Plakophiline 2

PKP2
Structures disponibles
PDB	Recherche d'orthologue: PDBe RCSB
Identifiants PDB
	3TT9,%%s3TT9
Identifiants
Aliases	PKP2
IDs externes	OMIM: 602861 MGI: 1914701 HomoloGene: 3364 GeneCards: PKP2
Position du gène (Homme)
Chr.	Chromosome 12 humain
Fin	32,896,777 bp
Position du gène (Souris)
Chr.	Chromosome 16 (souris)
Fin	16,090,576 bp
Expression génétique
	Fortement exprimé dans
	ventricule droit; ; apex of heart; ; myocardium of left ventricle; ; right uterine tube; ; auricule droit; ; cardiac muscle tissue of right atrium; ; mucosa of colon; ; mucosa of sigmoid colon; ; rectum; ; mucosa of transverse colon;
	Fortement exprimé dans
	Ileal epithelium; ; superior surface of tongue; ; vésicule biliaire; ; valve auriculo-ventriculaire; ; myocardium of ventricle; ; cardiac muscle tissue of left ventricle; ; endocardial cushion; ; atrium; ; Cellule de Paneth; ; epithelium of lens;
	Plus de données d'expression de référence
	; ;
	Plus de données d'expression de référence
Gene Ontology
Fonction moléculaire	sodium channel regulator activity; intermediate filament binding; transmembrane transporter binding; liaison protéique; cell adhesive protein binding involved in bundle of His cell-Purkinje myocyte communication; molecular adaptor activity; alpha-catenin binding; protein kinase C binding; cadherin binding;
Composant cellulaire	integral component of membrane; intercalated disc; jonction cellule-cellule; zonula adherens; membrane plasmique; desmosome; nucléoplasme; jonction cellulaire; Filament intermédiaire; noyau; cornified envelope; messenger ribonucleoprotein complex; cytoplasme;
Processus biologique	intermediate filament bundle assembly; cell communication by electrical coupling involved in cardiac conduction; ventricular cardiac muscle cell action potential; cardiac muscle cell action potential involved in contraction; bundle of His cell-Purkinje myocyte adhesion involved in cell communication; cell-cell signaling involved in cardiac conduction; ventricular cardiac muscle tissue morphogenesis; développement du cœur; desmosome assembly; adhésion cellulaire; positive regulation of sodium ion transport; regulation of heart rate by cardiac conduction; regulation of ventricular cardiac muscle cell action potential; maintenance of animal organ identity; keratinization; cornification; protein localization to plasma membrane; cell-cell adhesion; cell-cell junction assembly; adherens junction maintenance;
	Sources:Amigo / QuickGO
Orthologues
	5318
	67451
	ENSG00000057294
	ENSMUSG00000041957
	Q99959
	Q9CQ73
	NM_004572; NM_001005242
	NM_026163
	NP_001005242; NP_004563
	NP_080439
	Wikidata
Voir/Editer Humain	Voir/Editer Souris

La plakophiline 2 est une protéine constitutive du desmosome. Son gène est le PKL2. La mutation de ce dernier peut entraîner une dysplasie ventriculaire droite arythmogène.

Rôles

Elle régule la concentration cellulaire en connexine 43, une protéine de jonction communicante^[5] en se liant à cette dernière^[6]. Elle interagit également avec l'ankyrine G^[7] ainsi qu'avec des canaux sodiques^[8].

En médecine

La mutation de PKL2 est présente dans plus de la moitié des dysplasies ventriculaires droites arythmogènes familiales mais est absente dans les formes sporadiques^[9]. Elle pourrait également avoir une responsabilité dans le syndrome de Brugada^[10].

Notes et références

↑ ^{a b et c} GRCh38: Ensembl release 89: ENSG00000057294 - Ensembl, May 2017
↑ ^{a b et c} GRCm38: Ensembl release 89: ENSMUSG00000041957 - 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
↑ Oxford EM, Musa H, Maass K, Coombs W, Taffet SM, Delmar M, Connexin43 remodeling caused by inhibition of plakophilin-2 expression in cardiac cells, Circ Res, 2007;101:703–711
↑ Agullo-Pascual E, Reid DA, Keegan S, Sidhu M, Fenyö D, Rothenberg E, Delmar M, Super-resolution fluorescence microscopy of the cardiac connexome reveals plakophilin-2 inside the connexin43 plaque, Cardiovasc Res, 2013;100:231–240
↑ Sato PY, Coombs W, Lin X et al. Interactions between ankyrin-G, Plakophilin-2, and Connexin43 at the cardiac intercalated disc, Circ Res, 2011;109:193–201
↑ Sato PY, Musa H, Coombs W et al. Loss of plakophilin-2 expression leads to decreased sodium current and slower conduction velocity in cultured cardiac myocytes, Circ Res, 2009;105:523–526
↑ van Tintelen JP, Entius MM, Bhuiyan ZA et al. Plakophilin-2 mutations are the major determinant of familial arrhythmogenic right ventricular dysplasia/cardiomyopathy, Circulation, 2006;113:1650–1658
↑ Cerrone M, Lin X, Zhang M et al. Missense mutations in plakophilin-2 cause sodium current deficit and associate With a Brugada syndrome phenotype, Circulation, 2014;129:1092-1103

[refGRCh38Ensembl-1] {a b et c} GRCh38: Ensembl release 89: ENSG00000057294 - Ensembl, May 2017

[refGRCm38Ensembl-2] {a b et c} GRCm38: Ensembl release 89: ENSMUSG00000041957 - 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

[Oxford_2007-5] Oxford EM, Musa H, Maass K, Coombs W, Taffet SM, Delmar M, Connexin43 remodeling caused by inhibition of plakophilin-2 expression in cardiac cells, Circ Res, 2007;101:703–711

[Agullo-Pascual_2013-6] Agullo-Pascual E, Reid DA, Keegan S, Sidhu M, Fenyö D, Rothenberg E, Delmar M, Super-resolution fluorescence microscopy of the cardiac connexome reveals plakophilin-2 inside the connexin43 plaque, Cardiovasc Res, 2013;100:231–240

[Sato_2012-7] Sato PY, Coombs W, Lin X et al. Interactions between ankyrin-G, Plakophilin-2, and Connexin43 at the cardiac intercalated disc, Circ Res, 2011;109:193–201

[Sato_2009-8] Sato PY, Musa H, Coombs W et al. Loss of plakophilin-2 expression leads to decreased sodium current and slower conduction velocity in cultured cardiac myocytes, Circ Res, 2009;105:523–526

[van_Tintelen_2006-9] van Tintelen JP, Entius MM, Bhuiyan ZA et al. Plakophilin-2 mutations are the major determinant of familial arrhythmogenic right ventricular dysplasia/cardiomyopathy, Circulation, 2006;113:1650–1658

[Cerrone_2014-10] Cerrone M, Lin X, Zhang M et al. Missense mutations in plakophilin-2 cause sodium current deficit and associate With a Brugada syndrome phenotype, Circulation, 2014;129:1092-1103

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