Activation of human VPS4A by ESCRT-III proteins reveals ability of substrates to relieve enzyme autoinhibition

Journal of Biological Chemistry

Volumn 285, Issue 46, 2010, Pages 35428-35438

  Merrill, Samuel A ^a   Hanson, Phyllis I ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ATP HYDROLYSIS; ATP-ASE ACTIVITY; ATPASES; AUTOINHIBITION; C-TERMINAL FRAGMENTS; HETEROPOLYMERS; N-TERMINALS; NITRILOTRIACETIC ACID; SUBUNIT INTERACTIONS; VIRAL PARTICLES;

AMINO ACIDS; HYDROLYSIS; LIPOSOMES; OLIGOMERS; PHOSPHOLIPIDS;

ENZYMES;

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; AMINO ACID; CELL MEMBRANE PROTEIN; HISTAMINE; LIPID; LIPOSOME; NITRILOTRIACETATE NICKEL; OLIGOMER; PROTEIN CHMP1B; PROTEIN CHMP2A; PROTEIN CHMP3; PROTEIN CHMP4A; PROTEIN CHMP5; PROTEIN CHMP6; PROTEIN ESCRT III; PROTEIN VPS4A; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME SUBSTRATE COMPLEX; HUMAN; HUMAN CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DOMAIN; PROTEIN HYDROLYSIS; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; REGULATORY MECHANISM;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BINDING SITES; ENDOSOMAL SORTING COMPLEXES REQUIRED FOR TRANSPORT; ENZYME ACTIVATION; HISTIDINE; HUMANS; HYDROLYSIS; LIPOSOMES; MOLECULAR SEQUENCE DATA; MUTATION; NITRILOTRIACETIC ACID; ORGANOMETALLIC COMPOUNDS; PROTEIN BINDING; PROTEIN MULTIMERIZATION; SUBSTRATE SPECIFICITY;

EID: 78149276258     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.126318     Document Type: Article

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