Cargo selection into COPII vesicles is driven by the Sec24p subunit
Copyright policy )Cargo selection into COPII vesicles is driven by the Sec24p subunit
Transport of secretory proteins out of the endoplasmic reticulum (ER) is mediated by vesicles generated by the COPII coat complex. In order to understand how cargo molecules are selected by this cytoplasmic coat, we investigated the functional role of the Sec24p homolog, Lst1p. We show that Lst1p can function as a COPII subunit independently of Sec24p on native ER membranes and on synthetic liposomes. However, vesicles generated with Lst1p in the absence of Sec24p are deficient in a distinct subset of cargo molecules, including the SNAREs, Bet1p, Bos1p and Sec22p. Consistent with the absence of any SNAREs, these vesicles are unable to fuse with Golgi membranes. Furthermore, unlike Sec24p, Lst1p fails to bind to Bet1p in vitro, indicating a direct correlation between cargo binding and recruitment into vesicles. Our data suggest that the principle role of Sec24p is to discriminate cargo molecules for incorporation into COPII vesicles.
- University of California, Berkeley United States
- University of California System United States
- Centre national de la recherche scientifique France
- Howard Hughes Medical Institute United States
- University of California, San Francisco United States
Saccharomyces cerevisiae Proteins, Vesicular Transport Proteins, Membrane Proteins, Membrane Transport Proteins, Saccharomyces cerevisiae, Membrane Fusion, Protein Subunits, Protein Transport, Structure-Activity Relationship, Liposomes, Qc-SNARE Proteins, COP-Coated Vesicles, SNARE Proteins, Monomeric GTP-Binding Proteins
Saccharomyces cerevisiae Proteins, Vesicular Transport Proteins, Membrane Proteins, Membrane Transport Proteins, Saccharomyces cerevisiae, Membrane Fusion, Protein Subunits, Protein Transport, Structure-Activity Relationship, Liposomes, Qc-SNARE Proteins, COP-Coated Vesicles, SNARE Proteins, Monomeric GTP-Binding Proteins
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