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Vol. 12, Issue 12, 3759-3772, December 2001
Institute of Molecular and Cell Biology, National University of
Singapore, Singapore, 117609
The serine/threonine kinase Prk1p is known to be involved in the
regulation of the actin cytoskeleton organization in budding yeast. One
possible function of Prk1p is the negative regulation of Pan1p, an
actin patch regulatory protein that forms a complex in vivo with at
least two other proteins, Sla1p and End3p. In this report, we
identified Sla1p as another substrate for Prk1p. The phosphorylation of
Sla1p by Prk1p was established in vitro with the use of
immunoprecipitated Prk1p and in vivo with the use of
PRK1 overexpression, and was further supported by the
finding that immunoprecipitated Sla1p contained PRK1-
and ARK1-dependent kinase activities. Stable complex
formation between Prk1p and Sla1p/Pan1p in vivo could be observed once
the phosphorylation reaction was blocked by mutation in the catalytic
site of Prk1p. Elevation of Prk1p activities in wild-type cells
resulted in a number of deficiencies, including those in colocalization
of Pan1p and Sla1p, endocytosis, and cell wall morphogenesis, likely
attributable to a disintegration of the Pan1p/Sla1p/End3p complex.
These results lend a strong support to the model that the
phosphorylation of the Pan1p/Sla1p/End3p complex by Prk1p is one of the
important mechanisms by which the organization and functions of the
actin cytoskeleton are regulated.
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