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Vol. 11, Issue 11, 3737-3749, November 2000
Medical Research Council Laboratory of Molecular Biology, Cambridge
CB2 2QH, United Kingdom
Membrane proteins transported to the yeast vacuole can have two
fates. Some reach the outer vacuolar membrane, whereas others enter
internal vesicles, which form in late endosomes, and are ultimately
degraded. The vacuolar SNAREs Nyv1p and Vam3p avoid this fate by using
the AP-3-dependent pathway, which bypasses late endosomes, but the
endosomal SNARE Pep12p must avoid it more directly. Deletion analysis
revealed no cytoplasmic sequences necessary to prevent the
internalization of Pep12p in endosomes. However, introduction of acidic
residues into the cytoplasmic half of the transmembrane domain created
a dominant internalization signal. In other contexts, this same feature
diverted proteins from the Golgi to endosomes and slowed their exit
from the endoplasmic reticulum. The more modestly polar transmembrane
domains of Sec12p and Ufe1p, which normally serve to hold these
proteins in the endoplasmic reticulum, also cause Pep12p to be
internalized, as does that of the vacuolar protein Cps1p. It seems that
quality control mechanisms recognize polar transmembrane domains at
multiple points in the secretory and endocytic pathways and in
endosomes sort proteins for subsequent destruction in the vacuole.
These mechanisms may minimize the damaging effects of abnormally
exposed polar residues while being exploited for the localization of
some normal proteins.
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