Yeast carboxypeptidase Y can be translocated and glycosylated without its amino-terminal signal sequence

@article{BlachlyDyson1987YeastCY,
  title={Yeast carboxypeptidase Y can be translocated and glycosylated without its amino-terminal signal sequence},
  author={Elizabeth Blachly-Dyson and Tom H. Stevens},
  journal={The Journal of Cell Biology},
  year={1987},
  volume={104},
  pages={1183 - 1191}
}
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… CONTINUE READING
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tein sorting in yeast : the localization determinant of yeast vacuolar carboxypeptidase Y resides in the propeptide

  • G von Heijne
  • 1987

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