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Vol. 13, Issue 8, 2607-2625, August 2002
§
*Department of Molecular Biology and Microbiology and
SCD5 was identified as a multicopy suppressor of
clathrin HC-deficient yeast. SCD5 is essential, but an
scd5-Program in Genetics, Case Western Reserve University,
Cleveland Ohio 44106; and Biozentrum of the University
of Basel, CH-4056 Basel, Switzerland
338 mutant, expressing Scd5p with a C-terminal
truncation of 338 amino acids, is temperature sensitive for growth.
Further studies here demonstrate that scd5-338
affects receptor-mediated and fluid-phase endocytosis and normal actin
organization. The scd5-338 mutant contains larger and
depolarized cortical actin patches and a prevalence of G-actin bars.
scd5-338 also displays synthetic negative genetic
interactions with mutations in several other proteins important for
cortical actin organization and endocytosis. Moreover, Scd5p
colocalizes with cortical actin. Analysis has revealed that
clathrin-deficient yeast also have a major defect in cortical actin
organization and accumulate G-actin. Overexpression of
SCD5 partially suppresses the actin defect of clathrin
mutants, whereas combining scd5-338 with a clathrin
mutation exacerbates the actin and endocytic phenotypes. Both Scd5p and
yeast clathrin physically associate with Sla2p, a homologue of the
mammalian huntingtin interacting protein HIP1 and the related HIP1R.
Furthermore, Sla2p localization at the cell cortex is dependent on
Scd5p and clathrin function. Therefore, Scd5p and clathrin are
important for actin organization and endocytosis, and Sla2p may provide
a critical link between clathrin and the actin cytoskeleton in yeast,
similar to HIP1(R) in animal cells.
Corresponding author. E-mail address:
skl{at}po.cwru.edu.
Present addresses:
§Department Biochemistry, University
Ghent, Baertsoenkaai 3, B-9000 Ghent, Belgium;
¶Department of Genetics, University of Pennsylvania,
Philadelphia, PA 19104.
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