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MBC in Press, published online ahead of print September 26, 2007
Mol. Biol. Cell 10.1091/mbc.E07-06-0607

A more recent version of this article appeared on December 1, 2007
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Submitted on June 26, 2007
Revised on September 5, 2007
Accepted on September 13, 2007

Scd5p Mediates Phosphoregulation of Actin and Endocytosis by the Type 1 Phosphatase Glc7p in Yeast

Guisheng Zeng,* Bo Huang,* Suat Peng Neo, Junxia Wang, and Mingjie Cai

Institute of Molecular and Cell Biology, Singapore 138673, Republic of Singapore

Monitoring Editor: Sandra Schmid

Pan1p plays essential roles in both actin and endocytosis in yeast. It interacts with, and regulates the function of, multiple endocytic proteins and actin assembly machinery. Phosphorylation of Pan1p by the kinase Prk1p down-regulates its activity, resulting in disassembly of the endocytic vesicle coat complex and termination of vesicle-associated actin polymerization. In this study, we focus on the mechanism that acts to release Pan1p from phosphorylation inhibition. We show that Pan1p is dephosphorylated by the phosphatase Glc7p, and the dephosphorylation is dependent on the Glc7p-targeting protein Scd5p, which itself is a phosphorylation target of Prk1p. Scd5p links Glc7p to Pan1p in two ways: directly by interacting with Pan1p and indirectly by interacting with the Pan1p-binding protein End3p. Depletion of Glc7p from the cells causes defects in cell growth, actin organization and endocytosis, all of which can be partially suppressed by deletion of the PRK1 gene. These results suggest that Glc7p antagonizes the activity of the Prk1p kinase in regulating the functions of Pan1p and possibly other actin- and endocytosis-related proteins.

*These authors contributed equally to this work.

Address correspondence to: Mingjie Cai (mcbcaimj{at}imcb.a-star.edu.sg)






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