ArticleMolecular biology of the cell2002
Selective protein exit from yeast endoplasmic reticulum in absence of functional COPII coat component Sec13p.
Article in Molecular biology of the cell, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 37 citations in OpenAlex.
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- Proper secretion of the serpin antithrombin relies strictly on thiol-dependent quality control.The Journal of biological chemistry · 2019Article
- Vesicle-mediated ER export of proteins and lipids.Biochimica et biophysica acta · 2012Review
- A novel multiprotein complex is required to generate the prechylomicron transport vesicle from intestinal ER.Journal of lipid research · 2010Article
- Mechanisms of regulated unconventional protein secretion.Nature reviews. Molecular cell biology · 2009Review
- A block in endoplasmic reticulum-to-Golgi trafficking inhibits phospholipid synthesis and induces neutral lipid accumulation.The Journal of biological chemistry · 2008Article
- SEC18/NSF-independent, protein-sorting pathway from the yeast cortical ER to the plasma membrane.The Journal of cell biology · 2005Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sec13p has been thought to be an essential component of the COPII coat, required for exit of proteins from the yeast endoplasmic reticulum (ER). We show herein that normal function of Sec13p was not required for ER exit of the Hsp150 glycoprotein. Hsp150 was secreted to the medium under restrictive conditions in a sec13-1 mutant. The COPII components Sec23p and Sec31p and the GTP/GDP exchange factor Sec12p were required in functional form for secretion of Hsp150. Hsp150 leaves the ER in the absence of retrograde COPI traffic, and the responsible determinant is a peptide repeated 11 times in the middle of the Hsp150 sequence. Herein, we localized the sorting determinant for Sec13p-independent ER exit to the C-terminal domain. Sec13p-dependent invertase left the ER in the absence of normal Sec13p function, when fused to the C-terminal domain of Hsp150, demonstrating that this domain contained an active mediator of Sec13p-independent secretion. Thus, Hsp150 harbors two different signatures that regulate its ER exit. Our data show that transport vesicles lacking functional Sec13p can carry out ER-to-Golgi transport, but select only specific cargo protein(s) for ER exit.
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