Please use this identifier to cite or link to this item:
https://doi.org/10.1242/jcs.136754
DC Field | Value | |
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dc.title | TMEM115 is an integral membrane protein of the Golgi complex involved in retrograde transport | |
dc.contributor.author | Ong, Y.S | |
dc.contributor.author | Tran, T.H.T | |
dc.contributor.author | Gounkov, N.V | |
dc.contributor.author | Hong, W | |
dc.date.accessioned | 2020-10-26T07:23:01Z | |
dc.date.available | 2020-10-26T07:23:01Z | |
dc.date.issued | 2014 | |
dc.identifier.citation | Ong, Y.S, Tran, T.H.T, Gounkov, N.V, Hong, W (2014). TMEM115 is an integral membrane protein of the Golgi complex involved in retrograde transport. Journal of Cell Science 127 (13) : 2825-2839. ScholarBank@NUS Repository. https://doi.org/10.1242/jcs.136754 | |
dc.identifier.issn | 0021-9533 | |
dc.identifier.uri | https://scholarbank.nus.edu.sg/handle/10635/180178 | |
dc.description.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. Coimmunoprecipitation 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. © 2014. | |
dc.publisher | Company of Biologists Ltd | |
dc.rights | Attribution 4.0 International | |
dc.rights.uri | http://creativecommons.org/licenses/by/4.0/ | |
dc.source | Unpaywall 20201031 | |
dc.subject | agglutinin | |
dc.subject | beta cop protein | |
dc.subject | brefeldin A | |
dc.subject | coat protein complex I | |
dc.subject | conserved oligomeric golgi 3 complex protein | |
dc.subject | dimer | |
dc.subject | endoplasmic reticulum golgi intermediate compartment protein 53 | |
dc.subject | golgi a4 protein | |
dc.subject | golgin A5 protein | |
dc.subject | helix pomatia agglutinin | |
dc.subject | lectin | |
dc.subject | membrane protein | |
dc.subject | oligomer | |
dc.subject | peanut agglutinin | |
dc.subject | protein | |
dc.subject | TMEM 115 protein | |
dc.subject | unclassified drug | |
dc.subject | membrane protein | |
dc.subject | PL6 protein, human | |
dc.subject | protein binding | |
dc.subject | vesicular transport protein | |
dc.subject | amino terminal sequence | |
dc.subject | article | |
dc.subject | carboxy terminal sequence | |
dc.subject | cellular distribution | |
dc.subject | chromosome | |
dc.subject | controlled study | |
dc.subject | cytoplasm | |
dc.subject | endoplasmic reticulum | |
dc.subject | enzyme glycosylation | |
dc.subject | gene mutation | |
dc.subject | gene overexpression | |
dc.subject | gene silencing | |
dc.subject | Golgi complex | |
dc.subject | Helix pomatia | |
dc.subject | human | |
dc.subject | human cell | |
dc.subject | immunofluorescence | |
dc.subject | immunoprecipitation | |
dc.subject | in vitro study | |
dc.subject | membrane transport | |
dc.subject | priority journal | |
dc.subject | protein binding | |
dc.subject | protein expression | |
dc.subject | protein glycosylation | |
dc.subject | protein interaction | |
dc.subject | protein targeting | |
dc.subject | signal transduction | |
dc.subject | animal | |
dc.subject | Golgi complex | |
dc.subject | HeLa cell line | |
dc.subject | metabolism | |
dc.subject | mouse | |
dc.subject | protein transport | |
dc.subject | Animals | |
dc.subject | Golgi Apparatus | |
dc.subject | HeLa Cells | |
dc.subject | Humans | |
dc.subject | Membrane Proteins | |
dc.subject | Mice | |
dc.subject | Protein Binding | |
dc.subject | Protein Transport | |
dc.subject | Vesicular Transport Proteins | |
dc.type | Article | |
dc.contributor.department | INSTITUTE OF MOLECULAR & CELL BIOLOGY | |
dc.description.doi | 10.1242/jcs.136754 | |
dc.description.sourcetitle | Journal of Cell Science | |
dc.description.volume | 127 | |
dc.description.issue | 13 | |
dc.description.page | 2825-2839 | |
dc.published.state | Published | |
Appears in Collections: | Staff Publications Elements |
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