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A more recent version of this article appeared on August 1, 2002
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Submitted on January 8, 2002
Revised on April 15, 2002
Accepted on May 15, 2002
1 Department of Molecular Biology and Microbiology, and Program in Genetics, Case Western Reserve University, 10900 Euclid Avenue, Cleveland OH 44106
2 Biozentrum of the University of Basel, CH-4056 Basel, Switzerland (present address: Department Biochemistry, University Ghent, Baertsoenkaai 3, B-9000 Ghent, Belgium)
3 Department of Molecular Biology and Microbiology, Case Western Reserve University, 10900 Euclid Avenue, Cleveland OH 44106
4 Department of Molecular Biology and Microbiology, Case Western Reserve University, 10900 Euclid Avenue, Cleveland OH 44106 (present address: Department of Genetics, University of Pennsylvania, Philadelphia, PA 19104)
5 Biozentrum of the University of Basel, CH-4056 Basel, Switzerland
* Corresponding author. E-mail address: skl{at}po.cwru.edu.
SCD5 was identified as a multicopy suppressor of clathrin HC-deficient yeast. SCD5 is essential, but a scd5-
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, while 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 upon 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.
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