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Gene Review

GIN4  -  Gin4p

Saccharomyces cerevisiae S288c

Synonyms: D9719.13, Growth inhibitory protein 4, Serine/threonine-protein kinase GIN4, YDR507C
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High impact information on GIN4

  • Enhancement of microtubule shrinkage at the bud neck required the Par-1-related, septin-dependent kinases (SDK) Hsl1 and Gin4 [1].
  • Members of the septin family bind directly to Gin4, demonstrating that the functions of Gin4 and the septins must be closely linked within the cell [2].
  • In budding yeast, a protein kinase called Gin4 is specifically activated during mitosis and functions in a pathway initiated by the Clb2 cyclin to control bud growth [2].
  • Loss of septin function produces a phenotype that is very similar to the phenotype caused by loss of Gin4 function, and the septins are required early in mitosis to activate Gin4 kinase activity [2].
  • Affinity chromatography experiments demonstrate that Gin4 binds tightly to Nap1, indicating that the functions of these two proteins are closely tied within the cell [3].

Biological context of GIN4

  • Deletion of KCC4 had a similar effect to GIN4 deletion, causing moderate defects in bud formation at stationary phase; overexpression of Kcc4 inhibited cell growth [4].
  • Hsl1/Nik1, Kcc4 and Gin4 are structurally homologous protein kinases that localize to the bud neck and negatively regulate Swe1 by phosphorylation [4].
  • Overexpression of the GIN4 and GIN12 sequences induced elongated buds and a G2/M arrest-like phenotype, respectively [5].
  • Gin4 becomes hyperphosphorylated when cells enter mitosis, leading to activation of Gin4 kinase activity [6].
  • We have used genetics and biochemistry to identify additional proteins that function with Gin4 in this pathway, and both of these approaches have identified members of the septin family [2].

Associations of GIN4 with chemical compounds


Physical interactions of GIN4


Enzymatic interactions of GIN4

  • Thus, Elm1 regulates the septin assembly-dependent cellular events by directly phosphorylating and activating the Gin4-dependent pathway(s) [9].
  • In vitro studies with purified recombinant proteins demonstrated that Elm1 directly phosphorylates and activates Gin4, which in turn phosphorylates Shs1 [9].

Regulatory relationships of GIN4

  • 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 [6].
  • Evidence is presented which suggests that the hyperphosphorylated form of Cla4 is responsible for relaying the signal to activate Gin4 [10].

Other interactions of GIN4

  • Moreover, Hsl1, Kcc4, and Gin4 have homologs in higher eukaryotes, suggesting that the regulation of Swe1/Wee1 by this class of kinases is highly conserved [11].
  • Kcc4, like Hsl1 and Gin4, was found to localize to the bud neck in a septin-dependent fashion [11].
  • Genetic data support the idea that Shs1 is an important target of Gin4 kinase activity [6].
  • In this pathway, Clb2 initiates a series of events that lead to the mitosis-specific activation of the Gin4 protein kinase [10].
  • In Saccharomyces cerevisiae, additional functions have been ascribed to Nap1, as it has been shown to interact with Clb2 (B type cyclin) and Gin4 (septum formation) [12].


  1. Microtubule capture by the cleavage apparatus is required for proper spindle positioning in yeast. Kusch, J., Meyer, A., Snyder, M.P., Barral, Y. Genes Dev. (2002) [Pubmed]
  2. The septins are required for the mitosis-specific activation of the Gin4 kinase. Carroll, C.W., Altman, R., Schieltz, D., Yates, J.R., Kellogg, D. J. Cell Biol. (1998) [Pubmed]
  3. Control of mitotic events by Nap1 and the Gin4 kinase. Altman, R., Kellogg, D. J. Cell Biol. (1997) [Pubmed]
  4. The Saccharomyces cerevisiae bud-neck proteins Kcc4 and Gin4 have distinct but partially-overlapping cellular functions. Okuzaki, D., Watanabe, T., Tanaka, S., Nojima, H. Genes Genet. Syst. (2003) [Pubmed]
  5. Screening and identification of yeast sequences that cause growth inhibition when overexpressed. Akada, R., Yamamoto, J., Yamashita, I. Mol. Gen. Genet. (1997) [Pubmed]
  6. Cell cycle-dependent assembly of a Gin4-septin complex. Mortensen, E.M., McDonald, H., Yates, J., Kellogg, D.R. Mol. Biol. Cell (2002) [Pubmed]
  7. Cla4p, a Saccharomyces cerevisiae Cdc42p-activated kinase involved in cytokinesis, is activated at mitosis. Benton, B.K., Tinkelenberg, A., Gonzalez, I., Cross, F.R. Mol. Cell. Biol. (1997) [Pubmed]
  8. Nis1 encoded by YNL078W: a new neck protein of Saccharomyces cerevisiae. Iwase, M., Toh-e, A. Genes Genet. Syst. (2001) [Pubmed]
  9. Direct Phosphorylation and Activation of a Nim1-related Kinase Gin4 by Elm1 in Budding Yeast. Asano, S., Park, J.E., Yu, L.R., Zhou, M., Sakchaisri, K., Park, C.J., Kang, Y.H., Thorner, J., Veenstra, T.D., Lee, K.S. J. Biol. Chem. (2006) [Pubmed]
  10. Control of mitotic events by the Cdc42 GTPase, the Clb2 cyclin and a member of the PAK kinase family. Tjandra, H., Compton, J., Kellogg, D. Curr. Biol. (1998) [Pubmed]
  11. Nim1-related kinases coordinate cell cycle progression with the organization of the peripheral cytoskeleton in yeast. Barral, Y., Parra, M., Bidlingmaier, S., Snyder, M. Genes Dev. (1999) [Pubmed]
  12. Genome-wide expression analysis of NAP1 in Saccharomyces cerevisiae. Ohkuni, K., Shirahige, K., Kikuchi, A. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
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