Autolytic activity of human calpain 7 is enhanced by ESCRT-III-related protein IST1 through MIT-MIM interaction

FEBS Journal

Volumn 277, Issue 21, 2010, Pages 4412-4426

  Osako, Yohei ^a   Maemoto, Yuki ^a   Tanaka, Ryohei ^a   Suzuki, Hironori ^a   Shibata, Hideki ^a   Maki, Masatoshi ^a  

^a NAGOYA UNIVERSITY   (Japan)

Author keywords

Calpain 7; ESCRT III; IST1; Microtubuleinteracting and transport (MIT); Proteolysis

Indexed keywords

CALPAIN; CALPAIN 7; CARRIER PROTEIN; EPITOPE; ESCRT III PROTEIN; ESCRT PROTEIN; GLUTATHIONE TRANSFERASE; GREEN FLUORESCENT PROTEIN; INCREASED SODIUM TOLERANCE 1 PROTEIN; MICROTUBULE INTERACTING AND TRANSPORT INTERACTING MOTIF 1; MICROTUBULE INTERACTING AND TRANSPORT INTERACTING MOTIF 2; MICROTUBULE INTERACTING AND TRANSPORT PROTEIN; MICROTUBULE PROTEIN; MONOMERIC GREEN FLUORESCENT PROTEIN; UNCLASSIFIED DRUG; CAPN7 PROTEIN, HUMAN; CYSTEINE PROTEINASE INHIBITOR; DRUG DERIVATIVE; HYBRID PROTEIN; LEUCINE; LEUPEPTIN; N [N (3 CARBOXYOXIRANE 2 CARBONYL)LEUCYL]AGMATINE; N ETHYLMALEIMIDE; OLC1 PROTEIN, HUMAN; ONCOPROTEIN;

ARTICLE; AUTOLYSIS; CELL STRAIN HEK293; CONTROLLED STUDY; GENE MUTATION; HUMAN; IMMUNOPRECIPITATION; IN VITRO STUDY; IN VIVO STUDY; MAMMAL CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CLEAVAGE; PROTEIN DEGRADATION; PROTEIN PROTEIN INTERACTION; AMINO ACID SEQUENCE; BINDING SITE; BIOCATALYSIS; DRUG ANTAGONISM; DRUG EFFECT; ENZYME ACTIVE SITE; GENETIC TRANSFECTION; GENETICS; HYDROLYSIS; METABOLISM; MUTATION; PROTEIN BINDING; PROTEIN MOTIF; WESTERN BLOTTING;

MAMMALIA;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BINDING SITES; BIOCATALYSIS; BLOTTING, WESTERN; CALPAIN; CATALYTIC DOMAIN; CYSTEINE PROTEINASE INHIBITORS; ENDOSOMAL SORTING COMPLEXES REQUIRED FOR TRANSPORT; ETHYLMALEIMIDE; GLUTATHIONE TRANSFERASE; GREEN FLUORESCENT PROTEINS; HEK293 CELLS; HUMANS; HYDROLYSIS; IMMUNOPRECIPITATION; LEUCINE; LEUPEPTINS; MUTATION; ONCOGENE PROTEINS; PROTEIN BINDING; RECOMBINANT FUSION PROTEINS; TRANSFECTION;

EID: 79952112344     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2010.07822.x     Document Type: Article

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