Cell-matrix adhesion controls Golgi organization and function through Arf1 activation in anchorage-dependent cells
| Autor: | Vibha Singh, Nagaraj Balasubramanian, Chaitanya Erady |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Integrins Glycosylation Integrin Dynein Golgi Apparatus Biology Cell-Matrix Junctions Motor protein Mice 03 medical and health sciences symbols.namesake Cell-matrix adhesion Arf1 Microtubule Cell Adhesion Golgi Animals Humans Cells Cultured Cell Membrane Golgi organization Cell Biology Adhesion Golgi apparatus Embryo Mammalian Cell biology 030104 developmental biology biology.protein symbols ADP-Ribosylation Factor 1 Signal Transduction trans-Golgi Network Research Article |
| Zdroj: | Journal of Cell Science |
| ISSN: | 1477-9137 0021-9533 |
| Popis: | Cell-matrix adhesion regulates membrane trafficking controlling anchorage-dependent signaling. While a dynamic Golgi complex can contribute to this pathway, its regulation by adhesion remains unclear. Here we report that loss of adhesion dramatically disorganized the Golgi in mouse and human fibroblast cells. Golgi integrity is restored rapidly upon integrin-mediated re-adhesion to FN and is disrupted by integrin blocking antibody. In suspended cells, the cis, cis-medial and trans-Golgi networks differentially disorganize along the microtubule network but show no overlap with the ER, making this disorganization distinct from known Golgi fragmentation. This pathway is regulated by an adhesion-dependent reduction and recovery of Arf1 activation. Constitutively active Arf1 disrupts this regulation and prevents Golgi disorganization due to loss of adhesion. Adhesion-dependent Arf1 activation regulates its binding to the microtubule minus-end motor protein dynein to control Golgi reorganization, which is blocked by ciliobrevin. Adhesion-dependent Golgi organization controls its function, regulating cell surface glycosylation due to loss of adhesion, which is blocked by constitutively active Arf1. This study, hence, identified integrin-dependent cell-matrix adhesion to be a novel regulator of Arf1 activation, controlling Golgi organization and function in anchorage-dependent cells. This article has an associated First Person interview with the first author of the paper. Summary: Integrin-dependent cell-matrix adhesion activates Arf1, which then recruits dynein to regulate Golgi organization and function along the microtubule network. |
| Databáze: | OpenAIRE |
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