Originally published as Genetics Published Articles Ahead of Print on December 29, 2008.

Genetics, Vol. 181, 907-915, March 2009, Copyright © 2009
doi:10.1534/genetics.108.100099

A Mutant Plasma Membrane Protein Is Stabilized Upon Loss of Yvh1, a Novel Ribosome Assembly Factor

Yu Liu and Amy Chang¹

Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109

¹ Corresponding author: Department of Molecular, Cellular and Developmental Biology, 830 N. University, Ann Arbor, MI 48109.
E-mail: amychang{at}umich.edu

Pma1-10 is a mutant plasma membrane ATPase defective at the restrictive temperature in stability at the cell surface. At 37°, 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 Rpl19a and Rpl35a. 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.

Related articles in Genetics:

ISSUE HIGHLIGHTS

Genetics 2009 181: NP. [Full Text]  

This article has been cited by other articles:

				K.-Y. Lo, Z. Li, F. Wang, E. M. Marcotte, and A. W. Johnson Ribosome stalk assembly requires the dual-specificity phosphatase Yvh1 for the exchange of Mrt4 with P0 J. Cell Biol., September 21, 2009; 186(6): 849 - 862. [Abstract] [Full Text] [PDF]

				S. Kemmler, L. Occhipinti, M. Veisu, and V. G. Panse Yvh1 is required for a late maturation step in the 60S biogenesis pathway J. Cell Biol., September 21, 2009; 186(6): 863 - 880. [Abstract] [Full Text] [PDF]

				C. A. Bonham and P. O. Vacratsis Redox Regulation of the Human Dual Specificity Phosphatase YVH1 through Disulfide Bond Formation J. Biol. Chem., August 21, 2009; 284(34): 22853 - 22864. [Abstract] [Full Text] [PDF]

International Access Link

Online ISSN: 1943-2361  Print ISSN: 0016-6731
Copyright 2009 by the Genetics Society of America
phone: 412-268-1812   fax: 412-268-1813   email: genetics-gsa{at}andrew.cmu.edu