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A more recent version of this article appeared on July 1, 2008
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Submitted on December 1, 2007
Revised on March 10, 2008
Accepted on April 9, 2008
Department of Molecular, Cellular, and Developmental Biology, and Life Sciences Institute, University of Michigan, Ann Arbor, MI 48109-2216
Monitoring Editor: Charles Boone
The subcellular distribution of kinases and other signaling proteins is regulated in response to cellular cues; however, the extent of this regulation has not been investigated for any gene set in any organism. Here, we present a systematic analysis of protein kinases in the budding yeast, screening for differential localization during filamentous growth. Filamentous growth is an important stress response involving MAPK and PKA signaling modules, wherein yeast cells form interconnected and elongated chains. As standard strains of yeast are nonfilamentous, we constructed a unique set of 125 kinase-YFP chimeras in the filamentous
1278b strain for this study. In total, we identified six cytoplasmic kinases (Bcy1p, Fus3p, Ksp1p, Kss1p, Sks1p, Tpk2p) that localize predominantly to the nucleus during filamentous growth. These kinases form part of an interdependent, localization-based regulatory network: deletion of each individual kinase, or loss of kinase activity, disrupts the nuclear translocation of at least two other kinases. In particular, this study highlights a previously unknown function for the kinase Ksp1p, indicating the essentiality of its nuclear translocation during yeast filamentous growth. Thus, the localization of Ksp1p and the other kinases identified here is tightly controlled during filamentous growth, representing an overlooked regulatory component of this stress response.