Role of Sec24 isoforms in selective export of membrane proteins from the endoplasmic reticulum
Open accessAbstract
Sec24 of the COPII (coat protein complex II) vesicle coat mediates the selective export of membrane proteins from the endoplasmic reticulum (ER) in yeast. Human cells express four Sec24 isoforms, but their role is unknown. Here, we report the differential effects of Sec24 isoform-specific silencing on the transport of the membrane reporter protein ERGIC-53 (ER-Golgi intermediate compartment-53) carrying the cytosolic ER export signals di-phenylalanine, di-tyrosine, di-leucine, di-isoleucine, di-valine or terminal valine. Knockdown of single Sec24 isoforms showed dependence of di-leucine-mediated transport on Sec24A, but transport mediated by the other signals was not affected. By contrast, double knockdown of Sec24A with one of the other three Sec24 isoforms impaired all aromatic/hydrophobic signal-dependent transport. Double knockdown of Sec24B/C or Sec24B/D preferentially affected di-leucine-mediated transport, whereas knockdown of Sec24C/D affected di-isoleucine- and valine-mediated transport. The isoform-selective transport correlated with binding preferences of the signals for the corresponding isoforms in vitro. Thus, human Sec24 isoforms expand the repertoire of cargo for signal-mediated ER export, but are in part functionally redundant.
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ER exit codes include LL motifs, bound by the Sec24A isoform, and I/LXM motifs, bound by Sec24D.
“ER exit codes include LL motifs, bound by the Sec24A isoform, and I/LXM motifs, bound by Sec24D (Wendeler et al., 2007; Mancias and Goldberg, 2008).”
From Nicotine up-regulates α4β2 nicotinic receptors and ER exit sites via stoichiometry-dependent chaperoning (2011) · cites this paper as Wendeler et al., 2007
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Self-citation
- Authors
- Wendeler, M. W., Paccaud, J., & Hauri, H.
- Affiliations
- University of Basel (CH)
- OM Pharma (Switzerland) (CH)
- Venue
- The EMBO Reports
- Published
- 2007-01-26
- Volume
- 8
- Issue
- 3
- Pages
- 258-264
- ISSN
- 1469-221X (ISSN-L)
- 1469-3178
- PMC
- PMC1808030
- OpenAlex
- W2119963920
- Cited by
- 197
- References
- 19
- Citations by year
- 2026: 10 · 2025: 13 · 2024: 7 · 2023: 8 · 2022: 10 · 2021: 9 · 2020: 9 · 2019: 5 · 2018: 7 · 2017: 6 · 2016: 6 · 2015: 12 · 2014: 7 · 2013: 14 · 2012: 14
- FWCI
- 5.51
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- EMBO Reports (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Science Foundation
- Universität Basel
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
- Life Sciences › Neuroscience › Sensory Systems › Ion Channels and Receptors
- Keywords
- membrane protein transport, dileucine motif, ERGIC-53, functional redundancy, SEC24A, SEC24C, SEC24D, yeast
- MeSH terms
- Endoplasmic Reticulum, HeLa Cells, Humans, Membrane Proteins, Protein Isoforms, Protein Transport, Protein Sorting Signals, Vesicular Transport Proteins, RNA Interference, RNA, Small Interfering, Mannose-Binding Lectins
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