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Intracellular targeting and structural conservation of a prohormone-processing endoprotease
R S Fuller1, A J Brake, J Thorner
1Department of Biochemistry, University of California, Berkeley 94720.
Science (New York, N.Y.)
|October 27, 1989
Summary
The yeast Kex2 protease, essential for prohormone processing, requires specific domains for cellular localization. Its human homolog, furin, is a potential candidate for similar functions in humans.
Area of Science:
- Molecular Biology
- Cell Biology
- Biochemistry
Background:
- The KEX2 gene product in Saccharomyces cerevisiae is a key prohormone-processing endoprotease.
- This enzyme is a membrane-bound glycoprotein residing in the secretory pathway.
Purpose of the Study:
- To investigate the structural requirements for the proper cellular localization of the Kex2 protease.
- To identify potential human homologs involved in prohormone processing.
Main Methods:
- Analysis of mutant kex2 genes with truncated 3' ends.
- Sequence homology comparison between yeast Kex2 and human proteins.
Main Results:
- Carboxyl terminal domains of the Kex2 enzyme are crucial for its correct localization within yeast cells.
- The human gene product 'furin' exhibits 50% identity with the catalytic domain of Kex2 protease.
Conclusions:
- Specific carboxyl terminal domains dictate the localization of yeast Kex2 protease.
- Furin is a strong candidate for a human prohormone-processing enzyme due to significant catalytic domain homology with Kex2.