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doi:10.1534/genetics.105.052068
A more recent version of this article appeared on March 1, 2006.
REGULAR RESEARCH PAPERS |
The integral membrane protein Pom34p functionally links nucleoporin subcomplexes
Mi Miao 1, Kathryn J. Ryan 1 and Susan R. Wente 1*
1 Vanderbilt University Medical Center
* To whom correspondence should be addressed. E-mail: susan.wente{at}vanderbilt.edu.
Submitted on October 6, 2005
Revised on November 14, 2005
Accepted on 30 November 2005
Here we have examined the function of Pom34p, a novel membrane protein in S. cerevisiae, localized to nuclear pore complexes (NPCs). Membrane topology analysis revealed that Pom34p is a double-pass transmembrane protein with both the amino (N-) and carboxy (C-) termini positioned on the cytosolic/pore face. The network of genetic interactions between POM34 and genes encoding other nucleoporins was established, and showed specific links between Pom34p function and Nup170p, Nup188p, Nup59p, Gle2p, Nup159p, and Nup82p. The transmembrane domains of Pom34p in addition to either the N- or C-terminal region were necessary for its function in different double mutants. We further characterized the pom34
N nup188 mutant, and found it to be perturbed both in NPC structure and function. Mislocalization of a subset of nucleoporins harboring phenylalanine-glycine repeats was observed, and nuclear import capacity for the Kap104p and Kap121p pathways was inhibited. In contrast, the pom34 pom152 double mutant was viable at all temperatures and showed no such defects. Interestingly, POM152 overexpression suppressed the synthetic lethality of pom34 nup170 and pom34 nup59 mutants. We speculate that multiple integral membrane proteins, either within the nuclear pore domain or in the nuclear envelope, execute coordinated roles in NPC structure and function.
Key Words: nuclear export, nuclear import, nuclear pore complex, topology
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