Suppressors of YCK-encoded yeast casein kinase 1deficiency define the four subunits of a novel clathrin AP-like complex
Copyright policy )Suppressors of YCK-encoded yeast casein kinase 1deficiency define the four subunits of a novel clathrin AP-like complex
In Saccharomyces cerevisiae, the redundant YCK1 and YCK2 genes (Yeast Casein Kinase 1) are required for viability. We describe here the molecular analysis of four mutations that eliminate the requirement for Yck activity. These mutations alter proteins that resemble the four subunits of clathrin adaptors (APs), with highest sequence similarity to those of the recently identified AP-3 complex. The four yeast subunits are associated in a high-molecular-weight complex. These proteins have no essential function and are not redundant for function with other yeast AP-related proteins. Combination of suppressor mutations with a clathrin heavy chain mutation (chc1-ts) confers no synthetic growth defects. However, a yck(ts) mutation shows a strong synthetic growth defect with chc1-ts. Moreover, endocytosis of Ste3p is dramatically decreased in yck(ts) cells and is partially restored by the AP suppressor mutations. These results suggest that vesicle trafficking at the plasma membrane requires the activity of Yck protein kinases, and that the new AP-related complex may participate in this process.
- Case Western Reserve University United States
- University of California, Los Angeles United States
- Louisiana State University Health Sciences Center Shreveport United States
- Moravian College United States
Casein Kinase I, Protein Conformation, Blotting, Western, DNA Mutational Analysis, Molecular Sequence Data, Membrane Proteins, Nerve Tissue Proteins, Receptors, Cell Surface, Endosomes, Phosphoproteins, Clathrin, Endocytosis, Receptors, G-Protein-Coupled, Adaptor Proteins, Vesicular Transport, Monomeric Clathrin Assembly Proteins, Morphogenesis, Phosphorylation, Casein Kinases, Protein Kinases, Cell Division
Casein Kinase I, Protein Conformation, Blotting, Western, DNA Mutational Analysis, Molecular Sequence Data, Membrane Proteins, Nerve Tissue Proteins, Receptors, Cell Surface, Endosomes, Phosphoproteins, Clathrin, Endocytosis, Receptors, G-Protein-Coupled, Adaptor Proteins, Vesicular Transport, Monomeric Clathrin Assembly Proteins, Morphogenesis, Phosphorylation, Casein Kinases, Protein Kinases, Cell Division
citations This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).142 popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.Top 10% influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).Top 10% impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.Top 1%
Citations provided by BIP!Popularity provided by BIP!