Phosphoinositide binding to the substrate regulates susceptibility to proteolysis by calpain

Journal of Biological Chemistry

Volumn 283, Issue 14, 2008, Pages 9217-9223

  Sprague, Chelsea R ^a   Fraley, Tamara S ^a   Hyo, Sang Jang ^a   Lal, Sangeet ^a   Greenwood, Jeffrey A ^a  

^a OREGON STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTINIDES; CALCIUM; CALCIUM ALLOYS; CELL CULTURE; PROTEINS; SUBSTRATES;

ADHESION PROTEINS; BREAKDOWN PRODUCTS; CALCIUM IONOPHORES; CALPAIN; CALPAIN ACTIVITIES; CALPAINS; CALPONIN HOMOLOGIES; CLEAVAGE SITES; CRITICAL DETERMINANTS; CYTOSKELETAL; CYTOSKELETAL DYNAMICS; CYTOSKELETAL PROTEINS; CYTOSKELETAL STRUCTURES; DIPHOSPHATE; DO-MAINS; ELEVATED LEVELS; EMBRYONIC FIBROBLASTS; GLIOBLASTOMA CELLS; HIGHLY SENSITIVES; PATHOLOGICAL CONDITIONS; PHOSPHATIDYLINOSITOL; PHOSPHOINOSITIDE BINDINGS; POTENTIAL MECHANISMS; SUBSTRATE RECOGNITIONS; TRIS PHOSPHATES;

BINDING SITES;

ALPHA ACTININ; CALCIUM IONOPHORE; CALPAIN; CALPAIN 1; CALPAIN 2; CYTOSKELETON PROTEIN; PHOSPHATIDYLINOSITIDE; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; ACTIN; ACTININ; CALCIUM; PHOSPHATIDYLINOSITOL 3,4,5-TRIPHOSPHATE; POLYPHOSPHOINOSITIDE;

ADHESION; ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; CONTROLLED STUDY; EMBRYO; FIBROBLAST; GLIOBLASTOMA; GLIOMA CELL; HUMAN; HUMAN CELL; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CLEAVAGE; PROTEIN DEGRADATION; RAT; REGULATORY MECHANISM; SEQUENCE HOMOLOGY; ANIMAL; CYTOLOGY; CYTOSKELETON; DRUG ANTAGONISM; EMBRYO (ANATOMY); ENZYME SPECIFICITY; METABOLISM; PATHOLOGY; PHYSIOLOGY; PROTEIN TERTIARY STRUCTURE; TUMOR CELL LINE;

RATTUS;

ACTININ; ACTINS; ANIMALS; CALCIUM; CALPAIN; CELL LINE, TUMOR; CYTOSKELETON; EMBRYO, MAMMALIAN; FIBROBLASTS; PHOSPHATIDYLINOSITOL 4,5-DIPHOSPHATE; PHOSPHATIDYLINOSITOL PHOSPHATES; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RATS; SUBSTRATE SPECIFICITY;

EID: 44049089012     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M707436200     Document Type: Article

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