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J. Biol. Chem., Vol. 277, Issue 50, 48002-48008, December 13, 2002
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From the SCD5, an essential gene, encodes a
protein important for endocytosis and actin organization in yeast.
Previous two-hybrid screens showed that Scd5p interacts with Glc7p, a
yeast Ser/Thr-specific protein phosphatase-1 (PP1) that participates in
a variety of cellular processes. PP1 substrate specificity in
vivo is regulated by association with different regulatory or
targeting subunits, many of which have a consensus PP1-binding site
((V/I)XF, with a basic residue at the
Protein Phosphatase-1 Binding to Scd5p Is Important for
Regulation of Actin Organization and Endocytosis in Yeast*
,§,
Department of Molecular Biology and
Microbiology, Case Western Reserve University,
Cleveland, Ohio 44106-4960 and ¶ Biochemie-Zentrum, University
of Heidelberg, Im Neuenheimer Feld 328, 69120 Heidelberg, Germany
1 or 2 position).
Scd5p contains two of these potential PP1-binding motifs: KVDF (amino
acids 240-243) and KKVRF (amino acids 272-276). Deletion analysis
mapped the PP1-binding domain to a region of Scd5p containing these
motifs. Therefore, the consequence of mutating these two potential
PP1-binding sites was examined. Although mutation of KVDF had no
effect, alteration of KKVRF dramatically reduced Scd5p interaction with
Glc7p and resulted in temperature-sensitive growth. Furthermore, this
mutation caused defects in fluid phase and receptor-mediated
endocytosis and actin organization. Overexpression of GLC7
suppressed the temperature-sensitive growth of the KKVRF mutant and
partially rescued the actin organization phenotype. These results
provide evidence that Scd5p is a PP1 targeting subunit for regulation of actin organization and endocytosis or that Scd5p is a PP1 substrate, which regulates the function of Scd5p in these processes.
*
This work was supported in part by National Institutes of
Health Grant R01 GM55796 (to S. K. L.) and the Deutsche
Forshungsgemeinschaft Project SFB 352 (to M. G.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of
Molecular Biology and Microbiology, Case Western Reserve University, 10900 Euclid Ave., Cleveland, OH 44106-4960. Tel.: 216-368-6279; Fax:
216-368-3055; E-mail: skl@po.cwru.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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