The inactive form of a yeast casein kinase I suppresses the secretory defect of the sec12 mutant. Implication of negative regulation by the Hrr25 kinase in the vesicle budding from the endoplasmic reticulum.

@article{Murakami1999TheIF,
  title={The inactive form of a yeast casein kinase I suppresses the secretory defect of the sec12 mutant. Implication of negative regulation by the Hrr25 kinase in the vesicle budding from the endoplasmic reticulum.},
  author={Arisa Murakami and Keiji Kimura and Akihiko Nakano},
  journal={The Journal of biological chemistry},
  year={1999},
  volume={274 6},
  pages={3804-10}
}
Sec12p is the guanine nucleotide exchange factor of Sar1 GTPase and functions at the very upstream in the vesicle budding reactions from the endoplasmic reticulum (ER). We previously identified three yeast loci, RST1, RST2, and RST3, whose mutations suppressed the temperature-sensitive growth of the sec12-4 mutant (Nakano, A. (1996) J. Biochem. (Tokyo) 120, 642-646). In the present study, we cloned the wild-type RST2 gene by complementation of the cold-sensitive phenotype of the rst2-1 mutant… CONTINUE READING
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