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Transmembrane and Coiled-Coil Domain Family 1 Is a Novel Protein of the Endoplasmic Reticulum
The endoplasmic reticulum (ER) is a continuous membrane network in eukaryotic cells comprising the nuclear envelope, the rough ER, and the smooth ER. The ER has multiple critical functions and a characteristic structure. In this study, we identified a new protein of the ER, TMCC1 (transmembrane and...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3891740/ https://www.ncbi.nlm.nih.gov/pubmed/24454821 http://dx.doi.org/10.1371/journal.pone.0085206 |
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author | Zhang, Chao Kho, Yik-Shing Wang, Zhe Chiang, Yan Ting Ng, Gary K. H. Shaw, Pang-Chui Wang, Yuzhuo Qi, Robert Z. |
author_facet | Zhang, Chao Kho, Yik-Shing Wang, Zhe Chiang, Yan Ting Ng, Gary K. H. Shaw, Pang-Chui Wang, Yuzhuo Qi, Robert Z. |
author_sort | Zhang, Chao |
collection | PubMed |
description | The endoplasmic reticulum (ER) is a continuous membrane network in eukaryotic cells comprising the nuclear envelope, the rough ER, and the smooth ER. The ER has multiple critical functions and a characteristic structure. In this study, we identified a new protein of the ER, TMCC1 (transmembrane and coiled-coil domain family 1). The TMCC family consists of at least 3 putative proteins (TMCC1–3) that are conserved from nematode to human. We show that TMCC1 is an ER protein that is expressed in diverse human cell lines. TMCC1 contains 2 adjacent transmembrane domains near the C-terminus, in addition to coiled-coil domains. TMCC1 was targeted to the rough ER through the transmembrane domains, whereas the N-terminal region and C-terminal tail of TMCC1 were found to reside in the cytoplasm. Moreover, the cytosolic region of TMCC1 formed homo- or hetero-dimers or oligomers with other TMCC proteins and interacted with ribosomal proteins. Notably, overexpression of TMCC1 or its transmembrane domains caused defects in ER morphology. Our results suggest roles of TMCC1 in ER organization. |
format | Online Article Text |
id | pubmed-3891740 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-38917402014-01-21 Transmembrane and Coiled-Coil Domain Family 1 Is a Novel Protein of the Endoplasmic Reticulum Zhang, Chao Kho, Yik-Shing Wang, Zhe Chiang, Yan Ting Ng, Gary K. H. Shaw, Pang-Chui Wang, Yuzhuo Qi, Robert Z. PLoS One Research Article The endoplasmic reticulum (ER) is a continuous membrane network in eukaryotic cells comprising the nuclear envelope, the rough ER, and the smooth ER. The ER has multiple critical functions and a characteristic structure. In this study, we identified a new protein of the ER, TMCC1 (transmembrane and coiled-coil domain family 1). The TMCC family consists of at least 3 putative proteins (TMCC1–3) that are conserved from nematode to human. We show that TMCC1 is an ER protein that is expressed in diverse human cell lines. TMCC1 contains 2 adjacent transmembrane domains near the C-terminus, in addition to coiled-coil domains. TMCC1 was targeted to the rough ER through the transmembrane domains, whereas the N-terminal region and C-terminal tail of TMCC1 were found to reside in the cytoplasm. Moreover, the cytosolic region of TMCC1 formed homo- or hetero-dimers or oligomers with other TMCC proteins and interacted with ribosomal proteins. Notably, overexpression of TMCC1 or its transmembrane domains caused defects in ER morphology. Our results suggest roles of TMCC1 in ER organization. Public Library of Science 2014-01-14 /pmc/articles/PMC3891740/ /pubmed/24454821 http://dx.doi.org/10.1371/journal.pone.0085206 Text en © 2014 Zhang et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Zhang, Chao Kho, Yik-Shing Wang, Zhe Chiang, Yan Ting Ng, Gary K. H. Shaw, Pang-Chui Wang, Yuzhuo Qi, Robert Z. Transmembrane and Coiled-Coil Domain Family 1 Is a Novel Protein of the Endoplasmic Reticulum |
title | Transmembrane and Coiled-Coil Domain Family 1 Is a Novel Protein of the Endoplasmic Reticulum |
title_full | Transmembrane and Coiled-Coil Domain Family 1 Is a Novel Protein of the Endoplasmic Reticulum |
title_fullStr | Transmembrane and Coiled-Coil Domain Family 1 Is a Novel Protein of the Endoplasmic Reticulum |
title_full_unstemmed | Transmembrane and Coiled-Coil Domain Family 1 Is a Novel Protein of the Endoplasmic Reticulum |
title_short | Transmembrane and Coiled-Coil Domain Family 1 Is a Novel Protein of the Endoplasmic Reticulum |
title_sort | transmembrane and coiled-coil domain family 1 is a novel protein of the endoplasmic reticulum |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3891740/ https://www.ncbi.nlm.nih.gov/pubmed/24454821 http://dx.doi.org/10.1371/journal.pone.0085206 |
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