Journal
FEBS LETTERS
Volume 512, Issue 1-3, Pages 173-179Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(02)02252-4
Keywords
autophagy; cytoplasm to vacuole targeting; aminopeptidase I
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We here identify Mai1p, a homologue of the autophagy protein Aut10p, as a novel component essential for proaminopeptidase I (proAPI) maturation under non-starvation conditions. In mai1Delta cells mature vacuolar proteinases are detectable and vacuolar acidification is normal. In mai1Delta cells autophagy occurs, though at a somewhat reduced level. This is indicated by proAPI maturation during starvation and accumulation of autophagic bodies during starvation with phenylmethylsulfonyl fluoride. Homozygous diploid mai1Delta cells sporulate, but with a slightly reduced frequency. Biologically active Ha-tagged Mai1p, chromosomally expressed under its native promoter, is at least in part peripherally membrane-associated. In indirect immunofluorescence it localizes to the vacuolar membrane or structures nearby. In some cells Ha-tagged Mai1p appears concentrated at regions adjacent to the nucleus. (C) 2002 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.
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