A Mutant Plasma Membrane Protein Is Stabilized Upon Loss of Yvh1, a Novel Ribosome Assembly Factor
A Mutant Plasma Membrane Protein Is Stabilized Upon Loss of Yvh1, a Novel Ribosome Assembly Factor
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DOI:
10.1534/genetics.108.100099
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发表时间:
2009-03-01
期刊:
影响因子:
3.3
通讯作者:
Chang, Ainy
中科院分区:
文献类型:
--
作者:
Liu, Yu;Chang, Ainy
Pma1-10 is a mutant plasma membrane ATPase defective at the restrictive temperature in stability at the cell surface. At 37 degrees, 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, therapy 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; and yvh1 Delta 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 Rp119a and Rp135a. We propose that changes in ribosome biogenesis caused by loss Yvh1 or specific ribosomal proteins have effects on the plasma membrane, perhaps by producing specific translational changes.