Abstract
The Rho GTPase family can be classified into classic and atypical members. Classic members cycle between an inactive Guanosine DiPhosphate -bound state and an active Guanosine TriPhosphate-bound state. Atypical Rho GTPases, such as RND1, are predominantly in an active GTP-bound conformation. The role of classic members in oncogenesis has been the subject of numerous studies, while that of atypical members has been less explored. Besides the roles of RND1 in healthy tissues, recent data suggest that RND1 is involved in oncogenesis and response to cancer therapeutics. Here, we present the current knowledge on RND1 expression, subcellular localization, and functions in healthy tissues. Then, we review data showing that RND1 expression is dysregulated in tumors, the molecular mechanisms involved in this deregulation, and the role of RND1 in oncogenesis. For several aggressive tumors, RND1 presents the features of a tumor suppressor gene. In these tumors, low expression of RND1 is associated with a bad prognosis for the patients. Finally, we highlight that RND1 expression is induced by anticancer agents and modulates their response. Of note, RND1 mRNA levels in tumors could be used as a predictive marker of both patient prognosis and response to anticancer agents.
Highlights
RND1, an Atypical Rho GTPaseThe Rho family of GTPases includes 20 members, which can be classified into classic and atypical members in humans [1,2] (Figure 1)
RND1 presents the features of a tumor suppressor gene
As described in the previous section, RND1 is down-regulated in hepatocellular carcinoma, in the most aggressive subtypes of breast cancers and in glioblastoma patients, whereas it is over-expressed in esophageal squamous cell carcinoma, which could explain the contradictive effects of its variation on cell behavior
Summary
The Rho family of GTPases includes 20 members, which can be classified into classic and atypical members in humans [1,2] (Figure 1). RND1 shares 41% identity with RHOA protein (Figure 1), RND proteins differ from other Rho GTPases by several features They contain an extension of 30 amino acids at the C-terminal and RND1 and RND3 proteins possess 8 and 18 additional amino acids, respectively, at the N-terminal [3]. At the bound to GTP, both classic and atypical Rho GTPases bind to their effectors and activate signaling. An The essential role in oncogenesis and independent response on to epigenetic, transcriptional, post-transcriptional, and post-translational mechanisms, than on therapeutics Insofar as these data have been recently well reviewed for RND3 [13], we will focus our exchange bound to GTP, both classic atypical Rho bind to their effectors discussion[6].onFinally, RND1.when. We will review currentand knowledge on GTPases the expression, localization, and activate signaling pathways that regulate various cellular processes, such as cytoskeleton dynamic, regulation, and functions of RND1 in healthy tissues.
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