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doi:10.1534/genetics.108.100099
A more recent version of this article appeared on March 1, 2009.
Originally published as Genetics Published Articles Ahead of Print on December 29, 2008.
REGULAR RESEARCH PAPERS |
A Mutant Plasma Membrane Protein Is Stabilized Upon Loss of Yvh1, a Novel Ribosome Assembly Factor
Yu Liu 1 and Amy Chang 1*
1 University of Michigan
* To whom correspondence should be addressed. E-mail: amychang{at}umich.edu.
Submitted on December 23, 2008
Accepted on 24 December 2008
Pma1-10 is a mutant plasma membrane ATPase defective at the restrictive temperature in stability at the cell surface. At 37°C, Pma1-10 is ubiquitinated and internalized from the plasma membrane for degradation in the vacuole. YVH1, encoding a tyrosine phosphatase, is a mutant suppressor of pma1-10; in the absence of Yvh1, Pma1-10 remains stable at the plasma membrane, thereby permitting cells to grow. The RING finger domain of Yvh1, but not its phosphatase domain, is required for removal of mutant Pma1-10 from the plasma membrane. Yvh1 is a novel ribosome assembly factor: in yvh1
; cells, free 60S and 80S ribosomal subunits are decreased, free 40S subunits are increased, and half-mer polysomes are accumulated. Pma1-10 is also stabilized by deletion of 60S ribosomal proteins Rpl19 and Rpl35. We propose that changes in ribosome biogenesis caused by loss of Yvh1 or specific ribosomal proteins have effects on the plasma membrane, perhaps by producing specific translational changes.
Key Words: plasma membrane ATPase, protein stability, ribosome assembly
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