Dimerization of substrate adaptors can facilitate Cullin-mediated ubiquitylation of proteins by a "tethering" mechanism: A two-site interaction model for the Nrf2-Keap1 complex

Journal of Biological Chemistry

Volumn 281, Issue 34, 2006, Pages 24756-24768

  McMahon, Michael ^a   Thomas, Nerys ^a   Itoh, Ken ^b   Yamamoto, Masayuki ^b   Hayes, John D ^a  

^a UNIVERSITY OF DUNDEE   (United Kingdom)

^b UNIVERSITY OF TSUKUBA   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL BONDS; CONCENTRATION (PROCESS); DIMERS; SUBSTRATES;

HOMODIMERS; TWO-SITE INTERACTION MODEL; UBIQUITIN LIGASES;

PROTEINS;

ADAPTOR PROTEIN; CULLIN; HOMODIMER; LYSINE; PROTEIN CULLIN 3; PROTEIN KEAP1; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR NEH2; TRANSCRIPTION FACTOR NRF2; UBIQUITIN; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; BINDING SITE; COMPLEX FORMATION; CONTROLLED STUDY; DIMERIZATION; ENZYME SUBSTRATE; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; UBIQUITINATION;

ADAPTOR PROTEINS, SIGNAL TRANSDUCING; AMINO ACID SEQUENCE; ANIMALS; CARRIER PROTEINS; CELL CYCLE PROTEINS; CULLIN PROTEINS; CYTOSKELETAL PROTEINS; DIMERIZATION; MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NF-E2-RELATED FACTOR 2; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ANALYSIS;

EID: 33747728194     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M601119200     Document Type: Article

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