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Atypical Rho GTPases the RhoBTB family: role as adaptors of ubiquitin ligase complexes

AuthorsBerthold, Jessica; Schenkova, Kristína; Ramos, Sonia ; Aspenstrom, Pontus; Xiong, Yue; Rivero, Francisco
Issue Date2008
Citation87th Annual Meeting Cologne. Deutsche Physiologische Gesselschaft (2008)
AbstractRhoBTB proteins, a subfamily of atypical Rho GTPases, seem to have distinct function from that of the classical RhoGTPases. They consist of a .GTPase domain, a proline-rich region and two BTB domains. Using Y2H and Co-IP studies we found that RhoBTB2 and 3 interact with Cul3 through both BTB domains. RhoBTB3 might also be degraded in the proteasome. GTPbinding assay revealed that the GTPase domain of RhoBTB3 does not bind GTP. In our working model RhoBTB proteins play a role in targeting of substrates for ubiquitinylation and degradation via Cul3-dependent ubiquitin ligase complexes. Y2H screening identified nuclear protein MUFI as a potential interaction partner of RhoBTB3. MUFI interacts with RhoBTB3 in vivo and seems to be recruited by RhoBTB3 from the nucleus to the cytoplasm. MUFl serves as a linker protein in Cul5-based ubiquitin ligases. Our aim is to answer the question, whether MUF 1 is in volved in a multiprotein complex that involves Cul3 and Cul5. and e!ucidate the role of RhoBTB in the regulation of this complex.
Appears in Collections:(IF) Comunicaciones congresos
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