Scd5p and clathrin function are important for cortical actin organization, endocytosis, and localization of Sla2p in yeast

Kenneth R. Henry, Kathleen D'Hondt, Ji Suk Chang, Thomas Newpher, Kristen Huang, R. Tod Hudson, Howard Riezman, Sandra K. Lemmon

Research output: Contribution to journalArticlepeer-review

55 Scopus citations


SCD5 was identified as a multicopy suppressor of clathrin HC-deficient yeast. SCD5 is essential, but an scd5-Δ338 mutant, expressing Scd5p with a C-terminal truncation of 338 amino acids, is temperature sensitive for growth. Further studies here demonstrate that scd5-Δ338 affects receptor-mediated and fluid-phase endocytosis and normal actin organization. The scd5-Δ338 mutant contains larger and depolarized cortical actin patches and a prevalence of G-actin bars. scd5-Δ338 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-Δ338 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.

Original languageEnglish (US)
Pages (from-to)2607-2625
Number of pages19
JournalMolecular biology of the cell
Issue number8
StatePublished - Aug 2002
Externally publishedYes

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology


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