The Ras Superfamily of Small GTPases: The Unlocked Secrets

Gallelli, Luca; Trapani, Eliana; Trabalzini, Lorenza; Retta, Saverio Francesco

doi:10.1007/978-1-62703-791-4_1

Cited by 158 publications

(150 citation statements)

References 89 publications

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“…This superfamily comprises five main families, each of them characterized by a different function despite a conserved structure and similar biochemical properties (Goitre et al, 2014). Among them, the Rho family members are key regulators of the actin cytoskeleton and cell migration, whereas the Arf and Rab families are important regulators of the intracellular transport (Stenmark, 2009;Donaldson and Jackson, 2011;Hall, 2012).…”

Section: Discussionmentioning

confidence: 99%

A novel interaction between Rab7b and actomyosin reveals a dual role in intracellular transport and cell migration

Borg

Bakke

Progida

2014

Journal of Cell Science

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Rab proteins are small GTPases that regulate transport between the different compartments of the endomembrane system in eukaryotic cells. Here, we show that Rab7b, a Rab that controls the transport between late endosomes and the trans Golgi network, interacts directly with myosin II. We illustrate the functional relevance of this interaction, demonstrating that myosin II mediates the transport of Rab7b endosomes, as Rab7b dynamics are strongly affected after myosin II depletion or inhibition. We also demonstrate that a member of the Rab family regulates actin remodeling and, consequently, influences cell adhesion, polarization and migration. We find the molecular mechanism by which Rab7b influences stress fiber formationthrough controlling the activation status of the small GTPase RhoA and therefore influencing myosin light chain phosphorylation. Our findings reveal a newly identified role for Rab proteins outside of their canonical role in intracellular trafficking, identifying Rab7b as a coordinator of cytoskeletal organization.

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Section: Discussionmentioning

confidence: 99%

A novel interaction between Rab7b and actomyosin reveals a dual role in intracellular transport and cell migration

Borg

Bakke

Progida

2014

Journal of Cell Science

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“…5,[17][18][19] These include cell growth, motility, trafficking and other functions. 5,17,18 The Ras superfamily has 154 members grouped into 5 families: Ras, Arf, Rab, Rho and Ran (Fig. 1).…”

Section: Lipid Modification Of Ras Superfamily Proteinsmentioning

confidence: 99%

Membrane orientation dynamics of lipid-modified small GTPases

Prakash

Gorfe

2016

Small GTPases

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Lipid-modified GTPases in the Ras superfamily that mediate a variety of cell signaling processes were thought to be passively anchored to membranes. However, an increasing number of recent studies are finding that membrane binding of these proteins is hardly a passive process, and it involves the soluble catalytic domain as well as the lipid anchor. The catalytic domain adopts multiple orientations on the membrane surface due to internal fluctuations that are modulated by activation status and mutations. Distinct orientation preferences among small GTPases likely lead to differential signaling outcomes, as downstream effectors can sense different orientations. We review recent studies behind this important conclusion.

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“…mall GTPases are a large family of hydrolase enzymes that bind and hydrolyze GTP to GDP (1). Small GTPases possess a common, structurally preserved GTP-binding domain and form an independent superfamily containing proteins that control a vast number of important processes, including growth, cellular differentiation, cell movement, and lipid vesicle transport (2).…”

mentioning

confidence: 99%

Interaction of the Small GTPase Cdc42 with Arginine Kinase Restricts White Spot Syndrome Virus in Shrimp

Jiang

Wei

et al. 2017

J Virol

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Many types of small GTPases are widely expressed in eukaryotes and have different functions. As a crucial member of the Rho GTPase family, Cdc42 serves a number of functions, such as regulating cell growth, migration, and cell movement. Several RNA viruses employ Cdc42-hijacking tactics in their target cell entry processes. However, the function of Cdc42 in shrimp antiviral immunity is not clear. In this study, we identified a Cdc42 protein in the kuruma shrimp (Marsupenaeus japonicus) and named it MjCdc42. MjCdc42 was upregulated in shrimp challenged by white spot syndrome virus (WSSV). The knockdown of MjCdc42 and injection of Cdc42 inhibitors increased the proliferation of WSSV. Further experiments determined that MjCdc42 interacted with an arginine kinase (MjAK). By analyzing the binding activity and enzyme activity of MjAK and its mutant, ΔMjAK, we found that MjAK could enhance the replication of WSSV in shrimp. MjAK interacted with the envelope protein VP26 of WSSV. An inhibitor of AK activity, quercetin, could impair the function of MjAK in WSSV replication. Further study demonstrated that the binding of MjCdc42 and MjAK depends on Cys 271 of MjAK and suppresses the WSSV replication-promoting effect of MjAK. By interacting with the active site of MjAK and suppressing its enzyme activity, MjCdc42 inhibits WSSV replication in shrimp. Our results demonstrate a new function of Cdc42 in the cellular defense against viral infection in addition to the regulation of actin and phagocytosis, which has been reported in previous studies. IMPORTANCEThe interaction of Cdc42 with arginine kinase plays a crucial role in the host defense against WSSV infection. This study identifies a new mechanism of Cdc42 in innate immunity and enriches the knowledge of the antiviral innate immunity of invertebrates.

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The Ras Superfamily of Small GTPases: The Unlocked Secrets

Cited by 158 publications

References 89 publications

A novel interaction between Rab7b and actomyosin reveals a dual role in intracellular transport and cell migration

A novel interaction between Rab7b and actomyosin reveals a dual role in intracellular transport and cell migration

Membrane orientation dynamics of lipid-modified small GTPases

Interaction of the Small GTPase Cdc42 with Arginine Kinase Restricts White Spot Syndrome Virus in Shrimp

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