ER-localized bestrophin 1 activates Ca2+-dependent ion channels TMEM16A and SK4 possibly by acting as a counterion channel

Pflugers Archiv European Journal of Physiology

Volumn 459, Issue 3, 2010, Pages 485-497

  Barro Soria, René ^a   Aldehni, Fadi ^a   Almaça, Joana ^a   Witzgall, Ralph ^a   Schreiber, Rainer ^a   Kunzelmann, Karl ^a  

^a UNIVERSITY OF REGENSBURG   (Germany)

Author keywords

Bestrophin; Ca 2+ activated K+ currents; Ca2+ store; Ca2+ activated Cl currents; CaCC; ER; Pak2; Purinergic receptors endoplasmic reticulum; SK4; TMEM16A

Indexed keywords

BESTROPHIN 1; CALCIUM CHANNEL; CALCIUM ION; CELL PROTEIN; COUNTERION; INOSITOL TRISPHOSPHATE; P21 ACTIVATED KINASE 2; PROTEIN SK4; PROTEIN TMEM16A; PURINERGIC P2Y2 RECEPTOR; UNCLASSIFIED DRUG; ANO1 PROTEIN, HUMAN; BEST1 PROTEIN, HUMAN; CALCIUM; CHLORIDE CHANNEL; EYE PROTEIN; INTERMEDIATE CONDUCTANCE CALCIUM ACTIVATED POTASSIUM CHANNEL; KCNN4 PROTEIN, HUMAN; MEMBRANE PROTEIN; P21 ACTIVATED KINASE; PURINERGIC P2 RECEPTOR; TUMOR PROTEIN; VMD2 PROTEIN, MOUSE;

ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; CALCIUM CELL LEVEL; CALCIUM SIGNALING; CALCIUM TRANSPORT; CELL STRAIN HEK293; CONTROLLED STUDY; CYSTIC FIBROSIS; DYSTROPHY; EMBRYO; ENDOPLASMIC RETICULUM; ENDOTHELIUM CELL; HUMAN; HUMAN CELL; INFLAMMATORY DISEASE; MEMBRANE POTENTIAL; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; RESPIRATORY EPITHELIUM; RETINA MACULOPATHY; ANIMAL; CELL LINE; CYTOLOGY; GENETICS; METABOLISM; MOUSE; MOUSE MUTANT; OOCYTE; PATCH CLAMP; PHYSIOLOGY; RETINA MACULA DEGENERATION; RNA INTERFERENCE; ULTRASTRUCTURE; XENOPUS LAEVIS;

ANIMALS; CALCIUM; CALCIUM SIGNALING; CELL LINE; CHLORIDE CHANNELS; ENDOPLASMIC RETICULUM; EYE PROTEINS; HUMANS; INTERMEDIATE-CONDUCTANCE CALCIUM-ACTIVATED POTASSIUM CHANNELS; MACULAR DEGENERATION; MEMBRANE PROTEINS; MICE; MICE, KNOCKOUT; NEOPLASM PROTEINS; OOCYTES; P21-ACTIVATED KINASES; PATCH-CLAMP TECHNIQUES; RECEPTORS, PURINERGIC P2; RNA INTERFERENCE; XENOPUS LAEVIS;

EID: 77949884841     PISSN: 00316768     EISSN: 14322013     Source Type: Journal    
DOI: 10.1007/s00424-009-0745-0     Document Type: Article

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