Phosphorylation of the Cav3.2 T-type calcium channel directly regulates its gating properties

Proceedings of the National Academy of Sciences of the United States of America

Volumn 112, Issue 44, 2015, Pages 13705-13710

  Blesneac, Iulia ^a,b,c   Chemin, Jean ^a,b,c   Bidaud, Isabelle ^a,b,c   Huc Brandt, Sylvaine ^a,b,d   Vandermoere, Franck ^a,b   Lory, Philippe ^a,b,c  

^a UNIV MONTPELLIER   (France)

^b INSERM   (France)

^c Laboratory of Excellence in Ion Channel Science and Therapeutics   (France)

^d UNIVERSITÉ DE MONTPELLIER   (France)

Author keywords

Cav3.2 subunit; Mass spectrometry; Patch clamp; Phosphorylation; T type calcium channel

Indexed keywords

ALKALINE PHOSPHATASE; CALCIUM CHANNEL T TYPE; T TYPE CALCIUM CHANNEL CAV3.2; UNCLASSIFIED DRUG; CACNA1H PROTEIN, HUMAN;

ANIMAL TISSUE; ARTICLE; CHANNEL GATING; CONTROLLED STUDY; GENE LOCUS; HUMAN; HUMAN CELL; IN VIVO STUDY; MASS SPECTROMETRY; NONHUMAN; PATCH CLAMP TECHNIQUE; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; RAT; REGULATORY MECHANISM; HEK293 CELL LINE; METABOLISM; PHOSPHORYLATION; PHYSIOLOGY;

CALCIUM CHANNELS, T-TYPE; HEK293 CELLS; HUMANS; ION CHANNEL GATING; PATCH-CLAMP TECHNIQUES; PHOSPHORYLATION;

EID: 84946595518     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1511740112     Document Type: Article

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