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Membrane detachment is not essential for COG complex function
The conserved oligomeric Golgi (COG) complex is a vesicle tether of the “complexes associated with tethering containing helical rods” family, which functions on the cytoplasmic side of Golgi. It is currently unknown whether COG function, or function of any multisubunit vesicular tether, depends on c...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5896934/ https://www.ncbi.nlm.nih.gov/pubmed/29467253 http://dx.doi.org/10.1091/mbc.E17-11-0694 |
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author | Climer, Leslie K. Pokrovskaya, Irina D. Blackburn, Jessica B. Lupashin, Vladimir V. |
author_facet | Climer, Leslie K. Pokrovskaya, Irina D. Blackburn, Jessica B. Lupashin, Vladimir V. |
author_sort | Climer, Leslie K. |
collection | PubMed |
description | The conserved oligomeric Golgi (COG) complex is a vesicle tether of the “complexes associated with tethering containing helical rods” family, which functions on the cytoplasmic side of Golgi. It is currently unknown whether COG function, or function of any multisubunit vesicular tether, depends on cycling between the membrane and cytosol. Therefore, we permanently anchored key subunits of COG subcomplexes (COG4, COG7, and COG8) to Golgi membranes using transmembrane protein TMEM115 (TMEM-COG). All TMEM-COG subunits tested were Golgi localized, integrated into the COG complex, and stabilized membrane association of endogenous subunits. Interestingly, TMEM-COG4 and TMEM-COG7 equally rescued COG function in organization of Golgi markers, glycosylation, and abundance of COG-sensitive proteins. In contrast, TMEM-COG8 was not as effective, indicating that N-terminal attachment of COG8 interfered with overall COG structure and function, and none of the TMEM-COG subunits rescued the abnormal Golgi architecture caused by COG knockout. Collectively, these data indicate that both subcomplexes of the COG complex can perform most of COG function when permanently attached to membranes and that the cytosolic pool of COG is not completely essential to COG function. |
format | Online Article Text |
id | pubmed-5896934 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-58969342018-06-30 Membrane detachment is not essential for COG complex function Climer, Leslie K. Pokrovskaya, Irina D. Blackburn, Jessica B. Lupashin, Vladimir V. Mol Biol Cell Articles The conserved oligomeric Golgi (COG) complex is a vesicle tether of the “complexes associated with tethering containing helical rods” family, which functions on the cytoplasmic side of Golgi. It is currently unknown whether COG function, or function of any multisubunit vesicular tether, depends on cycling between the membrane and cytosol. Therefore, we permanently anchored key subunits of COG subcomplexes (COG4, COG7, and COG8) to Golgi membranes using transmembrane protein TMEM115 (TMEM-COG). All TMEM-COG subunits tested were Golgi localized, integrated into the COG complex, and stabilized membrane association of endogenous subunits. Interestingly, TMEM-COG4 and TMEM-COG7 equally rescued COG function in organization of Golgi markers, glycosylation, and abundance of COG-sensitive proteins. In contrast, TMEM-COG8 was not as effective, indicating that N-terminal attachment of COG8 interfered with overall COG structure and function, and none of the TMEM-COG subunits rescued the abnormal Golgi architecture caused by COG knockout. Collectively, these data indicate that both subcomplexes of the COG complex can perform most of COG function when permanently attached to membranes and that the cytosolic pool of COG is not completely essential to COG function. The American Society for Cell Biology 2018-04-15 /pmc/articles/PMC5896934/ /pubmed/29467253 http://dx.doi.org/10.1091/mbc.E17-11-0694 Text en © 2018 Climer et al. “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology. http://creativecommons.org/licenses/by-nc-sa/3.0/ This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License. |
spellingShingle | Articles Climer, Leslie K. Pokrovskaya, Irina D. Blackburn, Jessica B. Lupashin, Vladimir V. Membrane detachment is not essential for COG complex function |
title | Membrane detachment is not essential for COG complex function |
title_full | Membrane detachment is not essential for COG complex function |
title_fullStr | Membrane detachment is not essential for COG complex function |
title_full_unstemmed | Membrane detachment is not essential for COG complex function |
title_short | Membrane detachment is not essential for COG complex function |
title_sort | membrane detachment is not essential for cog complex function |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5896934/ https://www.ncbi.nlm.nih.gov/pubmed/29467253 http://dx.doi.org/10.1091/mbc.E17-11-0694 |
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