Eap45 in mammalian ESCRT-II binds ubiquitin via a phosphoinositide- interacting GLUE domain

Journal of Biological Chemistry

Volumn 280, Issue 20, 2005, Pages 19600-19606

  Slagsvold, Thomas ^a   Aasland, Rein ^b   Hirano, Satoshi ^c   Bache, Kristi G ^a   Raiborg, Camilla ^a   Trambaiolo, Daniel ^c   Wakatsuki, Soichi ^c   Stenmark, Harald ^a  

^a OSLO UNIVERSITY HOSPITAL   (Norway)

^b UNIVERSITY OF BERGEN   (Norway)

^c INSTITUTE OF MATERIALS STRUCTURE SCIENCE   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

BIODEGRADATION; BIOLOGICAL MEMBRANES; LIVING SYSTEMS STUDIES; YEAST;

ENDOCYTIC ROUTE; ENDOSOMES; ESCRT-II; LYSOMAL DEGRADATION;

PROTEINS;

BINDING PROTEIN; EAP45 PROTEIN; FUNGAL PROTEIN; MEMBRANE PROTEIN; PHOSPHATIDYLINOSITIDE; RECEPTOR; UBIQUITIN; UNCLASSIFIED DRUG; VPS36 PROTEIN; CARRIER PROTEIN; DNA BINDING PROTEIN; MULTIPROTEIN COMPLEX; RECOMBINANT PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN; TRANSCRIPTION FACTOR; VPS36 PROTEIN, S CEREVISIAE;

AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; ENDOCYTOSIS; ENDOSOME; GLUE DOMAIN; HUMAN; HUMAN CELL; LYSOSOME; MAMMAL; MOLECULAR RECOGNITION; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN TARGETING; SIGNAL TRANSDUCTION; UBIQUITINATION; YEAST; ANIMAL; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; HELA CELL; IN VITRO STUDY; METABOLISM; MOLECULAR GENETICS; MOUSE; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY;

MAMMALIA;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CARRIER PROTEINS; DNA-BINDING PROTEINS; ENDOSOMES; HELA CELLS; HUMANS; MEMBRANE TRANSPORT PROTEINS; MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MULTIPROTEIN COMPLEXES; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; TRANSCRIPTION FACTORS; UBIQUITIN;

EID: 19944419643     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M501510200     Document Type: Article

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