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Gene Review

RIM11  -  Rim11p

Saccharomyces cerevisiae S288c

Synonyms: GSK3, MDS1, Regulator of IME2 protein 11, Serine/threonine-protein kinase RIM11/MSD1, YM9375.08, ...
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Psychiatry related information on RIM11


High impact information on RIM11

  • Here we show that the stimulatory effect of yeast Rcn1 involves phosphorylation of a conserved serine residue by Mck1, a member of the GSK-3 family of protein kinases [2].
  • GSK-3 kinases enhance calcineurin signaling by phosphorylation of RCNs [2].
  • In this report we show that in vivo, in cells grown in a medium promoting vegetative growth with acetate as the sole carbon source (SA medium), Rim11 phosphorylates Ime1, the master transcriptional activator required for entry into the meiotic cycle and for the transcription of early meiosis-specific genes [3].
  • We further show that the glucose signal is transmitted through Rim11 [4].
  • We further show that this nutrient signal is transmitted to Rim11 and consequently to Ime1 by the cyclic AMP/protein kinase A signal transduction pathway [3].

Biological context of RIM11


Anatomical context of RIM11


Associations of RIM11 with chemical compounds

  • An Arabidopsis GSK3/shaggy-like gene that complements yeast salt stress-sensitive mutants is induced by NaCl and abscisic acid [11].
  • A computer search reveals significant homology to serine/threonine protein kinases closely related to members of the GSK-3 subfamily [12].
  • Characterization of one of these mutants, mds1, revealed that it was sensitive not only to novobiocin but also to a wide range of drugs [13].

Physical interactions of RIM11

  • Here, we characterize mutant Ime1p derivatives that interact with Rim11p but are not phosphorylated in vitro [14].

Enzymatic interactions of RIM11


Other interactions of RIM11

  • Analysis of RIM11, a yeast protein kinase that phosphorylates the meiotic activator IME1 [5].
  • Rog1 binds directly to Rsp5, and their interaction is dependent on GSK-3 [15].
  • The 42-kDa tyrosine-phosphorylated protein was identified as Mck1, which is a member of the GSK3 family of protein kinases and previously known to be phosphorylated on tyrosine [16].
  • Interaction of yeast repressor-activator protein Ume6p with glycogen synthase kinase 3 homolog Rim11p [17].
  • Human Tau was readily phosphorylated at pathological epitopes, but in opposite directions regulated by kinases Mds1 and Pho85, orthologues of glycogen synthase kinase-3beta and cdk5, respectively (1) [9].

Analytical, diagnostic and therapeutic context of RIM11


  1. Purification of GSK-3 by affinity chromatography on immobilized axin. Primot, A., Baratte, B., Gompel, M., Borgne, A., Liabeuf, S., Romette, J.L., Jho, E.H., Costantini, F., Meijer, L. Protein Expr. Purif. (2000) [Pubmed]
  2. GSK-3 kinases enhance calcineurin signaling by phosphorylation of RCNs. Hilioti, Z., Gallagher, D.A., Low-Nam, S.T., Ramaswamy, P., Gajer, P., Kingsbury, T.J., Birchwood, C.J., Levchenko, A., Cunningham, K.W. Genes Dev. (2004) [Pubmed]
  3. The in vivo activity of Ime1, the key transcriptional activator of meiosis-specific genes in Saccharomyces cerevisiae, is inhibited by the cyclic AMP/protein kinase A signal pathway through the glycogen synthase kinase 3-beta homolog Rim11. Rubin-Bejerano, I., Sagee, S., Friedman, O., Pnueli, L., Kassir, Y. Mol. Cell. Biol. (2004) [Pubmed]
  4. Glucose and nitrogen regulate the switch from histone deacetylation to acetylation for expression of early meiosis-specific genes in budding yeast. Pnueli, L., Edry, I., Cohen, M., Kassir, Y. Mol. Cell. Biol. (2004) [Pubmed]
  5. Analysis of RIM11, a yeast protein kinase that phosphorylates the meiotic activator IME1. Bowdish, K.S., Yuan, H.E., Mitchell, A.P. Mol. Cell. Biol. (1994) [Pubmed]
  6. Genetic evidence for transcriptional activation by the yeast IME1 gene product. Smith, H.E., Driscoll, S.E., Sia, R.A., Yuan, H.E., Mitchell, A.P. Genetics (1993) [Pubmed]
  7. Selection for early meiotic mutants in yeast. Mitchell, A.P., Bowdish, K.S. Genetics (1992) [Pubmed]
  8. Evidence for a role of glycogen synthase kinase-3 beta in rodent spermatogenesis. Guo, T.B., Chan, K.C., Hakovirta, H., Xiao, Y., Toppari, J., Mitchell, A.P., Salameh, W.A. J. Androl. (2003) [Pubmed]
  9. Microtubule binding and clustering of human Tau-4R and Tau-P301L proteins isolated from yeast deficient in orthologues of glycogen synthase kinase-3beta or cdk5. Vandebroek, T., Terwel, D., Vanhelmont, T., Gysemans, M., Van Haesendonck, C., Engelborghs, Y., Winderickx, J., Van Leuven, F. J. Biol. Chem. (2006) [Pubmed]
  10. Feedback inhibition on cell wall integrity signaling by Zds1 involves Gsk3 phosphorylation of a cAMP-dependent protein kinase regulatory subunit. Griffioen, G., Swinnen, S., Thevelein, J.M. J. Biol. Chem. (2003) [Pubmed]
  11. An Arabidopsis GSK3/shaggy-like gene that complements yeast salt stress-sensitive mutants is induced by NaCl and abscisic acid. Piao, H.L., Pih, K.T., Lim, J.H., Kang, S.G., Jin, J.B., Kim, S.H., Hwang, I. Plant Physiol. (1999) [Pubmed]
  12. The Kluyveromyces lactis gene KLGSK-3 combines functions which in Saccharomyces cerevisiae are performed by MCK1 and MSD1. Rodríguez-Belmonte, E., González-Siso, I., Cerdán, E. Curr. Genet. (1998) [Pubmed]
  13. Mutations in the Saccharomyces cerevisiae gene SAC1 cause multiple drug sensitivity. Hughes, W.E., Pocklington, M.J., Orr, E., Paddon, C.J. Yeast (1999) [Pubmed]
  14. Catalytic roles of yeast GSK3beta/shaggy homolog Rim11p in meiotic activation. Malathi, K., Xiao, Y., Mitchell, A.P. Genetics (1999) [Pubmed]
  15. Yeast glycogen synthase kinase 3 is involved in protein degradation in cooperation with Bul1, Bul2, and Rsp5. Andoh, T., Hirata, Y., Kikuchi, A. Mol. Cell. Biol. (2000) [Pubmed]
  16. Essential functions of protein tyrosine phosphatases PTP2 and PTP3 and RIM11 tyrosine phosphorylation in Saccharomyces cerevisiae meiosis and sporulation. Zhan, X.L., Hong, Y., Zhu, T., Mitchell, A.P., Deschenes, R.J., Guan, K.L. Mol. Biol. Cell (2000) [Pubmed]
  17. Interaction of yeast repressor-activator protein Ume6p with glycogen synthase kinase 3 homolog Rim11p. Malathi, K., Xiao, Y., Mitchell, A.P. Mol. Cell. Biol. (1997) [Pubmed]
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