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(Received for publication, November 7, 1995; and in revised form, January 10, 1996) When glucose-starved cells are replenished with glucose, the key
gluconeogenic enzyme, fructose-1,6-bisphosphatase (FBPase), is
selectively targeted from the cytosol to the yeast lysosome (vacuole)
for degradation. The glucose-induced targeting of FBPase to the vacuole
for degradation occurs in cells grown under a variety of metabolic
conditions. Immunoelectron microscopic studies demonstrate that the
uptake of FBPase by the vacuole is mediated in part by an autophagic
process. FBPase can be found on the vacuolar membrane and also at the
sites of membrane invaginations. Furthermore, FBPase is associated with
different forms of vesicles, which are induced to accumulate inside the
vacuole. We have identified peroxisomes as the organelles that are
delivered to the vacuole for degradation when cells are replenished
with glucose. Ultrastructural studies indicate that peroxisomes are
engulfed by the vacuole by an autophagic process, leading to the
destruction of whole organelles in the vacuole. Furthermore, the
galactose transporter (Gal2p) is also delivered from the plasma
membrane to the vacuole for degradation in response to glucose. Gal2p
is delivered to the vacuole through the endocytic pathway, as mutants
defective in receptor-mediated endocytosis fail to degrade Gal2p in
response to glucose.
Volume 271,
Number 17,
Issue of April 26, 1996 pp. 9934-9941
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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