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• W1983384469 abstract "We have constructed a series of mutations in the signal sequence of the yeast vacuolar protein carboxypeptidase Y (CPY), and have used pulse-chase radiolabeling and immunoprecipitation to examine the in vivo effects of these mutations on the entry of the mutant CPY proteins into the secretory pathway. We find that introduction of a negatively charged residue, aspartate, into the hydrophobic core of the signal sequence has no apparent effect on signal sequence function. In contrast, internal in-frame deletions within the signal sequence cause CPY to be synthesized as unglycosylated precursors. These are slowly and inefficiently converted to glycosylated precursors that are indistinguishable from the glycosylated forms produced from the wild-type gene. These precursors are converted to active CPY in a PEP4-dependent manner, indicating that they are correctly localized to the vacuole. Surprisingly, a deletion mutation that removes the entire CPY signal sequence has a similar effect: unglycosylated precursor accumulates in cells carrying this mutant gene, and greater than 10% of it is posttranslationally glycosylated. Thus, the amino-terminal signal sequence of CPY, while important for translocation efficiency, is not absolutely required for the translocation of this protein." @default.
• W1983384469 created "2016-06-24" @default.
• W1983384469 creator A5013876167 @default.
• W1983384469 creator A5026009753 @default.
• W1983384469 date "1987-05-01" @default.
• W1983384469 modified "2023-10-02" @default.
• W1983384469 title "Yeast carboxypeptidase Y can be translocated and glycosylated without its amino-terminal signal sequence." @default.
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• W1983384469 doi "https://doi.org/10.1083/jcb.104.5.1183" @default.
• W1983384469 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2114485" @default.
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