The early secretory pathway in extracellular matrix secretion
| Dates: | 6 March 2014 |
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| Times: | 13:00 - 14:00 |
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| What is it: | Seminar |
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| Organiser: | Faculty of Life Sciences |
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| Who is it for: | University staff |
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| Speaker: | David Stephens |
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This seminar is part of the Tissue Systems seminar series. Our work seeks to develop a mechanistic understanding of the organization and function of the secretory pathway. Our lab is especially interested in the relationship between endomembranes and the microtubule cytoskeleton. I will present our work that explores the relationship between intracellular organization, extracellular matrix secretion and assembly, and ciliogenesis. Our work examines how the organization of ER-to-Golgi transport and Golgi function relate to ECM assembly and to ciliogenesis. In recent years, we have studied how the early secretory pathway (ER-to-Golgi transport and Golgi organization) relates to the secretion of unusually large cargo molecules such as procollagens. ER exit sites (ERES) are highly organized in metazoans and we have defined some of the molecular detail of this organization (Traffic, 2006, Journal of Cell Science 2009 and 2010) and defined how COPII coat assembly at ERES is linked to efficient extracellular matrix secretion (Journal of Cell Science 2008). Experiments in zebrafish have enabled us to extend this work to a better understanding of the role of ERES in development (Journal of Cell Science 2012 and Biology Open 2013). We have recently characterized other proteins that control the structure of ERES and of the Golgi and are now studying how higher order organization of these structures links to ECM assembly. This work has recently extended in scope to include the relationship between ECM secretion and ciliogenesis. The Golgi matrix protein giantin is required for normal chondrogenesis in vivo. We found unexpectedly that giantin is required for ciliogenesis by controlling the localization and consequently function of a key component of the dynein-2 motor (Journal of Cell Science, 2013). Dynein-2 is known to be mutated in a series of skeletal ciliopathies providing a further functional link between secretory pathway function and matrix secretion.
Speaker
David Stephens
Organisation: University of Bristol
Travel and Contact Information
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Lecture Theatre
Michael Smith Building
Manchester
