Distinct sequence determinants direct intracellular sorting and modification of a yeast vacuolar protease. Academic Article uri icon


  • We have mapped a sequence determinant in the vacuolar glycoprotein carboxypeptidase Y (CPY) that directs intracellular sorting of this enzyme. Through the study of hybrid proteins, consisting of amino-terminal segments of CPY fused to the secretory enzyme invertase, we have found that the N-terminal 50 amino acids of CPY are sufficient to direct delivery of a CPY-Inv hybrid protein to the yeast vacuole. Our data suggest that this 50 amino acid segment of CPY contains two distinct functional domains; an N-terminal signal peptide followed by a segment of 30 amino acids that contains the vacuolar sorting signal. Deletion of this putative vacuole sorting signal from an otherwise wild-type CPY protein leads to missorting of CPY. Furthermore, examination of the Asn-linked oligosaccharides present on CPY and CPY-Inv hybrid proteins suggests that an additional determinant in CPY specifies the extent to which these proteins are glycosylated in the Golgi complex.

published proceedings

  • Cell

altmetric score

  • 9

author list (cited authors)

  • Johnson, L. M., Bankaitis, V. A., & Emr, S. D.

citation count

  • 281

complete list of authors

  • Johnson, LM||Bankaitis, VA||Emr, SD

publication date

  • March 1987

published in