Vps27-Hse1 and ESCRT-I complexes cooperate to increase efficiency of sorting ubiquitinated proteins at the endosome

Journal of Cell Biology

Volumn 163, Issue 2, 2003, Pages 237-243

  Bilodeau, Patricia S ^a   Winistorfer, Stanley C ^a   Kearney, William R ^b   Robertson, Andrew D ^a   Piper, Robert C ^a,b  

^a UNIVERSITY OF IOWA   (United States)

^b UNIVERSITY OF IOWA   (United States)

Author keywords

Endosome; Lysosome; Multivesicular body; Ubiquitin

Indexed keywords

ESCRT I PROTEIN; HSE1 PROTEIN; PROTEIN; UBIQUITIN; UNCLASSIFIED DRUG; VPS23 PROTEIN; VPS27 PROTEIN;

ARTICLE; BINDING SITE; COMPLEX FORMATION; ENDOSOME; IMMUNOPRECIPITATION; ISOTOPE LABELING; LYSOSOME; MUTAGENESIS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PLASMID; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN MOTIF; PROTEIN TARGETING;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BINDING SITES; CARRIER PROTEINS; CELLS, CULTURED; CONSERVED SEQUENCE; ENDOSOMES; FUNGAL PROTEINS; LYSOSOMES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PEPTIDES; PROTEIN STRUCTURE, TERTIARY; PROTEIN TRANSPORT; RECEPTORS, CYTOPLASMIC AND NUCLEAR; RECOMBINANT FUSION PROTEINS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SEQUENCE DELETION; SEQUENCE HOMOLOGY, AMINO ACID; TRANSPORT VESICLES; UBIQUITIN; VESICULAR TRANSPORT PROTEINS;

EID: 0242266922     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.200305007     Document Type: Article

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