<scp>RhoD</scp> Binds the Rab5 Effector Rabankyrin‐5 and has a Role in Trafficking of the Platelet‐derived Growth Factor Receptor

Nehru, Vishal; Voytyuk, Oleksandr; Lennartsson, Johan; Aspenström, Pontus

doi:10.1111/tra.12121

Cited by 28 publications

(27 citation statements)

References 36 publications

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“…This is in line with findings of Sandilands and colleagues, showing that the membrane targeting and spatial activation of Src kinase family members are influenced by palmitoylation, which determines their localization to RhoB and RhoD-positive endosomes, respectively [120]. However, as RhoD has also been shown to localize to Rab5-positive early endosomes [121] where it binds the Rab5 effector Rabankyrin-5 and regulates together with Rab5 receptor tyrosine kinase (RTK) trafficking [122], it is tempting to speculate that RhoB and RhoD might also control the same subset of endosomes by affecting each other. This could be reminiscent of the crosstalk between RhoB and Rac1 [123] or RhoB and Cdc42 [124].…”

Section: Rho Gtpases Acting Along the Endocytic Pathwaysupporting

confidence: 89%

Spatiotemporal Control of Intracellular Membrane Trafficking by Rho GTPases

Noll

Haußer

2019

Cells

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As membrane-associated master regulators of cytoskeletal remodeling, Rho GTPases coordinate a wide range of biological processes such as cell adhesion, motility, and polarity. In the last years, Rho GTPases have also been recognized to control intracellular membrane sorting and trafficking steps directly; however, how Rho GTPase signaling is regulated at endomembranes is still poorly understood. In this review, we will specifically address the local Rho GTPase pools coordinating intracellular membrane trafficking with a focus on the endo-and exocytic pathways. We will further highlight the spatiotemporal molecular regulation of Rho signaling at endomembrane sites through Rho regulatory proteins, the GEFs and GAPs. Finally, we will discuss the contribution of dysregulated Rho signaling emanating from endomembranes to the development and progression of cancer.an inactive GDP-bound and an active GTP-bound state. Rho GDP/GTP cycling is tightly regulated by guanine nucleotide exchange factors (GEFs) that promote the formation of the active GTP-bound form through exchanging GDP for GTP. On the contrary, GTPase-activating proteins (GAPs) catalyze the intrinsic GTPase activity and promote the formation of inactive GDP-bound Rho. This inactive state can be subsequently recognized by guanine nucleotide dissociation inhibitors (GDIs), which sequester Rho GTPases in the cytosol [5,6] (Figure 1). Whereas classical Rho GTPases are regulated by GDP/GTP cycling, atypical Rho GTPases are regulated by other mechanisms that occur in particular at the transcriptional and post-translational level [7]. In the case of atypical Rho GTPases, GTP is usually constitutively bound, either because these Rho GTPases possess high intrinsic nucleotide exchange activity or have substitutions in their GTPase domain that prevent GTP hydrolysis.

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Section: Rho Gtpases Acting Along the Endocytic Pathwaysupporting

confidence: 89%

Spatiotemporal Control of Intracellular Membrane Trafficking by Rho GTPases

Noll

Haußer

2019

Cells

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“…RhoD and Rabankyrin-5 co-localise to Rab5-positive endosomes, which suggests a role for Rabankyrin-5 in the coordination of RhoD and Rab5 in endosomal trafficking (Nehru et al, 2013b). There is a mutual dependency of RhoD and Rabanbkirin-5 in endosome trafficking, as the knock-down of either RhoD or Rabankyrin-5 results in the mislocalisation of the other.…”

Section: Rhod In the Control Of Endosome Motility And Receptor Internmentioning

confidence: 96%

“…The biological context in which RhoD and Rabankyrin-5 collaborate appears to relate to trafficking of receptor tyrosine kinases. Of note, knock-down of RhoD can interfere with the internalisation of the PDGF-β receptor and the subsequent activation of its downstream signalling cascades (Schnatwinkel et al, 2004;Nehru et al, 2013b). This suggests that RhoD and Rabankyrin-5 are likely to have important roles in the coordination of RhoD and Rab activities; for instance, during internalisation and trafficking of transmembrane receptors.…”

Section: Rhod In the Control Of Endosome Motility And Receptor Internmentioning

confidence: 99%

Atypical Rho GTPases RhoD and Rif integrate cytoskeletal dynamics and membrane trafficking

Aspenström¹

2014

Biological Chemistry

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The Rho GTPases are essential regulators of basic cellular processes, including cell migration, cell contraction and cell division. Most studies still involve just the three canonical members, RhoA, Rac1 and Cdc42, although the Rho GTPases comprise at least 20 members. The aim of this review is to highlight some of the recent advances in our knowledge regarding the less-studied Rho members, with the focus on RhoD and Rif. The phenotypic alterations to cell behaviour that are triggered by RhoD and Rif suggest that they have unique impacts on cytoskeletal dynamics that distinguish them from the well-studied members of the Rho GTPases. In addition, RhoD has a role in the regulation of intracellular transport of vesicles. Taken together, the available data indicate that RhoD and Rif have functions as master regulators in the integration of cytoskeletal reorganisation and membrane trafficking.

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“…Although RhoD was recruited to S. Typhimurium invasion sites in a SopB-dependent manner, it did not contribute to any of the tested phenotypes. RhoD has been shown to participate in actin cytoskeleton reorganisation (Blom, Reis, Heldin, Kreuger, & Aspenstrom, 2017;Durkin et al, 2017;Gad, Nehru, Ruusala, & Aspenstrom, 2012;Koizumi et al, 2012;Nehru, Almeida, & Aspenstrom, 2013) and membrane trafficking events (Blom et al, 2015;Nehru, Voytyuk, Lennartsson, & Aspenstrom, 2013). Future studies are needed to elucidate its role in S. Typhimurium infection.…”

Section: R-ras1mentioning

confidence: 99%

Salmonellaexploits host Rho GTPase signalling pathways through the phosphatase activity of SopB

Truong

Boddy

Canadien

et al. 2018

Cellular Microbiology

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Salmonella uses Type 3 secretion systems (T3SSs) to deliver virulence factors, called effectors, into host cells during infection. The T3SS effectors promote invasion into host cells and the generation of a replicative niche. SopB is a T3SS effector that plays an important role in Salmonella pathogenesis through its lipid phosphatase activity. Here, we show that SopB mediates the recruitment of Rho GTPases (RhoB, RhoD, RhoH, and RhoJ) to bacterial invasion sites. RhoJ contributes to Salmonella invasion, and RhoB and RhoH play an important role in Akt activation. R-Ras1 also contributes to SopB-dependent Akt activation by promoting the localised production of PI(3,4)P /PI(3,4,5)P . Our studies reveal new signalling factors involved in SopB-dependent Salmonella infection.

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RhoD Binds the Rab5 Effector Rabankyrin‐5 and has a Role in Trafficking of the Platelet‐derived Growth Factor Receptor

Cited by 28 publications

References 36 publications

Spatiotemporal Control of Intracellular Membrane Trafficking by Rho GTPases

Spatiotemporal Control of Intracellular Membrane Trafficking by Rho GTPases

Atypical Rho GTPases RhoD and Rif integrate cytoskeletal dynamics and membrane trafficking

Salmonellaexploits host Rho GTPase signalling pathways through the phosphatase activity of SopB

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