Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 98, Issue 16, Pages 9104-9109Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.161282998
Keywords
-
Categories
Funding
- NIGMS NIH HHS [GM 58212, R01 GM058212] Funding Source: Medline
Ask authors/readers for more resources
Pma1 is a plasma membrane HT-ATPase whose activity at the cell surface is essential for cell viability. In this paper we describe a temperature-sensitive pma1 allele, pma1-10 (with two point mutations in the first cytoplasmic loop of Pma1}, in which the newly synthesized mutant protein fails to remain stable at the cell surface at 37 degreesC. Instead, Pma1-10 appears to undergo internalization for vacuolar degradation in a manner dependent on End4, Vps27, Doa4, and Pep4. By contrast with wild-type Pma1, mutant Pma1-10 is hypophosphorylated and fails to associate with a Triton-insoluble fraction at 37 degreesC, suggesting failure to enter lipid rafts. Kinetic analysis reveals that, at the permissive temperature, newly synthesized Pma1-10 acquires Triton-insolubility before becoming stabilized. We suggest that phosphorylation and lipid raft association may play important rotes in maintaining protein stability at the plasma membrane.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available