Intracellular targeting and structural conservation of a prohormone-processing endoprotease

Science. 1989 Oct 27;246(4929):482-6. doi: 10.1126/science.2683070.

Abstract

The prohormone-processing endoprotease (KEX2 gene product) of the yeast Saccharomyces cerevisiae is a membrane-bound, 135,000-dalton glycoprotein, which contains both asparagine-linked and serine- and threonine-linked oligosaccharide and resides in a secretory compartment. Analysis of mutant kex2 genes truncated at their 3' end indicates that carboxyl terminal domains of the enzyme are required for its proper localization within the cell. A human gene product, "furin," shares 50% identity with the catalytic domain of Kex2 protease and is, therefore, a candidate for a human prohormone-processing enzyme.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Humans
  • Molecular Sequence Data
  • Mutation
  • Proprotein Convertases*
  • Saccharomyces cerevisiae / enzymology
  • Saccharomyces cerevisiae Proteins*
  • Sequence Homology, Nucleic Acid
  • Serine Endopeptidases / genetics*
  • Serine Endopeptidases / metabolism
  • Subcellular Fractions / enzymology
  • Subtilisins*

Substances

  • Saccharomyces cerevisiae Proteins
  • Proprotein Convertases
  • Serine Endopeptidases
  • Subtilisins
  • KEX2 protein, S cerevisiae

Associated data

  • GENBANK/M24201