High impact information on ELM1

• These results demonstrate that the Elm1 kinase plays an important role in G(1) events required for bud emergence and septin organization [1].
• We found that inhibition of Elm1 kinase activity during G(2) results in a phenotype similar to the phenotype caused by deletion of the ELM1 gene, as expected [1].
• However, inhibition of Elm1 kinase activity earlier in the cell cycle results in a prolonged G(1) delay [1].
• In budding yeast, the Elm1 kinase is required for coordination of cell growth and cell division at G(2)/M [1].
• Previous studies have suggested that Elm1 may function to negatively regulate the Swe1 kinase [2].

Biological context of ELM1

• Cells carrying a deletion of the ELM1 gene undergo a prolonged mitotic delay, fail to negatively regulate polar bud growth during mitosis, and show defects in septin organization [2].
• Deletion of ELM1 does not give an snf- phenotype [3].
• We propose a model in which the Elm1 kinase functions in a mitotic signaling network that controls events required for normal bud growth and cytokinesis, while the Swe1 kinase functions in a checkpoint pathway that delays nuclear division in response to defects in these events [2].
• Elm1p also activated the purified SNF1 complex, and this correlated with phosphorylation of Thr210 in the activation loop [3].
• A 'signal integration' model for the complex relationship of Elm1 and the RAS/cAMP pathway in controlling morphogenesis in response to nutrients is proposed [4].

Anatomical context of ELM1

• A triple mutant, delta dhh1 ssd1-d delta elm1, apparently had very fragile cell walls and could grow only in a medium supplemented with 1 M sorbitol [5].

Associations of ELM1 with chemical compounds

• Constitutively elongated Saccharomyces cerevisiae mutants (elm) have been isolated; the ELM1 gene encodes a putative serine/threonine protein kinase [4].
• The control of morphogenesis in Saccharomyces cerevisiae by Elm1 kinase is responsive to RAS/cAMP pathway activity and tryptophan availability [4].
• Collectively, these data show that ELM1, and genes encoding related serine/threonine protein kinases, are required for regulation of multidrug resistance involving, at least in part, control of PDR5 transcription [6].
• Constitutive filamentous growth resulting from deletion of the protein kinase Elm1 was prevented by modification of Cdc28 such that it could not be phosphorylated on tyrosine residue 19 [7].

Enzymatic interactions of ELM1

• In vitro studies with purified recombinant proteins demonstrated that Elm1 directly phosphorylates and activates Gin4, which in turn phosphorylates Shs1 [8].

Regulatory relationships of ELM1

• Our results indicate that cytokinesis in budding yeast is regulated by Elm1 [9].
• Thus, Elm1 regulates the septin assembly-dependent cellular events by directly phosphorylating and activating the Gin4-dependent pathway(s) [8].

Other interactions of ELM1

• CDC28, ELM1 and SSD1 were thus found to be such candidates and we subsequently analysed their interactions [5].
• Elm1p is one of three upstream kinases for the Saccharomyces cerevisiae SNF1 complex [3].
• Localization of Hsl1p to the neck requires Elm1p function [10].
• Overexpression of Elm1 partially rescues the ts phenotype of cdc25 and cyr1 mutants [4].
• Deletion of ELM1 in low PKA activity mutants increased the severity of their phenotypes, and activation of Ras2 decreases the cell elongation phenotype of elm1 mutants [4].

References