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Article

Multiple interactions drive adaptor-mediated recruitment of the ubiquitin ligase rsp5 to membrane proteins in vivo and in vitro.

Molecular biology of the cell - 1 Jul 2007

Sullivan James A, Lewis Michael J, Nikko Elina, Pelham Hugh R B

Abstract excerpt

Recognition of membrane proteins by the Nedd4/Rsp5 ubiquitin ligase family is a critical step in their targeting to the multivesicular body pathway. Some substrates contain "PY" motifs (PPxY), which bind to WW domains in the ligase. Others lack PY motifs and instead rely on adaptors that recruit the ligase to them. To investigate the mechanism of adaptor-mediated ubiquitination, we have characterized the...

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Share to Adaptor Proteins, Signal Transducing
Share to Amino Acid Motifs

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Endosomal Sorting Complexes Required for Transport

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Source

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Identifiers

PMID: 17429078
DOI: 10.1091/mbc.e07-01-0011
PMCID: PMC1924809

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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Multiple interactions drive adaptor-mediated recruitment of the ubiquitin ligase rsp5 to membrane proteins in vivo and in vitro.PMID 17429078Read ↗

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