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The Golgi vesicle tether p115 can bind directly to the ER exit site organiser Sec16A.

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Title: The Golgi vesicle tether p115 can bind directly to the ER exit site organiser Sec16A.
Authors: Yakunin I; MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK., Gillingham AK; MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK., Pereira C; Cambridge Institute for Medical Research, University of Cambridge, Cambridge CB2 0XY, UK., Gershlick DC; Cambridge Institute for Medical Research, University of Cambridge, Cambridge CB2 0XY, UK., Munro S; MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Source: Journal of cell science [J Cell Sci] 2026 Jul 01; Vol. 139 (13). Date of Electronic Publication: 2026 Jun 30.
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
Language: English
Journal Info: Publisher: Company of Biologists Country of Publication: England NLM ID: 0052457 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1477-9137 (Electronic) Linking ISSN: 00219533 NLM ISO Abbreviation: J Cell Sci Subsets: MEDLINE
Imprint Name(s): Publication: Cambridge : Company of Biologists
Original Publication: London.
MeSH Terms: Endoplasmic Reticulum*/metabolism , Golgi Apparatus*/metabolism , Vesicular Transport Proteins*/metabolism , Vesicular Transport Proteins*/chemistry , Vesicular Transport Proteins*/genetics , Membrane Proteins*/metabolism, COP-Coated Vesicles/metabolism ; Humans ; Protein Binding ; HeLa Cells ; Protein Transport ; Golgi Matrix Proteins
Abstract: Newly made secretory and membrane proteins exit the endoplasmic reticulum (ER) in COPII vesicles that form at specialised ER exit sites. These exit sites are typically near the early Golgi compartments that receive these vesicles. A key player in the delivery of vesicles to the early Golgi is p115 (also known as USO1), a homodimer with a folded head domain and a coiled-coil tail that is anchored to Golgi membranes. p115 has been shown to capture vesicles and to bind to SNARE proteins to promote membrane fusion. Here, we report that the head domain of human p115 can bind directly to Sec16A, a large scaffolding protein that organises ER sites and promotes COPII vesicle formation. Structural prediction and deletion mapping defined the region of interaction to a conserved motif in the unstructured N-terminal region of Sec16A, and mutations in p115 that block motif binding reduced the efficiency of secretion. This interaction could potentially allow a subset of p115 molecules to reach across from the early Golgi to ER exit sites to contribute to the large-scale organisation of the early secretory pathway.
(© 2026. Published by The Company of Biologists.)
Competing Interests: Competing interests The authors declare no competing or financial interests.
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Grant Information: MC_U105178783 United Kingdom MRC_ Medical Research Council; BB/W005905/1 United Kingdom BB_ Biotechnology and Biological Sciences Research Council; UKRI715 United Kingdom BB_ Biotechnology and Biological Sciences Research Council; Medical Research Council Laboratory of Molecular Biology
Contributed Indexing: Keywords: COPII vesicles; ER exit site; Golgi; Membrane traffic
Substance Nomenclature: 0 (SEC16A protein, human)
0 (Vesicular Transport Proteins)
0 (Membrane Proteins)
162079-20-1 (vesicular transport factor p115)
0 (Golgi Matrix Proteins)
Entry Date(s): Date Created: 20260522 Date Completed: 20260630 Latest Revision: 20261001
Update Code: 20261001
PubMed Central ID: PMC7619307
DOI: 10.1242/jcs.264894
PMID: 42169630
Database: MEDLINE
Description
ISSN:1477-9137
DOI:10.1242/jcs.264894