ArticleThe Journal of biological chemistry2009
Molecular dissection of Erv26p identifies separable cargo binding and coat protein sorting activities.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 27 citations in OpenAlex.
- JAGN1, tetraspanins, and Erv proteins: is common topology indicative of common function in cargo sorting?American journal of physiology. Cell physiology · 2020Article
- Article
- Folding and Misfolding of Human Membrane Proteins in Health and Disease: From Single Molecules to Cellular Proteostasis.Chemical reviews · 2019Article
- Two novel effectors of trafficking and maturation of the yeast plasma membrane HTraffic (Copenhagen, Denmark) · 2017Article
- The Golgin protein Coy1 functions in intra-Golgi retrograde transport and interacts with the COG complex and Golgi SNAREs.Molecular biology of the cell · 2017Article
- Identification of rice cornichon as a possible cargo receptor for the Golgi-localized sodium transporter OsHKT1;3.Journal of experimental botany · 2015Article
- Article
- Isoform-selective oligomer formation of Saccharomyces cerevisiae p24 family proteins.The Journal of biological chemistry · 2013Article
- Vesicle-mediated export from the ER: COPII coat function and regulation.Biochimica et biophysica acta · 2013Review
- Review
- Proteostasis strategies for restoring alpha1-antitrypsin deficiency.Proceedings of the American Thoracic Society · 2010Review
- Svp26 facilitates endoplasmic reticulum to golgi transport of a set of mannosyltransferases in Saccharomyces cerevisiae.The Journal of biological chemistry · 2010Article
- Chaperone requirements for biosynthesis of the trypanosome variant surface glycoprotein.PloS one · 2010Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Efficient export of secretory alkaline phosphatase (ALP) from the endoplasmic reticulum depends on the conserved transmembrane sorting adaptor Erv26p/Svp26p. In the present study we investigated the mechanism by which Erv26p couples pro-ALP to the coat protein complex II (COPII) export machinery. Site-specific mutations were introduced into Erv26p, and mutant proteins were assessed in cell-free assays that monitor interactions with pro-ALP cargo and packaging into COPII vesicles. Mutations in the second and third loop domains of Erv26p inhibited interaction with pro-ALP, whereas mutations in the C-terminal tail sequence influenced incorporation into COPII vesicles and subcellular distribution. Interestingly mutations in the second loop domain also influenced Erv26p homodimer associations. Finally we demonstrated that Ktr3p, a cis-Golgi-localized mannosyltransferase, also relies on Erv26p for efficient COPII-dependent export from the endoplasmic reticulum. These findings demonstrate that Erv26p acts as a protein sorting adaptor for a variety of Type II transmembrane cargo proteins and requires domain-specific interactions with both cargo and coat subunits to promote efficient secretory protein transport.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.