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A role for Yip1p in COPII vesicle biogenesis
Matthew Heidtman1, Catherine Z Chen, Ruth N Collins
1Department of Biochemistry, Dartmouth Medical School, Hanover, NH 03755, USA.
The Journal of Cell Biology
|October 15, 2003
Summary
Yeast Ypt1p-interacting protein (Yip1p) is crucial for COPII vesicle biogenesis during early secretory pathway transport. Antibodies against Yip1p inhibit ER to Golgi transport, highlighting its role in vesicle budding.
Area of Science:
- Cell Biology
- Molecular Biology
- Protein Trafficking
Background:
- Yeast Ypt1p-interacting protein (Yip1p) is a transmembrane protein interacting with Rab GTPases.
- Yip1p has been identified in ER-derived transport vesicles, suggesting a role in the early secretory pathway.
Purpose of the Study:
- To investigate the function of Yip1p in protein transport through the early secretory pathway.
- To determine if Yip1p plays a direct role in ER to Golgi transport.
Main Methods:
- Utilized a cell-free assay to study ER to Golgi protein transport.
- Employed affinity-purified antibodies against Yip1p to assess its function.
- Analyzed temperature-sensitive yip1-4 mutant strains and performed genetic interaction analyses.
- Conducted ordering experiments with ER membranes and COPII proteins.
Main Results:
- Antibodies against Yip1p specifically inhibited COPII-dependent budding from the ER.
- The yip1-4 mutant accumulated ER membranes at nonpermissive temperatures, without vesicle intermediate accumulation.
- Genetic analyses supported a role for Yip1p in ER budding.
- Early addition of COPII proteins reduced sensitivity to anti-Yip1p antibodies, indicating an early requirement for Yip1p.
Conclusions:
- Yip1p plays a significant, previously unrecognized role in COPII vesicle biogenesis.
- Yip1p is essential for the budding of transport vesicles from the ER.