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Vol. 10, Issue 9, 2879-2889, September 1999
and
*Zentrum für Biochemie und Molekulare Zellbiologie, Abteilung
Biochemie 2, Georg-August Universität Göttingen, D-37073
Göttingen, Germany; and In eukaryotic cells, both lysosomal and nonlysosomal pathways are
involved in degradation of cytosolic proteins. The physiological condition of the cell often determines the degradation pathway of a
specific protein. In this article, we show that cytosolic proteins can
be taken up and degraded by isolated Saccharomyces cerevisiae vacuoles. After starvation of the cells, protein
uptake increases. Uptake and degradation are temperature dependent and show biphasic kinetics. Vacuolar protein import is dependent on cytosolic heat shock proteins of the hsp70 family and on
protease-sensitive component(s) on the outer surface of vacuoles.
Degradation of the imported cytosolic proteins depends on a functional
vacuolar ATPase. We show that the cytosolic isoform of yeast
glyceraldehyde-3-phosphate dehydrogenase is degraded via this pathway.
This import and degradation pathway is reminiscent of the protein
transport pathway from the cytosol to lysosomes of mammalian cells.
Instituto de
Investigaciones Citológicas, Fundación Valenciana de
Investigaciones Biomédicas, 46010-Valencia, Spain
Corresponding author. E-mail address:
Horst{at}uni-bc2.gwdg.de.
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