The Bcl-2 protein family member bok binds to the coupling domain of inositol 1,4,5-trisphosphate receptors and protects them from proteolytic cleavage

Journal of Biological Chemistry

Volumn 288, Issue 35, 2013, Pages 25340-25349

  Schulman, Jacqualyn J ^a   Wright, Forrest A ^a   Kaufmann, Thomas ^b   Wojcikiewicz, Richard J H ^a  

^a State University of New York Upstate Medical University: College of Medicine   (United States)

^b UNIVERSITY OF BERN   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

BCL-2 PROTEIN FAMILIES; CHANNEL ACTIVITY; NOVEL COMPONENT; PROTEOLYTIC CLEAVAGE; RECEPTOR COMPLEX;

CELL DEATH;

PROTEINS;

CALCIUM CHANNEL; CASPASE 3; CHYMOTRYPSIN; INOSITOL 1,4,5 TRISPHOSPHATE RECEPTOR; PROTEIN BCL 2; PROTEIN BOK; TETRAMER; UNCLASSIFIED DRUG;

ANIMAL CELL; APOPTOSIS; ARTICLE; BINDING SITE; CALCIUM CELL LEVEL; CALCIUM TRANSPORT; CELL MEMBRANE; CELLULAR DISTRIBUTION; COMPLEX FORMATION; CONTROLLED STUDY; CROSS COUPLING REACTION; DOWN REGULATION; EMBRYO; ENDOPLASMIC RETICULUM; HUMAN; HUMAN CELL; IN VITRO STUDY; IN VIVO STUDY; MOLECULAR DOCKING; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; REGULATORY MECHANISM; SIGNAL TRANSDUCTION;

APOPTOSIS; BCL-2 FAMILY PROTEINS; BOK; CASPASE; INOSITOL 1,4,5-TRISPHOSPHATE; INOSITOL 1,4,5-TRISPHOSPHATE RECEPTOR; PROTEOLYSIS; UBIQUITIN;

ANIMALS; APOPTOSIS; CALCIUM; CASPASE 3; CELL LINE, TRANSFORMED; ENDOPLASMIC RETICULUM; HELA CELLS; HUMANS; INOSITOL 1,4,5-TRISPHOSPHATE RECEPTORS; MICE; MICE, KNOCKOUT; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; PROTEOLYSIS; PROTO-ONCOGENE PROTEINS C-BCL-2;

EID: 84883403649     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.496570     Document Type: Article

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