Regulation of post-Golgi LH3 trafficking is essential for collagen homeostasis
Lysine hydroxylation of procollagen precursors by LH3 is required for collagen fibril crosslinking and stabilization. Here the authors show that the trafficking protein VIPAR is required for correct sorting of LH3 into post-Golgi collagen carriers and for correct collagen modification and structure.
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| Format: | Article |
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Nature Publishing Group
2016-07-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/ncomms12111 |
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doaj-e77a5c9ad1f34f37a39287201a081ba72021-05-11T10:42:31ZengNature Publishing GroupNature Communications2041-17232016-07-017111410.1038/ncomms12111Regulation of post-Golgi LH3 trafficking is essential for collagen homeostasisBlerida Banushi0Federico Forneris1Anna Straatman-Iwanowska2Adam Strange3Anne-Marie Lyne4Clare Rogerson5Jemima J. Burden6Wendy E. Heywood7Joanna Hanley8Ivan Doykov9Kornelis R. Straatman10Holly Smith11Danai Bem12Janos Kriston-Vizi13Gema Ariceta14Maija Risteli15Chunguang Wang16Rosalyn E. Ardill17Marcin Zaniew18Julita Latka-Grot19Simon N. Waddington20S. J. Howe21Francesco Ferraro22Asllan Gjinovci23Scott Lawrence24Mark Marsh25Mark Girolami26Laurent Bozec27Kevin Mills28Paul Gissen29MRC Laboratory for Molecular Cell Biology, University College LondonDepartment of Biology and Biotechnology, The Armenise-Harvard Laboratory of Structural Biology, University of PaviaMRC Laboratory for Molecular Cell Biology, University College LondonEastman Dental Institute, University College LondonDepartment of Statistical Science, University College LondonMRC Laboratory for Molecular Cell Biology, University College LondonMRC Laboratory for Molecular Cell Biology, University College LondonInstitute of Child Health, University College LondonInstitute of Child Health, University College LondonInstitute of Child Health, University College LondonCentre for Core Biotechnology Services, University of LeicesterMRC Laboratory for Molecular Cell Biology, University College LondonCentre for Cardiovascular Sciences, School of Clinical and Experimental Medicine, College of Medical and Dental Sciences, University of BirminghamMRC Laboratory for Molecular Cell Biology, University College LondonDepartment of Pediatric Nephrology, University Hospital Vall d'Hebron, Universitat Autonoma BarcelonaFaculty of Biochemistry and Molecular Medicine, University of OuluMedical Research Center Oulu, Oulu University Hospital, University of OuluRoyal Hospital for Sick ChildrenChildren's HospitalChildren's Memorial Health InstituteInstitute for Women’s Health, University College LondonInstitute for Women’s Health, University College LondonMRC Laboratory for Molecular Cell Biology, University College LondonMRC Laboratory for Molecular Cell Biology, University College LondonMRC Laboratory for Molecular Cell Biology, University College LondonMRC Laboratory for Molecular Cell Biology, University College LondonDepartment of Statistics, University of WarwickEastman Dental Institute, University College LondonInstitute of Child Health, University College LondonMRC Laboratory for Molecular Cell Biology, University College LondonLysine hydroxylation of procollagen precursors by LH3 is required for collagen fibril crosslinking and stabilization. Here the authors show that the trafficking protein VIPAR is required for correct sorting of LH3 into post-Golgi collagen carriers and for correct collagen modification and structure.https://doi.org/10.1038/ncomms12111 |
| collection |
DOAJ |
| language |
English |
| format |
Article |
| sources |
DOAJ |
| author |
Blerida Banushi Federico Forneris Anna Straatman-Iwanowska Adam Strange Anne-Marie Lyne Clare Rogerson Jemima J. Burden Wendy E. Heywood Joanna Hanley Ivan Doykov Kornelis R. Straatman Holly Smith Danai Bem Janos Kriston-Vizi Gema Ariceta Maija Risteli Chunguang Wang Rosalyn E. Ardill Marcin Zaniew Julita Latka-Grot Simon N. Waddington S. J. Howe Francesco Ferraro Asllan Gjinovci Scott Lawrence Mark Marsh Mark Girolami Laurent Bozec Kevin Mills Paul Gissen |
| spellingShingle |
Blerida Banushi Federico Forneris Anna Straatman-Iwanowska Adam Strange Anne-Marie Lyne Clare Rogerson Jemima J. Burden Wendy E. Heywood Joanna Hanley Ivan Doykov Kornelis R. Straatman Holly Smith Danai Bem Janos Kriston-Vizi Gema Ariceta Maija Risteli Chunguang Wang Rosalyn E. Ardill Marcin Zaniew Julita Latka-Grot Simon N. Waddington S. J. Howe Francesco Ferraro Asllan Gjinovci Scott Lawrence Mark Marsh Mark Girolami Laurent Bozec Kevin Mills Paul Gissen Regulation of post-Golgi LH3 trafficking is essential for collagen homeostasis Nature Communications |
| author_facet |
Blerida Banushi Federico Forneris Anna Straatman-Iwanowska Adam Strange Anne-Marie Lyne Clare Rogerson Jemima J. Burden Wendy E. Heywood Joanna Hanley Ivan Doykov Kornelis R. Straatman Holly Smith Danai Bem Janos Kriston-Vizi Gema Ariceta Maija Risteli Chunguang Wang Rosalyn E. Ardill Marcin Zaniew Julita Latka-Grot Simon N. Waddington S. J. Howe Francesco Ferraro Asllan Gjinovci Scott Lawrence Mark Marsh Mark Girolami Laurent Bozec Kevin Mills Paul Gissen |
| author_sort |
Blerida Banushi |
| title |
Regulation of post-Golgi LH3 trafficking is essential for collagen homeostasis |
| title_short |
Regulation of post-Golgi LH3 trafficking is essential for collagen homeostasis |
| title_full |
Regulation of post-Golgi LH3 trafficking is essential for collagen homeostasis |
| title_fullStr |
Regulation of post-Golgi LH3 trafficking is essential for collagen homeostasis |
| title_full_unstemmed |
Regulation of post-Golgi LH3 trafficking is essential for collagen homeostasis |
| title_sort |
regulation of post-golgi lh3 trafficking is essential for collagen homeostasis |
| publisher |
Nature Publishing Group |
| series |
Nature Communications |
| issn |
2041-1723 |
| publishDate |
2016-07-01 |
| description |
Lysine hydroxylation of procollagen precursors by LH3 is required for collagen fibril crosslinking and stabilization. Here the authors show that the trafficking protein VIPAR is required for correct sorting of LH3 into post-Golgi collagen carriers and for correct collagen modification and structure. |
| url |
https://doi.org/10.1038/ncomms12111 |
| work_keys_str_mv |
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