pICln binds to a mammalian homolog of a yeast protein involved in regulation of cell morphology

Grigory Krapivinsky, William Pu, Kevin Wickman, Luba Krapivinsky, David E. Clapham

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56 Scopus citations

Abstract

Since its cloning and tentative identification as a chloride channel, the function of the pICln protein has been debated. Although there is no consensus regarding the specific function of pICln, it was suggested to play a role, directly or indirectly, in the function of a swelling-induced chloride conductance. Previously, the protein was shown to exist in several discrete protein complexes. To determine the function of the protein, we have begun the systematic identification of all proteins to which it binds. Here we show that four proteins firmly bind to pICln and identify the 72-kDa pICln-binding protein by affinity purification and peptide micro-sequencing. The interaction between this protein and pICln was verified several ways, including the extraction of several pICln clones from a cDNA library using the 72-kDa protein as a bait in a yeast two-hybrid screen. The protein is homologous to the yeast Skb1 protein. Skb1 interacts with Shk1, a homolog of the p21(Cdc42/Rac)-activated protein kinases (PAKs). The known involvement of PAKs in cytoskeletal rearrangement suggests that pICln may be linked to a system regulating cell morphology.

Original languageEnglish (US)
Pages (from-to)10811-10814
Number of pages4
JournalJournal of Biological Chemistry
Volume273
Issue number18
DOIs
StatePublished - May 1 1998

Bibliographical note

Copyright:
Copyright 2007 Elsevier B.V., All rights reserved.

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