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Vol. 13, Issue 6, 2091-2105, June 2002
and
*Department of Molecular, Cellular, and Developmental Biology,
Sinsheimer Labs, University of California, Santa Cruz, California
95065; and Gin4, a Nim1-related kinase, is required in budding yeast for
localization of the septins and for proper control of daughter cell
growth during G2/M. Gin4 becomes hyperphosphorylated when cells enter
mitosis, leading to activation of Gin4 kinase activity. In this study,
we have used immunoaffinity chromatography to identify proteins that
associate with Gin4 during mitosis, with the goal of finding targets of
Gin4 kinase activity and proteins that play a role in Gin4 activation.
We show that during mitosis Gin4 is assembled into a multiprotein
complex that includes Nap1, Bni5, the septins, and at least two
molecules of Gin4. The associated Gin4 molecules present in this
complex phosphorylate each other, leading to Gin4 hyperphosphorylation.
Furthermore, the Shs1 septin present in the complex undergoes
Gin4-dependent phosphorylation during mitosis and appears to be a
substrate of Gin4 in vitro, suggesting that it is a target of Gin4
kinase activity in vivo. Genetic data support the idea that Shs1 is an
important target of Gin4 kinase activity. Association of Gin4 with the
septins during mitosis requires Shs1, Nap1, Cla4, Elm1, and the kinase activities of Gin4 and Cdc28. Self-association of Gin4 molecules requires Shs1 but not Cla4 or Nap1. Previous work has suggested that
the septins function together as a tight complex, and we found that the
majority of the Shs1 in the cell is tightly bound to the other septins
Cdc3, Cdc10, Cdc11, and Cdc12. Interestingly, however, Shs1 can bind to
Gin4 and induce Gin4 oligomerization under conditions in which the
Cdc11 septin does not bind to Gin4, suggesting that Shs1 can function
independently of the other septins. Taken together, these findings
suggest that highly regulated protein-binding events ensure that the
Gin4 kinase is activated only during mitosis and only in association
with Shs1, a likely in vivo substrate of Gin4. In addition, these
results provide clues to how Gin4 may regulate the localization or
function of the septins.
Department of Cell Biology, The Scripps
Research Institute, La Jolla, California 92037
Corresponding author. E-mail
address: kellogg{at}darwin.ucsc.edu.
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