Projects per year
Abstract
Collagen is the most abundant protein in the animal kingdom. It is of fundamental importance during development for cell differentiation and tissue morphogenesis as well as in pathological processes such as fibrosis and cancer cell migration. However, our understanding of the mechanisms of procollagen secretion remains limited. Here, we show that TFG organizes transitional ER (tER) and ER exit sites (ERESs) into larger structures. Depletion of TFG results in dispersion of tER elements that remain associated with individual ER-Golgi intermediate compartments (ERGICs) as largely functional ERESs. We show that TFG is not required for the transport and packaging of small soluble cargoes but is necessary for the export of procollagen from the ER. Our work therefore suggests a key relationship between the structure and function of ERESs and a central role for TFG in optimizing COPII assembly for procollagen export.
Original language | English |
---|---|
Article number | 15 |
Pages (from-to) | 1648-59 |
Number of pages | 12 |
Journal | Cell Reports |
Volume | 15 |
Issue number | 8 |
Early online date | 12 May 2016 |
DOIs | |
Publication status | Published - 24 May 2016 |
Structured keywords
- BrisSynBio
- Bristol BioDesign Institute
Keywords
- Synthetic biology
Fingerprint
Dive into the research topics of 'TFG Promotes Organization of Transitional ER and Efficient Collagen Secretion'. Together they form a unique fingerprint.Projects
- 4 Finished
-
Photo-oxidation and cryofluorescence for Correlative Light Electron Microscopy
1/12/13 → 1/12/16
Project: Research
-
-
The role of Sec16A in driving secretory cargo export from the endoplasmic reticulum.
9/07/12 → 9/07/15
Project: Research
Equipment
-
Wolfson Bioimaging Facility
Mark Jepson (Manager)
Faculty of Life SciencesFacility/equipment: Facility
Profiles
-
Professor David J Stephens
- Fundamental Bioscience
- School of Biochemistry - Professor of Cell Biology
- Dynamic Cell Biology
Person: Academic , Member