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000196924 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000031328 - Ensembl, May 2017

[3] « Publications PubMed pour l'Homme », sur National Center for Biotechnology Information, U.S. National Library of Medicine

[4] « Publications PubMed pour la Souris », sur National Center for Biotechnology Information, U.S. National Library of Medicine

[5] Feng YY, Chen MH, Moskowitz IP et al. Filamin A (flna) is required for cell-cell contact in vascular development and cardiac morphogenesis, Proc Natl Acad Sci USA, 2006;103:19836-19841

[6] Bandaru S, Grönros J, Redfors B et al. Deficiency of filamin A in endothelial cells impairs left ventricular remodelling after myocardial infarction, Cardiovasc Res, 2015;105:151-159

[7] Zheng X, Zhou X, Rouhi P et al. Hypoxia-induced and calpain-dependent cleavage of filamin A regulates the hypoxic response, Proc Natl Acad Sci USA, 2014;111:2560-2565

[8] Robertson SP, Twigg SR, Sutherland-Smith AJ et al. Localized mutations in the gene encoding the cytoskeletal protein filamin A cause diverse malformations in humans, Nature Gen, 2003;33:487-491

[9] Kyndt F, Gueffet JP, Probst V et el. Mutations in the gene encoding filamin A as a cause for familial cardiac valvular dystrophy, Circulation, 2007;115:40-49

[10] Nurden P, Debili N, Coupry I et al. Thrombocytopenia resulting from mutations in filamin A can be expressed as an isolated syndrome, Blood, 2011;118:5928–5937