Pharmaceutical Sciences Faculty Publications
Direct Phosphorylation and Activation of a Nim1-Related Kinase Gin4 by Elm1 in Budding Yeast
Document Type
Article
Publication Date
9-15-2006
Journal Title
The Journal of Biological Chemistry
ISSN
0021-9258
Volume
281
Issue
37
First Page
27090
Last Page
27098
DOI
10.1074/jbc.M601483200
PubMed ID
16861226
Abstract
In budding yeast, Gin4, a Nim1-related kinase, plays an important role in proper organization of the septin ring at the mother-bud neck, a filamentous structure that is critical for diverse cellular processes including mitotic entry and cytokinesis. How Gin4 kinase activity is regulated is not known. Here we showed that a neck-associated Ser/Thr kinase Elm1, which is important for septin assembly, is critical for proper modification of Gin4 and its physiological substrate Shs1. In vitro studies with purified recombinant proteins demonstrated that Elm1 directly phosphorylates and activates Gin4, which in turn phosphorylates Shs1. Consistent with these observations, acute inhibition of Elm1 activity abolished mitotic Gin4 phosphorylation and Gin4-dependent Shs1 modification in vivo. In addition, a gin4 mutant lacking the Elm1-dependent phosphorylation sites exhibited an impaired localization to the bud-neck and, as a result, induced a significant growth defect with an elongated bud morphology. Thus, Elm1 regulates the septin assembly-dependent cellular events by directly phosphorylating and activating the Gin4-dependent pathway(s).
Keywords
Animals, cyclin-dependent kinases, enzyme activation, gene expression regulation, enzymologic, gene expression regulation, fungal, insecta, membrane proteins, models, biological, peptides, phosphorylation, plasmids, protein kinases
Recommended Citation
Asano, Satoshi; Park, Jung-Eun; Yu, Li-Rong; Zhou, Ming; Sakchaisri, Krisada; Park, Chong J.; Kang, Young H.; Thorner, Jeremy; Veenstra, Timothy D.; and Lee, Kyung S., "Direct Phosphorylation and Activation of a Nim1-Related Kinase Gin4 by Elm1 in Budding Yeast" (2006). Pharmaceutical Sciences Faculty Publications. 391.
https://digitalcommons.cedarville.edu/pharmaceutical_sciences_publications/391