GRASP and IPCEF Promote ARF-to-Rac Signaling and Cell Migration by Coordinating the Association of ARNO/cytohesin 2 with Dock180

White, David T.; McShea, Katie M.; Attar, Myriam A.; Santy, Lorraine C.

doi:10.1091/mbc.e09-03-0217

Cited by 45 publications

(64 citation statements)

References 55 publications

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“…Interestingly, Arf6 is positioned upstream of Rac activation in various biological processes. One model advocates that Arf6 activation will recruit the DOCK180-ELMO complex to the leading edge of a cell to promote lamellipodia formation (8,29,31). An interesting question that arises is whether there is a direct interaction between Arf6 and ELMO that guides its membrane localization.…”

Section: Discussionmentioning

confidence: 99%

The Arf Family GTPase Arl4A Complexes with ELMO Proteins to Promote Actin Cytoskeleton Remodeling and Reveals a Versatile Ras-binding Domain in the ELMO Proteins Family

Patel

Chiang

Tran

et al. 2011

Journal of Biological Chemistry

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Background: ELMO complexes with DOCK180 and contributes to Rac signaling. Results: Arl4A binds ELMO and is a membrane localization signal that triggers DOCK180-Rac-dependent actin cytoskeleton remodeling. Conclusion: ELMO, via its versatile Ras-binding domain, binds its effector Arl4A, and this novel interaction facilitates Rac signaling. Significance: This is the first demonstration of a Ras-binding domain that binds Arf or Rho family GTPases.

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Section: Discussionmentioning

confidence: 99%

The Arf Family GTPase Arl4A Complexes with ELMO Proteins to Promote Actin Cytoskeleton Remodeling and Reveals a Versatile Ras-binding Domain in the ELMO Proteins Family

Patel

Chiang

Tran

et al. 2011

Journal of Biological Chemistry

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“…These results suggest that modulation of ARF6 by the two GEFS ARNO and EFA6 is probably responsible for the developmental change from bidirectional to retrograde flow of integrin. Transfection with ACAP1 and ARNO-E156K will reverse the activation of ARF6, but will also have other effects due to the coat protein actions of ACAP1 and the interactions of ARNO with trafficking-related scaffolding proteins and paxillin (Mo et al, 2012, White et al, 2010.…”

Section: Does the Activation State Of Arf6 Controlled By Gaps And Gementioning

confidence: 99%

Exclusion of Integrins from CNS Axons Is Regulated by Arf6 Activation and the AIS

et al. 2015

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Integrins are adhesion and survival molecules involved in axon growth during CNS development, as well as axon regeneration after injury in the peripheral nervous system (PNS). Adult CNS axons do not regenerate after injury, partly due to a low intrinsic growth capacity. We have previously studied the role of integrins in axon growth in PNS axons; in the present study, we investigate whether integrin mechanisms involved in PNS regeneration may be altered or lacking from mature CNS axons by studying maturing CNS neurons in vitro. In rat cortical neurons, we find that integrins are present in axons during initial growth but later become restricted to the somato-dendritic domain. We investigated how this occurs and whether it can be altered to enhance axonal growth potential. We find a developmental change in integrin trafficking; transport becomes predominantly retrograde throughout axons, but not dendrites, as neurons mature. The directionality of transport is controlled through the activation state of ARF6, with developmental upregulation of the ARF6 GEF ARNO enhancing retrograde transport. Lowering ARF6 activity in mature neurons restores anterograde integrin flow, allows transport into axons, and increases axon growth. In addition, we found that the axon initial segment is partly responsible for exclusion of integrins and removal of this structure allows integrins into axons. Changing posttranslational modifications of tubulin with taxol also allows integrins into the proximal axon. The experiments suggest that the developmental loss of regenerative ability in CNS axons is due to exclusion of growth-related molecules due to changes in trafficking.

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“…Arf GEFs (notably cytohesins and EFA6) and Arf GAPs also interact with Rho-family G proteins and other actin cytoskeleton regulators (Myers and Casanova, 2008;Randazzo et al, 2007). Arf6 activates Rac by recruiting the Rac GEF complex DOCK180/Elmo to the plasma membrane, a process that is mediated in part through the binding of cytohesin to the DOCK180 interactor IPCEF (Santy et al, 2005;White et al, 2010). In addition, Arf1 cooperates with Rac for efficient recruitment of the WASP family verprolin-homologous protein (WAVE) regulatory complex to the plasma membrane (Koronakis et al, 2011).…”

Section: Arf Regulation Of the Actin Cytoskeletonmentioning

confidence: 99%

Arfs at a Glance

Jackson

Bouvet

2014

Journal of Cell Science

119

117

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The Arf small G proteins regulate protein and lipid trafficking in eukaryotic cells through a regulated cycle of GTP binding and hydrolysis. In their GTP-bound form, Arf proteins recruit a specific set of protein effectors to the membrane surface. These effectors function in vesicle formation and tethering, non-vesicular lipid transport and cytoskeletal regulation. Beyond fundamental membrane trafficking roles, Arf proteins also regulate mitosis, plasma membrane signaling, cilary trafficking and lipid droplet function. Tight spatial and temporal regulation of the relatively small number of Arf proteins is achieved by their guanine nucleotideexchange factors (GEFs) and GTPase-activating proteins (GAPs), which catalyze GTP binding and hydrolysis, respectively. A unifying function of Arf proteins, performed in conjunction with their regulators and effectors, is sensing, modulating and transporting the lipids that make up cellular membranes. In this Cell Science at a Glance article and the accompanying poster, we discuss the unique features of Arf small G proteins, their functions in vesicular and lipid trafficking in cells, and how these functions are modulated by their regulators, the GEFs and GAPs. We also discuss how these Arf functions are subverted by human pathogens and disease states.

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GRASP and IPCEF Promote ARF-to-Rac Signaling and Cell Migration by Coordinating the Association of ARNO/cytohesin 2 with Dock180

Cited by 45 publications

References 55 publications

The Arf Family GTPase Arl4A Complexes with ELMO Proteins to Promote Actin Cytoskeleton Remodeling and Reveals a Versatile Ras-binding Domain in the ELMO Proteins Family

The Arf Family GTPase Arl4A Complexes with ELMO Proteins to Promote Actin Cytoskeleton Remodeling and Reveals a Versatile Ras-binding Domain in the ELMO Proteins Family

Exclusion of Integrins from CNS Axons Is Regulated by Arf6 Activation and the AIS

Arfs at a Glance

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