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Article

WW domains 2 and 3 of Rsp5p play overlapping roles in binding to the LPKY motif of Spt23p and Mga2p.

The international journal of biochemistry & cell biology - 1 Jan 2008

Bhattacharya Sabyasachi, Zoladek Teresa, Haines Dale S

Abstract excerpt

Rsp5p of Saccharomyces cerevisiae is a member of the C2-WW-HECT family of ubiquitin ligases and it interacts with targets via its WW domains. Spt23p and Mga2p are Rsp5p substrates and Rsp5p activates the OLE1 inducing functions of these membrane-localized transcription factors by ubiquitination. Although it is known that Rsp5p binds Mga2p and Spt23p via an imperfect WW domain-binding site (LPKY) that is located...

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Identifiers

PMID: 17719829
DOI: 10.1016/j.biocel.2007.07.007
PMCID: PMC2129131

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WW domains 2 and 3 of Rsp5p play overlapping roles in binding to the LPKY motif of Spt23p and Mga2p.PMID 17719829Read ↗

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