Abstract
The biomechanical and biochemical properties of connective tissues are determined by the composition and quality of their extracellular matrix. This, in turn, is highly dependent on the function and organisation of the secretory pathway. The Golgi complex plays a vital role in directing matrix output by co-ordinating the post-translational modification and proteolytic processing of matrix components prior to their secretion. These modifications have broad impacts on the secretion and subsequent assembly of matrix components, as well as their function in the extracellular environment. In this Review, we highlight the role of the Golgi in the formation of an adaptable, healthy matrix, with a focus on proteoglycan and procollagen secretion as example cargoes. We then discuss the impact of Golgi dysfunction on connective tissue in the context of human disease and ageing.
| Original language | English |
|---|---|
| Article number | jcs258879 |
| Number of pages | 20 |
| Journal | Journal of Cell Science |
| Volume | 135 |
| Issue number | 1 |
| Early online date | 13 Jan 2022 |
| DOIs | |
| Publication status | E-pub ahead of print - 13 Jan 2022 |
Bibliographical note
Funding Information:We are grateful to Professor Karl Kadler and Dr Yinhui Lu, Wellcome Centre for Cell-Matrix Research, University of Manchester, for providing the electron microscopy images of mouse tendon fibroblasts used in Fig. 1 and Movies 1 and 2. Fig. 2 was created with BioRender.com. We would like to acknowledge the Biotechnology and Biological Sciences Research Council (BBSRC; BB/T001984/1, awarded to D.S., M.L. and N.S.) and the University of Manchester and Singapore A*Star Institute (JH) for funding. Open access funding provided by University of Bristol. Deposited in PMC for immediate release.
Publisher Copyright:
© 2022. Published by The Company of Biologists Ltd
Keywords
- Golgi complex
- Collagen
- Extracellular matrix
- Glycosylation
- Proteoglycans
- Secretory pathway
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