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Published 22 November 2004. doi:10.1083/jcb.200405168
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 167, Number 4, 605-611
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 Mlp-dependent anchorage and stabilization of a desumoylating enzyme is required to prevent clonal lethality

Xiaolan Zhao, Chia-Yung Wu, and Günter Blobel

Laboratory of Cell Biology, The Rockefeller University, New York, NY 10021

Correspondence to Günter Blobel: blobel{at}rockefeller.edu


Abstract
Myosin-like proteins 1 and 2 (Mlp1 and Mlp2) form filaments attached to the nucleoplasmic side of the nuclear pore complexes via interaction with the nucleoporin Nup60. Here, we show that Mlps and Nup60, but not several other nucleoporins, are required to localize and stabilize a desumoylating enzyme Ulp1. Moreover, like Mlps, Ulp1 exhibits a unique asymmetric distribution on the nuclear envelope. Consistent with a role in regulating Ulp1, removal of either or both MLPs affects the SUMO conjugate pattern. We also show that deleting MLPs or the localization domains of Ulp1 results in DNA damage sensitivity and clonal lethality, the latter of which is caused by increased levels of 2-micron circle DNA. Epistatic and dosage suppression analyses further demonstrate that Mlps function upstream of Ulp1 in 2-micron circle maintenance and the damage response. Together, our results reveal that Mlps play important roles in regulating Ulp1 and subsequently affect sumoylation stasis, growth, and DNA repair.

C.-Y. Wu's present address is Dept. of Biology, Massachusetts Institute of Technology, 31 Ames St. 68-135, Cambridge, MA 02139.

Abbreviations used in this paper: Mlp, myosin-like protein; NPC, nuclear pore complex; SUMO, small ubiquitin-like modifier.


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