Cell-matrix adhesion controls Golgi organization and function by regulating Arf1 activation in anchorage-dependent cells.
Posted on: 19 February 2018
Preprint posted on 9 February 2018
Article now published in Journal of Cell Science at http://dx.doi.org/10.1242/jcs.215855
From the outside in (and back out again) - a new form of communication between the extracellular matrix and the intracellular secretory pathway is discovered.
Selected by Nicola Stevenson
Categories: cell biology
Key findings
In this study the authors nicely demonstrate that detachment of adherent cells from the matrix results in the dispersal of Golgi elements. This is then reversed upon interaction with fibronectin coated surfaces indicating cell surface-matrix interactions can regulate Golgi structure. The mechanism for this centres around activation of the small GTPase Arf1; upon detachment, levels of active Arf1 drop, reducing the amount of dynein that is recruited to Golgi membranes. Active Arf1 then rapidly recovers as cells encounter fibronectin and reorganises Golgi membranes in a dynein- and microtubule-dependent manner. Although the role of integrins in initiating this signalling is not directly demonstrated, it is strongly implicated from past studies and fits the model. Lectin labelling of the cell surface also shows that glycosylation is upregulated in detached cells which contain a dispersed Golgi apparatus. This is a new model for secretory pathway regulation by the extracellular environment.
Importance
The important implication of this study is that matrix-integrin interactions can alter the cell surface glycome by activating signalling pathways at the Golgi. Detached cells will therefore interact with the environment differently compared to attached cells. As the authors highlight, this is likely to be a highly important consideration when thinking about tumour growth and metastasis.
Future directions
I chose this paper as it piqued my interest about what this could mean for our understanding of matrix biology. Although outside the scope of the current study, the data presented imply there is potential for feedback between intregrin-matrix interactions and matrix secretion. The authors acknowledge that the system may be sensitive enough to respond to changes in matrix binding that fall short of cell detachment; it would therefore be exciting to see whether matrix quality or composition can be sensed and modulated through this integrin-Golgi signalling pathway.
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