Here we identify Mon1p as being essential for the cvt-pathway and autophagy. Thus, mon1Delta cells are impaired in proaminopeptidase I maturation and homozygous diploid mon1Delta cells do not sporulate. Quantitative autophagy measurements suggest a complete autophagy block. The autophagosomal marker protein GFP-Aut7p accumulates in mon1Delta cells at punctate structures outside the vacuole. Furthermore, proaminopeptidase I accumulates in mon1Delta cells in a proteinase-protected form. Our data demonstrate that mon1Delta cells are defective in the fusion of cvt-vesicles and autophagosomes with the vacuole. Consistent with this, GFP-Mon1p localizes to the cytosol and to punctate structures within the cytosol.
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Mutations in the Saccharomyces cerevisiae vacuolar fusion proteins Ccz1, Mon1 and Ypt7 cause defects in cell cycle progression in a num1Delta background.
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Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland.
The proteins Ccz1 and Mon1 are known to function together with the Rab-GTPase Ypt7 in membrane fusion reactions at the yeast vacuole. In a genome-wide analysis they have also been found to interact genetically with the nuclear-migration protein Num1. In this study we analyze these synthetic effects and we show that the mutants ccz1Delta num1Delta, mon1Delta num1Delta and ypt7Delta num1Delta exhibit severe defects in cell cycle progression.
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Institute of Biochemistry, University of Stuttgart, Pfaffenwaldring 55, Germany.
Here we identify Mon1p as being essential for the cvt-pathway and autophagy. Thus, mon1Delta cells are impaired in proaminopeptidase I maturation and homozygous diploid mon1Delta cells do not sporulate. Quantitative autophagy measurements suggest a complete autophagy block.
View Article and Find Full Text PDFThe Ccz1-Mon1 protein complex is required for the late step of multiple vacuole delivery pathways.
J Biol Chem
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Department of Molecular, Cellular, and Developmental Biology, Life Sciences Institute, University of Michigan, Ann Arbor, Michigan 48109-1048, USA.
Mon1 and Ccz1 were identified from a gene deletion library as mutants defective in the vacuolar import of aminopeptidase I (Ape1) via the cytoplasm to vacuole targeting (Cvt) pathway. The mon1Delta and ccz1Delta strains also displayed defects in autophagy and pexophagy, degradative pathways that share protein machinery and mechanistic features with the biosynthetic Cvt pathway. Further analyses indicated that Mon1, like Ccz1, was required in nearly all membrane-trafficking pathways where the vacuole represented the terminal acceptor compartment.
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