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Structural insights into the architecture and membrane interactions of the conserved COMMD proteins
The COMMD proteins are a conserved family of proteins with central roles in intracellular membrane trafficking and transcription. They form oligomeric complexes with each other and act as components of a larger assembly called the CCC complex, which is localized to endosomal compartments and mediate...
Autores principales: | , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6089597/ https://www.ncbi.nlm.nih.gov/pubmed/30067224 http://dx.doi.org/10.7554/eLife.35898 |
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author | Healy, Michael D Hospenthal, Manuela K Hall, Ryan J Chandra, Mintu Chilton, Molly Tillu, Vikas Chen, Kai-En Celligoi, Dion J McDonald, Fiona J Cullen, Peter J Lott, J Shaun Collins, Brett M Ghai, Rajesh |
author_facet | Healy, Michael D Hospenthal, Manuela K Hall, Ryan J Chandra, Mintu Chilton, Molly Tillu, Vikas Chen, Kai-En Celligoi, Dion J McDonald, Fiona J Cullen, Peter J Lott, J Shaun Collins, Brett M Ghai, Rajesh |
author_sort | Healy, Michael D |
collection | PubMed |
description | The COMMD proteins are a conserved family of proteins with central roles in intracellular membrane trafficking and transcription. They form oligomeric complexes with each other and act as components of a larger assembly called the CCC complex, which is localized to endosomal compartments and mediates the transport of several transmembrane cargos. How these complexes are formed however is completely unknown. Here, we have systematically characterised the interactions between human COMMD proteins, and determined structures of COMMD proteins using X-ray crystallography and X-ray scattering to provide insights into the underlying mechanisms of homo- and heteromeric assembly. All COMMD proteins possess an α-helical N-terminal domain, and a highly conserved C-terminal domain that forms a tightly interlocked dimeric structure responsible for COMMD-COMMD interactions. The COMM domains also bind directly to components of CCC and mediate non-specific membrane association. Overall these studies show that COMMD proteins function as obligatory dimers with conserved domain architectures. |
format | Online Article Text |
id | pubmed-6089597 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | eLife Sciences Publications, Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-60895972018-08-15 Structural insights into the architecture and membrane interactions of the conserved COMMD proteins Healy, Michael D Hospenthal, Manuela K Hall, Ryan J Chandra, Mintu Chilton, Molly Tillu, Vikas Chen, Kai-En Celligoi, Dion J McDonald, Fiona J Cullen, Peter J Lott, J Shaun Collins, Brett M Ghai, Rajesh eLife Cell Biology The COMMD proteins are a conserved family of proteins with central roles in intracellular membrane trafficking and transcription. They form oligomeric complexes with each other and act as components of a larger assembly called the CCC complex, which is localized to endosomal compartments and mediates the transport of several transmembrane cargos. How these complexes are formed however is completely unknown. Here, we have systematically characterised the interactions between human COMMD proteins, and determined structures of COMMD proteins using X-ray crystallography and X-ray scattering to provide insights into the underlying mechanisms of homo- and heteromeric assembly. All COMMD proteins possess an α-helical N-terminal domain, and a highly conserved C-terminal domain that forms a tightly interlocked dimeric structure responsible for COMMD-COMMD interactions. The COMM domains also bind directly to components of CCC and mediate non-specific membrane association. Overall these studies show that COMMD proteins function as obligatory dimers with conserved domain architectures. eLife Sciences Publications, Ltd 2018-08-01 /pmc/articles/PMC6089597/ /pubmed/30067224 http://dx.doi.org/10.7554/eLife.35898 Text en © 2018, Healy et al http://creativecommons.org/licenses/by/4.0/ http://creativecommons.org/licenses/by/4.0/This article is distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use and redistribution provided that the original author and source are credited. |
spellingShingle | Cell Biology Healy, Michael D Hospenthal, Manuela K Hall, Ryan J Chandra, Mintu Chilton, Molly Tillu, Vikas Chen, Kai-En Celligoi, Dion J McDonald, Fiona J Cullen, Peter J Lott, J Shaun Collins, Brett M Ghai, Rajesh Structural insights into the architecture and membrane interactions of the conserved COMMD proteins |
title | Structural insights into the architecture and membrane interactions of the conserved COMMD proteins |
title_full | Structural insights into the architecture and membrane interactions of the conserved COMMD proteins |
title_fullStr | Structural insights into the architecture and membrane interactions of the conserved COMMD proteins |
title_full_unstemmed | Structural insights into the architecture and membrane interactions of the conserved COMMD proteins |
title_short | Structural insights into the architecture and membrane interactions of the conserved COMMD proteins |
title_sort | structural insights into the architecture and membrane interactions of the conserved commd proteins |
topic | Cell Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6089597/ https://www.ncbi.nlm.nih.gov/pubmed/30067224 http://dx.doi.org/10.7554/eLife.35898 |
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