Channel function is dissociated from the intrinsic kinase activity and autophosphorylation of TRPMT/ChaK1

Journal of Biological Chemistry

Volumn 280, Issue 21, 2005, Pages 20793-20803

  Matsushita, Masayuki ^a   Kozak, J Ashot ^d   Shimizu, Yoshio ^c   McLachlin, Derek T ^c   Yamaguchi, Hiroto ^b   Wei, Fan Yan ^a   Tomizawa, Kazuhito ^a   Matsui, Hideki ^a   Chait, Brian T ^c   Cahalan, Michael D ^d   Nairn, Angus C ^c,e  

^a OKAYAMA UNIVERSITY MEDICAL SCHOOL   (Japan)

^b NARA INSTITUTE OF SCIENCE AND TECHNOLOGY   (Japan)

^c ROCKEFELLER UNIVERSITY   (United States)

^d UNIVERSITY OF CALIFORNIA   (United States)

^e YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; ENZYME INHIBITION; MASS SPECTROMETRY; POSITIVE IONS;

CHANNEL FUNCTIONS; KINASE ACTIVITY; PHOSPHORYLATION; TRANSMEMBRANE SEGMENTS;

ENZYMES;

CALCIUM ION; CATION CHANNEL; MAGNESIUM ION; PHOSPHOTRANSFERASE; PROTEIN CHAK1; PROTEIN SERINE THREONINE KINASE; PROTEIN TRPM7; SERINE; UNCLASSIFIED DRUG; ZINC ION;

ANIMAL CELL; ARTICLE; AUTOPHOSPHORYLATION; CALCIUM TRANSPORT; CARBOXY TERMINAL SEQUENCE; CELLULAR DISTRIBUTION; CONTROLLED STUDY; DISSOCIATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; HUMAN; HUMAN CELL; IN VITRO STUDY; MASS SPECTROMETRY; MEMBRANE CHANNEL; MUTANT; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; REGULATORY MECHANISM; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CALCIUM; CATIONS, DIVALENT; CELL LINE; CRYSTALLIZATION; ELECTRIC CONDUCTIVITY; ESCHERICHIA COLI; GENE EXPRESSION; ION CHANNELS; MAGNESIUM; MASS SPECTROMETRY; MEMBRANE PROTEINS; MICE; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PATCH-CLAMP TECHNIQUES; PHOSPHORYLATION; PROTEIN KINASES; RECOMBINANT FUSION PROTEINS; SPODOPTERA; STRUCTURE-ACTIVITY RELATIONSHIP; TRPM CATION CHANNELS; ZINC;

EID: 20144366217     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M413671200     Document Type: Article

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