The Golgi Apparatus: Roles for Distinct “Cis” and “Trans” Compartments

Rothman, James E.

doi:10.1002/9780470720745.ch7

Cited by 6 publications

(1 citation statement)

References 45 publications

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“…This could reflect in the 351 greater disorganization of the trans-Golgi in non-adherent cells. While such a differential 352 role and regulation of trans vs cis/cis-medial is speculated (Rothman, 1982 the Golgi is fragmented to drive this change (Migita and Inoue, 2012;Petrosyan, 2015). 376…”

Section: Studies In Neuronal Cells Have Shown a Calcium-dependent Intmentioning

confidence: 99%

Cell-matrix adhesion controls Golgi organization and function by regulating Arf1 activation in anchorage dependent cells

Singh¹,

Erady²,

Balasubramanian³

2018

Preprint

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Cell-matrix adhesion regulates membrane trafficking to control anchorage-dependent signaling. While a dynamic Golgi complex can contribute to this pathway, its control by adhesion remains untested. We find the loss of adhesion rapidly disorganizes the Golgi in mouse and human fibroblast cells, its integrity restored rapidly on re-adhesion to fibronectin (but not poly-l-lysine coated beads) along the microtubule network. Adhesion regulates the trans-Golgi more prominently than the cis /cis-medial Golgi, though they show no fallback into the ER making this reorganization distinct from known Golgi fragmentation. This is controlled by an adhesion-dependent drop and recovery of Arf1 activation, mediated through the Arf1 GEF BIG1/2 over GBF1. Constitutively active Arf1 disrupts this regulation and prevents Golgi disorganization in non-adherent cells. Adhesion regulates active Arf1 binding to the microtubule minus-end motor protein dynein to control Golgi reorganization, which ciliobrevin blocks. This regulation by adhesion controls Golgi function, promoting cell surface glycosylation on the loss of adhesion that constitutively active Arf1 blocks. This study hence identifies cell-matrix adhesion to be a novel regulator of Arf1 activation, controlling Golgi organization and function in anchorage-dependent cells.Summary StatementThis study identifies a role for cell-matrix adhesion in regulating organelle (Golgi) architecture and function which could have implications for multiple cellular pathways and function.

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Section: Studies In Neuronal Cells Have Shown a Calcium-dependent Intmentioning

confidence: 99%

Cell-matrix adhesion controls Golgi organization and function by regulating Arf1 activation in anchorage dependent cells

Singh¹,

Erady²,

Balasubramanian³

2018

Preprint

View full text Add to dashboard Cite

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Mapping the β-Cell in 3D at the Nanoscale Using Novel Cellular Electron Tomography and Computational Approaches

Noske

Marsh

2011

BetaSys

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Gibberellic acid controls specific acid-phosphatase isozymes in aleurone cells and protoplasts of Avena fatua L.

Hooley

1984

Planta

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In the presence of gibberellic acid (GA3) aleurone layers and isolated aleurone protoplasts of Avena fatua accumulate specific isozymes of acid phosphatase (EC 3.1.3.2). Some of these may be involved in mobilizing aleurone-grain phosphate reserves during germination. The hormone also controls secretion of other specific molecular forms of the enzyme that probably assist in endosperm hydrolysis. The accumulation and secretion of putative cell-wall-associated isozymes are stimulated by the action of GA3 in isolated protoplasts. This effect however, is apparently over-ridden in the intact tissue, possibly by a cell-wall-based feedback mechanism.

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The Golgi Apparatus: Roles for Distinct “Cis” and “Trans” Compartments

Cited by 6 publications

References 45 publications

Cell-matrix adhesion controls Golgi organization and function by regulating Arf1 activation in anchorage dependent cells

Cell-matrix adhesion controls Golgi organization and function by regulating Arf1 activation in anchorage dependent cells

Mapping the β-Cell in 3D at the Nanoscale Using Novel Cellular Electron Tomography and Computational Approaches

Gibberellic acid controls specific acid-phosphatase isozymes in aleurone cells and protoplasts of Avena fatua L.

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