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This paper shows that actin depolarization in response to mild heat shock requires a signaling pathway involving the putative plasma membrane sensor Wsc1p, the Rho guanine nucleotide exchange factor Rom2p, and the protein kinase C homologue Pkc1p. These same proteins are suggested to be responsible for the subsequent repolarization of actin, in this case acting through the MAPK Mpk1p. Depolarization and subsequent repolarization of actin are shown to drive a similar relocalization on the part of glucan synthase, responsible for synthesizing a major cell wall polysaccharide, and it is suggested that this behavior constitutes a stress response that helps the cell to survive cell wall damage.
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This paper provides data suggesting that JBP1, a human homologue of Hsl7p, is a protein arginine methyltransferase. JBP1 was identified as a JAK-interacting protein, and immunoprecipitated JBP1 methylates histones and myelin basic protein in vitro.
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2 arrest. The authors suggest that the morphogenesis checkpoint operates through bifurcated pathways promoting both Swe1p stabilization and inhibition of Mih1p.
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McMillan, J.N.1
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This paper shows that Hsl7p is localized to the daughter side of the mother-bud neck in a manner that depends on Hsl1p, and that Hsl7p interacts physically with both Hsl1p and Swe1p. The authors suggest that Hsl7p acts as an adaptor to link Hsl1p and Swe1p.
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2 delays associated with the generation of elongated buds. Perturbations that affect actin organization, however, do not cause delocalization of this module from the neck. We suggest that the location of the module serves to couple Swe1p degradation to bud formation.
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2 delays associated with the generation of elongated buds. Perturbations that affect actin organization, however, do not cause delocalization of this module from the neck. We suggest that the location of the module serves to couple Swe1p degradation to bud formation.
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This paper shows that Bub2p and Byr4p are localized to the spindle pole bodies in S. cerevisiae and function in the same pathway to inhibit exit from mitosis.
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