High impact information on BEM3

• Loss of polarisome components and mutation of Cdc24 decrease the frequency of projection formation, while loss of Bem3 increases the frequency of projection formation [1].
• Specifically, Cdc42(D38E)p showed reduced interactions with the Cla4p p21-activated protein kinase and the Bem3p GTPase-activating protein and cdc42(D38E) was the only mutant allele able to complement the Deltacdc42 null mutant [2].
• The nonaxial budding defect of dbm1 mutants can be rescued partially by overproduction of Bem3p and is exacerbated by its absence [3].
• However, when cells lacking both Cdc42 GTPase-activating proteins, encoded by RGA2 and BEM3, were grown under pseudohyphal-promoting conditions the bud was highly elongated and lacked a constriction at its base, so that its shape resembled a hyphal germ tube [4].
• We also report the identification of a new gene, BEM3, that is a multicopy suppressor of the temperature-sensitive lethality caused by mutations in the bud emergence gene BEM2 [5].

Biological context of BEM3

• Biochemical comparisons of the Saccharomyces cerevisiae Bem2 and Bem3 proteins. Delineation of a limit Cdc42 GTPase-activating protein domain [6].

Associations of BEM3 with chemical compounds

• Control of the yeast bud-site assembly GTPase Cdc42. Catalysis of guanine nucleotide exchange by Cdc24 and stimulation of GTPase activity by Bem3 [5].

Other interactions of BEM3

• For example, deletion of RGA1, but not RGA2 or BEM3, caused hyperinvasive growth [7].

References