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Multiple sorting pathways between the late Golgi and the vacuole in yeast
1Institute of Molecular Biology, University of Oregon, Eugene, OR 97403-1229, USA.
Biochimica Et Biophysica Acta
|August 26, 1998
Summary
Two distinct protein transport pathways, CPY and ALP, deliver proteins from the Golgi to the vacuole. The ALP pathway bypasses the prevacuolar compartment (PVC) and is signal-mediated, unlike the CPY pathway.
Area of Science:
- Cell Biology
- Molecular Biology
- Protein Trafficking
Background:
- Proteins synthesized in the Golgi are sorted to various destinations, including the cell surface and vacuole.
- Two primary routes, the CPY pathway and the ALP pathway, mediate Golgi-to-vacuole transport.
- The CPY pathway involves transit through an endosomal/prevacuolar compartment (PVC), while the ALP pathway bypasses the PVC.
Purpose of the Study:
- To investigate the distinct mechanisms and regulatory proteins involved in Golgi-to-vacuole protein sorting.
- To identify signals and protein factors that direct proteins to either the CPY or ALP pathway.
- To elucidate the molecular machinery, including SNARE complexes, governing vacuolar transport.
Main Methods:
- Analysis of protein sorting pathways using genetic and molecular approaches.
- Identification of genes regulating CPY and ALP pathway specificity.
- Characterization of SNARE complexes involved in transport to the PVC and vacuole.
Main Results:
- The ALP pathway is signal-mediated and saturable, distinct from the CPY pathway.
- Specific genes have been identified for each pathway, with others affecting both.
- Progress made in identifying SNARE proteins crucial for Golgi-to-PVC and vacuole fusion.
Conclusions:
- At least two distinct pathways (CPY and ALP) exist for Golgi-to-vacuole protein transport.
- Regulation of vacuolar targeting involves pathway-specific and common factors.
- SNARE complexes play critical roles in mediating vesicle fusion events during vacuolar transport.