TMEM115 as an integral membrane protein of the Golgi apparatus involved in retrograde transport
Open accessAbstract
Searching and evaluating the Human Protein Atlas for transmembrane proteins enabled us to identify an integral membrane protein, TMEM115 that is enriched in the Golgi apparatus. Biochemical and cell biological analysis suggests that TMEM115 has 4 candidate transmembrane domains located at the N-terminal region. Both the N- and C-terminal domains are oriented towards the cytoplasm. Immunofluoresence analysis supports that TMEM115 is enriched in the Golgi cisternae. Functionally, TMEM115 knockdown or overexpression delays Brefeldin-A induced Golgi-to-ER retrograde transport, phenocopying cells with mutations or silencing of the COG complex. Co-immunoprecipitation and in vitro binding experiments reveals that TMEM115 interacts with COG complex, and may self-interact to form dimers or oligomers. A short region (residues 206–229) immediately to the C-terminal side of the 4th transmembrane domain is both necessary and sufficient for Golgi targeting. Knockdown of TMEM115 also reduces the binding of lectins PNA and HPA, suggesting an altered O-linked glycosylation profile. These results establish that TMEM115 is a novel integral membrane protein of the Golgi stack regulating Golgi-ER retrograde transport and is likely part of the machinery of the COG complex.
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The yeast ortholog of CG13784 (ANY1) has been found to suppress loss of lipid flippases that act in endosome-to-Golgi recycling.
“the yeast ortholog of CG13784 (ANY1) has been found to suppress loss of lipid flippases that act in endosome-to-Golgi recycling [67,68].”
From Functional unknomics: Systematic screening of conserved genes of unknown function (2023) · cites this paper as [67]
The Introduction discusses retrograde endosome-to-Golgi transport, but it does not connect that pathway to ANY1, CG13784, or lipid flippases. Searches of our full-text copy for those terms and for suppression of flippase loss found no passage addressing the claimed finding; no page number is available in the copy. (LLM, conf=0.74)
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- Authors
- Ong, Y. S., Tran, T. H. T., Gounko, N. V., & Hong, W.
- Affiliations
- Institute of Molecular and Cell Biology (SG)
- Institute of Medical Biology (SG)
- National University of Singapore (SG)
- Corresponding author
- Hong, Wanjin
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2014-01-01
- Volume
- 127
- Issue
- Pt 13
- Pages
- 2825-39
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- PMC
- PMC4077589
- OpenAlex
- W2157098888
- Cited by
- 18
- References
- 92
- Citations by year
- 2026: 1 · 2025: 2 · 2023: 4 · 2022: 2 · 2020: 3 · 2018: 2 · 2017: 1 · 2016: 3
- FWCI
- 0.66
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Cell Science (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- National University of Singapore (submittedVersion, cc-by)
- Lirias (submittedVersion)
- HighWire Press Open Archive (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- Golgi apparatus, retrograde transport, Golgi-to-ER transport, conserved oligomeric Golgi complex, integral membrane proteins, transmembrane domain, Golgi targeting, O-glycosylation, peanut agglutinin, Helix pomatia agglutinin
- MeSH terms
- Animals, Golgi Apparatus, HeLa Cells, Humans, Membrane Proteins, Protein Binding, Protein Transport, Vesicular Transport Proteins, Mice
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