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Cullin 3/KCTD5 Promotes the Ubiqutination of Rho Guanine Nucleotide Dissociation Inhibitor 1 and Regulates Its Stability

Journal of Microbiology and Biotechnology 2020년 30권 10호 p.1488 ~ 1494
조희준, 류기준, 백경은, Lim Jee-Won, 김태영, 송채영, 유지윤, 이희구,
소속 상세정보
조희준 ( Cho Hee-Jun ) - Korea Research Institute of Bioscience and Biotechnology Immunotherapy Research Center
류기준 ( Ryu Ki-Jun ) - Gyeongsang National University Division of Applied Life Science
백경은 ( Baek Kyoung-Eun ) - Korea Research Institute of Bioscience and Biotechnology Immunotherapy Research Center
 ( Lim Jee-Won ) - Korea Research Institute of Bioscience and Biotechnology Immunotherapy Research Center
김태영 ( Kim Tae-Young ) - Gyeongsang National University Division of Applied Life Science
송채영 ( Song Chae-Yeong ) - Gyeongsang National University Division of Applied Life Science
유지윤 ( Yoo Ji-Yun ) - Gyeongsang National University Division of Applied Life Science
이희구 ( Lee Hee-Gu ) - Gyeongsang National University Division of Applied Life Science

Abstract


Rho guanine nucleotide dissociation inhibitor 1 (RhoGDI1) plays important roles in numerous cellular processes, including cell motility, adhesion, and proliferation, by regulating the activity of Rho GTPases. Its expression is altered in various human cancers and is associated with malignant progression. Here, we show that RhoGDI1 interacts with Cullin 3 (CUL3), a scaffold protein for E3 ubiquitin ligase complexes. Ectopic expression of CUL3 increases the ubiquitination of RhoGDI1. Furthermore, potassium channel tetramerization domain containing 5 (KCTD5) also binds to RhoGDI1 and increases its interaction with CUL3. Ectopic expression of KCTD5 increases the ubiquitination of RhoGDI1, whereas its knockdown by RNA interference has the opposite effect. Depletion of KCTD5 or expression of dominant-negative CUL3 (DN-CUL3) enhances the stability of RhoGDI1. Our findings reveal a previously unknown mechanism for controlling RhoGDI1 degradation that involves a CUL3/KCTD5 ubiquitin ligase complex.

키워드

RhoGDI1; Rho GTPases; Cullin3; KCTD5; ubiquitination

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