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PMID: 9250663 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Suppressors of YCK-encoded yeast casein kinase 1 deficiency define the four subunits of a novel clathrin AP-like complex.

The EMBO journal ·Vol. 16 ·No. 14 ·1997-07-16 ·Pages 4194-204

Panek HR, Stepp JD, Engle HM, Marks KM, Tan PK, Lemmon SK, Robinson LC

Abstract

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.

MeSH Terms
Adaptor Proteins, Vesicular Transport Blotting, Western Casein Kinase I Casein Kinases Cell Division Clathrin/genetics,metabolism DNA Mutational Analysis Endocytosis Endosomes/metabolism Membrane Proteins/metabolism Molecular Sequence Data Monomeric Clathrin Assembly Proteins Morphogenesis Nerve Tissue Proteins/chemistry,genetics,metabolism Phosphoproteins/chemistry,genetics,metabolism Phosphorylation Protein Conformation Protein Kinases/genetics,metabolism Receptors, Cell Surface/metabolism Receptors, G-Protein-Coupled Receptors, Mating Factor Receptors, Pheromone Saccharomyces cerevisiae/enzymology,genetics,growth & development,metabolism Saccharomyces cerevisiae Proteins Suppression, Genetic/genetics
Chemicals
Adaptor Proteins, Vesicular Transport Clathrin Membrane Proteins Monomeric Clathrin Assembly Proteins Nerve Tissue Proteins Phosphoproteins Receptors, Cell Surface Receptors, G-Protein-Coupled Receptors, Mating Factor Receptors, Pheromone STE3 protein, S cerevisiae Saccharomyces cerevisiae Proteins clathrin assembly protein AP180 Protein Kinases Casein Kinase I Casein Kinases YCK1 protein, S cerevisiae YCK2 protein, S cerevisiae
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Panek H R
LSU Medical Center, Department of Biochemistry and Molecular Biology, Shreveport, LA 71130, USA.
Stepp J D
Engle H M
Marks K M
Tan P K
Lemmon S K
Robinson L C
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1997-07-16
Pages
4194-204
Language
English
Region
England
NLM ID
8208664
PMCID
PMC1170045
Subset
IM
Grants
PHS HHS · 39040 · United States
NIA NIH HHS · AG00105 · United States
Databases
GENBANK
G07072, L07073, L07074, L13939, L26291, M23674, M34177, M62419, M64998, R02669, R54523, T30164, T98538, U09841, U35411, U36858, U37673, U44890, X54424, X60288, X76053, X91067, Z36157, Z49274, Z50113, Z71255
SWISSPROT
P18484, P36000, P38065
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