ArticleFrontiers in cell and developmental biology2014
Distinct N-terminal regions of the exomer secretory vesicle cargo Chs3 regulate its trafficking itinerary.
Article in Frontiers in cell and developmental biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 11 citations in OpenAlex.
- Rethinking the Yeast Endomembrane System.Sub-cellular biochemistry · 2026Review
- The N-terminal disordered region of ChsB regulates its efficient transport to the hyphal apical surface in Aspergillus nidulans.Current genetics · 2023Article
- Exomer complex regulates protein traffic at the TGN through differential interactions with cargos and clathrin adaptor complexes.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021Article
- Calcineurin-dependent regulation of endocytosis by a plasma membrane ubiquitin ligase adaptor, Rcr1.The Journal of cell biology · 2020Article
- The Functional Specialization of Exomer as a Cargo Adaptor During the Evolution of Fungi.Genetics · 2018Article
- Involvement of the exomer complex in the polarized transport of Ena1 required forMolecular biology of the cell · 2017Article
- A CDC25 family protein phosphatase gates cargo recognition by the Vps26 retromer subunit.eLife · 2017Article
- Maintaining protein homeostasis: early and late endosomal dual recycling for the maintenance of intracellular pools of the plasma membrane protein Chs3.Molecular biology of the cell · 2016Article
- Cargo adaptors: structures illuminate mechanisms regulating vesicle biogenesis.Trends in cell biology · 2015Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Cells transport integral membrane proteins between organelles by sorting them into vesicles. Cargo adaptors act to recognize sorting signals in transmembrane cargos and to interact with coat complexes that aid in vesicle biogenesis. No coat proteins have yet been identified that generate secretory vesicles from the trans-Golgi network (TGN) to the plasma membrane, but the exomer complex has been identified as a cargo adaptor complex that mediates transport of several proteins in this pathway. Chs3, the most well-studied exomer cargo, cycles between the TGN and the plasma membrane in synchrony with the cell cycle, providing an opportunity to study regulation of proteins that cycle in response to signaling. Here we show that different segments of the Chs3 N-terminus mediate distinct trafficking steps. Residues 10-27, known to mediate retention, also appear to play a role in internalization. Residues 28-52 are involved in transport to the plasma membrane and recycling out of endosomes to prevent degradation in the vacuole. We also present the crystal structure of residues 10-27 bound to the exomer complex, suggesting different cargo adaptors could compete for binding to this segment, providing a potential mechanism for regulation.
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