ArticleJournal of cell science2014
TMEM115 is an integral membrane protein of the Golgi complex involved in retrograde transport.
Article in Journal of cell science, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 18 citations in OpenAlex.
- CRISPR screening identifies DTX4 governing alveolar macrophage cholesterol efflux in pulmonary alveolar proteinosis.JCI insight · 2026Article
- Identification of TMEM115 as a tumor suppressor gene and clinical prognostic factor that influences TERT expression in pancreatic cancer.Scientific reports · 2026Article
- Variations in rumen microbiota and host genome impacted feed efficiency in goat breeds.Frontiers in microbiology · 2025Article
- TMEM115: a promising marker for glioma immunotherapy and prognosis.Frontiers in immunology · 2025Article
- AMPK associates with and causes fragmentation of the Golgi by phosphorylating the guanine nucleotide exchange factor GBF1.Journal of cell science · 2024Article
- Functional unknomics: Systematic screening of conserved genes of unknown function.PLoS biology · 2023Article
- Golgi-IP, a tool for multimodal analysis of Golgi molecular content.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- RNAseq Analysis of FABP4 Knockout Mouse Hippocampal Transcriptome Suggests a Role for WNT/β-Catenin in Preventing Obesity-Induced Cognitive Impairment.International journal of molecular sciences · 2023Article
- Sugary Logistics Gone Wrong: Membrane Trafficking and Congenital Disorders of Glycosylation.International journal of molecular sciences · 2020Review
- Membrane detachment is not essential for COG complex function.Molecular biology of the cell · 2018Article
- Rhomboids, signalling and cell biology.Biochemical Society transactions · 2016Review
- Bridging the Gap between Glycosylation and Vesicle Traffic.Frontiers in cell and developmental biology · 2016Review
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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 complex. Biochemical and cell biological analysis suggested that TMEM115 has four candidate transmembrane domains located in the N-terminal region. Both the N- and C-terminal domains are oriented towards the cytoplasm. Immunofluorescence 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 conserved oligomeric Golgi (COG) complex. Co-immunoprecipitation and in vitro binding experiments reveals that TMEM115 interacts with the COG complex, and might self-interact to form dimers or oligomers. A short region (residues 206-229) immediately to the C-terminal side of the fourth transmembrane domain is both necessary and sufficient for Golgi targeting. Knockdown of TMEM115 also reduces the binding of the lectins peanut agglutinin (PNA) and Helix pomatia agglutinin (HPA), suggesting an altered O-linked glycosylation profile. These results establish that TMEM115 is an integral membrane protein of the Golgi stack regulating Golgi-to-ER retrograde transport and is likely to be part of the machinery of the COG complex.
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Registered trials
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