Ral-Arf6 crosstalk regulates Ral dependent exocyst trafficking and anchorage independent growth signalling

Pawar, Archana; Meier, Jeremy A.; Dasgupta, Anwesha; Diwanji, Neha; Deshpande, Neha; Saxena, Kritika; Buwa, Natasha; Inchanalkar, Siddhi; Schwartz, Martin A.; Balasubramanian, Nagaraj

doi:10.1016/j.cellsig.2016.05.023

Cited by 19 publications

(24 citation statements)

References 64 publications

(129 reference statements)

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“…RalB seems to be more potent than RalA in the regulation of cell invasion and migration . Studies have shown that RalA plays an integral role in disrupting cellular adhesion via controlling Arf6 activation . Others have suggested RalA inhibits p53, which in turn helps promote invasion .…”

Section: Ral Signaling In Cancermentioning

confidence: 99%

Ral signaling pathway in health and cancer

et al. 2017

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The Ral (Ras‐Like) signaling pathway plays an important role in the biology of cells. A plethora of effects is regulated by this signaling pathway and its prooncogenic effectors. Our team has demonstrated the overactivation of the RalA signaling pathway in a number of human malignancies including cancers of the liver, ovary, lung, brain, and malignant peripheral nerve sheath tumors. Additionally, we have shown that the activation of RalA in cancer stem cells is higher in comparison with differentiated cancer cells. In this article, we review the role of Ral signaling in health and disease with a focus on the role of this multifunctional protein in the generation of therapies for cancer. An improved understanding of this pathway can lead to development of a novel class of anticancer therapies that functions on the basis of intervention with RalA or its downstream effectors.

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Section: Ral Signaling In Cancermentioning

confidence: 99%

Ral signaling pathway in health and cancer

et al. 2017

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“…Cell-matrix adhesion is a vital regulator of many cellular processes ( Berrier and Yamada, 2007 ; Caswell et al, 2009 ; Danen and Yamada, 2001 ) and disease conditions ( Desgrosellier and Cheresh, 2010 ; Wu and Reddy, 2012 ). A role for integrin-mediated adhesion in regulating membrane trafficking is seen to affect membrane order ( Gaus et al, 2006 ), receptor mobility and activation to drive anchorage-dependent signaling ( Balasubramanian et al, 2007b , 2010 ; Pawar et al, 2016 ). Loss of adhesion dramatically turns off this signaling, which then recovers upon re-adhesion to the matrix ( del Pozo et al, 2004 ).…”

Section: Introductionmentioning

confidence: 99%

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

Singh

Erady

Balasubramanian

2018

Journal of Cell Science

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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.

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“…Rab11 binds FIP3 and FIP4, which also interact with Arf6 and exocyst, and this multicomplex regulates cytokinesis . RalA regulates Arf6 activation and active Arf6 mediates Ral‐exocyst‐dependent delivery of raft microdomains to the PM . Rab11a and Rab27b are simultaneously involved in bacterial expulsion via binding to exocyst subunits …”

Section: How Is the Exocyst Complex Assembled?mentioning

confidence: 99%

The Exocyst: Dynamic Machine or Static Tethering Complex?

Nishida-Fukuda

2019

BioEssays

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The exocyst is a conserved octameric complex that physically tethers a vesicle to the plasma membrane, prior to membrane fusion. It is important not only for secretion and membrane delivery but also, in mammalian cells, for cytokinesis, ciliogenesis, autophagy, tumorigenesis, and host defense. The combination of genome editing and advanced light microscopy of exocyst subunits in living cells has recently shown the complex to be much more dynamic than previously appreciated, and exposed how little we still know about its function and regulation.

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Ral-Arf6 crosstalk regulates Ral dependent exocyst trafficking and anchorage independent growth signalling

Cited by 19 publications

References 64 publications

Ral signaling pathway in health and cancer

Ral signaling pathway in health and cancer

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

The Exocyst: Dynamic Machine or Static Tethering Complex?

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