RhoU forms homo-oligomers to regulate cellular responses

Natasha S. Clayton, Richard G. Hodge, Elvira Infante, Dominic Alibhai, Felix Zhou, Anne J. Ridley*

*Corresponding author for this work

Research output: Contribution to journalArticle (Academic Journal)peer-review


RhoU is an atypical member of the Rho family of small G-proteins, which has N- and C-terminal extensions compared to the classic Rho GTPases RhoA, Rac1 and Cdc42, and associates with membranes through C-terminal palmitoylation rather than prenylation. RhoU mRNA expression is upregulated in prostate cancer and is considered a marker for disease progression. Here, we show that RhoU overexpression in prostate cancer cells increases cell migration and invasion. To identify RhoU targets that contribute to its function, we found that RhoU homodimerizes in cells. We map the region involved in this interaction to the C-terminal extension and show that C-terminal palmitoylation is required for self-association. Expression of the isolated C-terminal extension reduces RhoU-induced activation of p21-activated kinases (PAKs), which are known downstream targets for RhoU, and induces cell morphological changes consistent with inhibiting RhoU function. Our results show for the first time that the activity of a Rho family member is stimulated by self-association, and this is important for its activity.

Original languageEnglish
Article numberjcs261645
Number of pages10
JournalJournal of Cell Science
Issue number2
Publication statusPublished - 30 Jan 2024

Bibliographical note

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  • Cell morphology
  • p21-activated kinase
  • PAKs
  • Phosphorylation
  • Rho GTPases
  • RhoU


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