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10.1242/jcs.175273 http://scihub22266oqcxt.onion/10.1242/jcs.175273 C4852765!4852765 !26906412     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26906412 &cmd=llinks): Failed to open stream: HTTP request failed! 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Transmembrane protein TMEM170A is a newly discovered regulator of ER and nuclear envelope morphogenesis in human cells |pdf=|usr=}}{{26906412 }} gab.com Text Transmembrane protein TMEM170A is a newly discovered regulator of ER and nuclear envelope morphogenesis in human cells JO: J Cell Sci http://www.kidney.de/pget.php?&tw=1&pmid=26906412 #FOAvip The mechanism of endoplasmic reticulum (ER) morphogenesis is incompletely understood. ER tubules are shaped by the reticulons (RTNs) and DP1/Yop1p family members, but the mechanism of ER sheet formation is much less clear. Here, we characterize TMEM170A, a human transmembrane protein, which localizes in ER and nuclear envelope membranes. Silencing or overexpressing TMEM170A in HeLa K cells alters ER shape and morphology. Ultrastructural analysis reveals that downregulation of TMEM170A specifically induces tubular ER formation, whereas overexpression of TMEM170A induces ER sheet formation, indicating that TMEM170A is a newly discovered ER-sheet-promoting protein. Additionally, downregulation of TMEM170A alters nuclear shape and size, decreases the density of nuclear pore complexes (NPCs) in the nuclear envelope and causes either a reduction in inner nuclear membrane (INM) proteins or their relocalization to the ER. TMEM170A interacts with RTN4, a member of the reticulon family; simultaneous co-silencing of TMEM170A and RTN4 rescues ER, NPC and nuclear-envelope-related phenotypes, implying that the two proteins have antagonistic effects on ER membrane organization, and nuclear envelope and NPC formation. Twit Text FOAVip Transmembrane protein TMEM170A is a newly discovered regulator of ER and nuclear envelope morphogenesis in human cells ????J Cell Sci http://www.kidney.de/pget.php?&tw=1&pmid=26906412 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26906412 #FOAvip English Wikipedia <ref>{{Cite pmid|26906412 }}</ref> Transmembrane protein TMEM170A is a newly discovered regulator of ER and nuclear envelope morphogenesis in human cells #MMPMID26906412 Christodoulou A ; Santarella-Mellwig R ; Santama N ; Mattaj IW J Cell Sci 2016[Apr]; 129 (8 ): 1552-65 PMID26906412 show ga The mechanism of endoplasmic reticulum (ER) morphogenesis is incompletely understood. ER tubules are shaped by the reticulons (RTNs) and DP1/Yop1p family members, but the mechanism of ER sheet formation is much less clear. Here, we characterize TMEM170A, a human transmembrane protein, which localizes in ER and nuclear envelope membranes. Silencing or overexpressing TMEM170A in HeLa K cells alters ER shape and morphology. Ultrastructural analysis reveals that downregulation of TMEM170A specifically induces tubular ER formation, whereas overexpression of TMEM170A induces ER sheet formation, indicating that TMEM170A is a newly discovered ER-sheet-promoting protein. Additionally, downregulation of TMEM170A alters nuclear shape and size, decreases the density of nuclear pore complexes (NPCs) in the nuclear envelope and causes either a reduction in inner nuclear membrane (INM) proteins or their relocalization to the ER. TMEM170A interacts with RTN4, a member of the reticulon family; simultaneous co-silencing of TMEM170A and RTN4 rescues ER, NPC and nuclear-envelope-related phenotypes, implying that the two proteins have antagonistic effects on ER membrane organization, and nuclear envelope and NPC formation. |Endoplasmic Reticulum/*physiology [MESH] |HeLa Cells [MESH] |Humans [MESH] |Membrane Proteins/genetics/*metabolism [MESH] |Nogo Proteins/genetics/*metabolism [MESH] |Nuclear Envelope/*metabolism [MESH] |Nuclear Pore/metabolism [MESH] |Protein Transport/genetics [MESH] |RNA, Small Interfering/genetics [MESH]Transmembrane protein TMEM170A is a newly discovered regulator of ER a(epmc).pdf DeepDyve Pubget Overpricing