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Science 20 October 1995: Vol. 270. no. 5235, pp. 464 - 467 DOI: 10.1126/science.270.5235.464
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Reports
Role of Yeast Insulin-Degrading Enzyme Homologs in Propheromone
Processing and Bud Site Selection
Neil Adames,
Kelly Blundell,
Matthew N. Ashby,
Charles Boone (1)
The Saccharomyces cerevisiae AXL1 gene product Axl1p
shares homology with the insulin-degrading enzyme family of
endoproteases. Yeast axl1 mutants showed a defect in
a-factor pheromone secretion, and a probable site of
processing by Axl1p was identified within the a-factor
precursor. In addition, Axl1p appears to function as a morphogenetic
determinant for axial bud site selection. Amino acid substitutions
within the presumptive active site of Axl1p caused defects in
propheromone processing but failed to perturb bud site selection. Thus,
Axl1p has been shown to participate in the dual regulation of distinct
signaling pathways, and a member of the insulinase family has been
implicated in propeptide processing.
N. Adames, K. Blundell, C. Boone, Institute of Molecular Biology
and Biochemistry, Simon Fraser University, Burnaby, British Columbia,
V5A 1S6, Canada.
M. N. Ashby, Department of Molecular and Cell Biology, University of
California, Berkeley, CA 94720, USA.
(1) To whom correspondence should be addressed.
THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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142, 1473-1485
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PNAS
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Genes & Dev.
10, 777-793
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- NRD convertase: a putative processing endoprotease associated with the axoneme and the manchette in late spermatids.
- V Chesneau, A Prat, D Segretain, V Hospital, A Dupaix, T Foulon, B Jegou, and P Cohen (1996)
J. Cell Sci.
109, 2737-2745
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- Programming of Cell Polarity in Budding Yeast by Endogenous and Exogenous Signals.
- I. Herskowitz, H.-O. Park, S. Sanders, N. Valtz, and M. Peter (1995)
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60, 717-727
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