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Published online April 2, 2007
doi:10.1083/jcb.200608066
The Journal of Cell Biology, Vol. 177, No. 1, 39-49
The Rockefeller University Press, 0021-9525 $30.00
© 2007 Makhnevych et al.
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Article

 The role of karyopherins in the regulated sumoylation of septins

Taras Makhnevych1, Christopher Ptak1, C. Patrick Lusk1, John D. Aitchison1,2, and Richard W. Wozniak1

1 Department of Cell Biology, University of Alberta, Edmonton, Alberta T6G 2H7 Canada
2 Institute for Systems Biology, Seattle, WA 98103

Correspondence to Richard W. Wozniak: rick.wozniak{at}ualberta.ca; or John D. Aitchison: jaitchis{at}systemsbiology.org

In the yeast Saccharomyces cerevisiae, several components of the septin ring are sumoylated during anaphase and then abruptly desumoylated at cytokinesis. We show that septin sumoylation is controlled by the interactions of two enzymes of the sumoylation pathway, Siz1p and Ulp1p, with the nuclear transport machinery. The E3 ligase Siz1p is imported into the nucleus by the karyopherin Kap95p during interphase. In M phase, Siz1p is exported from the nucleus by the karyopherin Kap142p/Msn5p and subsequently targeted to the septin ring, where it participates in septin sumoylation. We also show that the accumulation of sumoylated septins during mitosis is dependent on the interactions of the SUMO isopeptidase Ulp1p with Kap121p and Kap95p–Kap60p and the nuclear pore complex (NPC). In addition to sequestering Ulp1 at the NPC, Kap121p is required for targeting Ulp1p to the septin ring during mitosis. We present a model in which Ulp1p is maintained at the NPC during interphase and transiently interacts with the septin ring during mitosis.

T. Makhnevych and C. Ptak contributed equally to this paper.

Abbreviations used in this paper: INM, inner nuclear membrane; NE, nuclear envelope; NES, nuclear export signal; NPC, nuclear pore complex; TAP, tandem affinity purification; WT, wild type.


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