{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nRhoG serves as a pivotal regulator of actin cytoskeletal dynamics to promote cell motility and invasive behavior in diverse physiological and pathological settings. In endothelial cells, RhoG is activated downstream of adhesion receptors to drive the formation of dynamic plasma‐membrane “cups” that facilitate leukocyte transendothelial migration, while in migrating cells it orchestrates lamellipodia formation via Rac activation through effectors such as ELMO and Dock180. In cancer cells, RhoG functions downstream of receptors like EphA2 to promote ligand‐independent migration and invasion, modulates invadopodia disassembly to fine‐tune extracellular matrix degradation, and contributes to the aggressive behavior observed in certain carcinomas. These studies collectively underscore its key role in the regulation of cell migration and metastasis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "7"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its roles in motility and invasion, RhoG is crucial for multiple aspects of cellular homeostasis and specialized membrane trafficking processes that impact immune and vascular functions. It regulates the activation of neutrophils during the respiratory burst, contributes to the efficient release of cytotoxic granules from lymphocytes (with deficiencies leading to hemophagocytic lymphohistiocytosis), and governs platelet activation essential for thrombus formation. RhoG also participates in caveolar trafficking and modulates focal adhesion turnover, thereby influencing cell–matrix adhesion and contractility; its ability to suppress anoikis via a phosphatidylinositol 3‐kinase–dependent mechanism further supports cell survival. Moreover, regulation by microRNA‐124 in retinal pigment epithelial cells highlights its role in controlling proliferation and migration in non‐immune contexts. These diverse functions emphasize RhoG’s importance in coordinating vesicular trafficking, adhesion dynamics, and cell survival."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "18"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAt the mechanistic level, RhoG signaling is finely regulated by several guanine nucleotide exchange factors (GEFs) and modulatory interactions, as well as by pathogen‐derived effectors. Biochemical analyses have demonstrated that RhoG can be activated by GEFs that also target Rac1 and Cdc42, and structural studies reveal a preferential exchange by the N‐terminal DH/PH module of Trio, establishing RhoG as a primary target. RhoG regulates downstream effectors such as Dock4, thereby promoting Rac1 activation, and its activity is subject to modulation by bacterial virulence factors—including Yersinia effectors that first stimulate and later inactivate RhoG—as well as by tyrosine phosphorylation events that dampen the catalytic activity of its specific exchange factor SGEF. In addition, microRNA‐124–mediated targeting of RhoG transcripts further illustrates a post‐transcriptional mechanism for controlling its activity in oncogenic contexts. Recent high‐resolution analyses of the DOCK/ELMO complex provide structural insight into RhoG‐induced allosteric activation that couples membrane recruitment with efficient Rac activation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "19", "end_ref": "27"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Hironori Katoh, Kiyo Hiramoto, Manabu Negishi "}, {"type": "b", "children": [{"type": "t", "text": "Activation of Rac1 by RhoG regulates cell migration."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Sci (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1242/jcs.02720"}], "href": "https://doi.org/10.1242/jcs.02720"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16339170"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16339170"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Jaap D van Buul, Michael J Allingham, Thomas Samson, et al. 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