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Originally published as Genetics Published Articles Ahead of Print on July 2, 2006.
Genetics, Vol. 174, 215-227, September 2006, Copyright © 2006
doi:10.1534/genetics.106.058362
The Conserved ATPase Get3/Arr4 Modulates the Activity of Membrane-Associated Proteins in Saccharomyces cerevisiae
Kathryn L. Auld*,
Amy L. Hitchcock*,1,
Hugh K. Doherty
,
Seth Frietze*,
Linda S. Huang and
Pamela A. Silver*,2
* Department of Systems Biology, Harvard Medical School, Boston, Massachusetts 02115 and Department of Biology, University of Massachusetts, Boston, Massachusetts 02125
2 Corresponding author: Department of Systems Biology, Harvard Medical School, WAB536, 200 Longwood Ave., Boston, MA 02115.
E-mail: pamela_silver{at}dfci.harvard.edu
The regulation of cellular membrane dynamics is crucial for maintaining proper cell growth and division. The Cdc48-Npl4-Ufd1 complex is required for several regulated membrane-associated processes as part of the ubiquitin–proteasome system, including ER-associated degradation and the control of lipid composition in yeast. In this study we report the results of a genetic screen in Saccharomyces cerevisiae for extragenic suppressors of a temperature-sensitive npl4 allele and the subsequent analysis of one suppressor, GET3/ARR4. The GET3 gene encodes an ATPase with homology to the regulatory component of the bacterial arsenic pump. Mutants of GET3 rescue several phenotypes of the npl4 mutant and transcription of GET3 is coregulated with the proteasome, illustrating a functional relationship between GET3 and NPL4 in the ubiquitin–proteasome system. We have further found that Get3 biochemically interacts with the trans-membrane domain proteins Get1/Mdm39 and Get2/Rmd7 and that 
get3 is able to suppress phenotypes of get1 and get2 mutants, including sporulation defects. In combination, our characterization of GET3 genetic and biochemical interactions with NPL4, GET1, and GET2 implicates Get3 in multiple membrane-dependent pathways.
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