ArticleMolecular and cellular biochemistry2015
Cullin 4A and 4B ubiquitin ligases interact with γ-tubulin and induce its polyubiquitination.
Article in Molecular and cellular biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 12 citations in OpenAlex.
- Docetaxel response in BRCA1,p53-deficient mammary tumor cells is affected by Huntingtin and BAP1.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Genetic requirements for repair of lesions caused by single genomic ribonucleotides in S phase.Nature communications · 2023Article
- γ-Tubulin in microtubule nucleation and beyond.Frontiers in cell and developmental biology · 2022Review
- The emerging role for Cullin 4 family of E3 ligases in tumorigenesis.Biochimica et biophysica acta. Reviews on cancer · 2019Review
- N-terminal truncations of human bHLH transcription factor Twist1 leads to the formation of aggresomes.Molecular and cellular biochemistry · 2018Article
- miR-181a-2 downregulates the E3 ubiquitin ligase CUL4A transcript and promotes cell proliferation.Medical oncology (Northwood, London, England) · 2017Article
- Cullin E3 Ligase Activity Is Required for Myoblast Differentiation.Journal of molecular biology · 2017Article
- The preclinical discovery and development of bortezomib for the treatment of mantle cell lymphoma.Expert opinion on drug discovery · 2017Review
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Regulated polyubiquitination is a key step for controlling protein degradation and maintaining proper balance between the proliferation of normal and uncontrolled cells. Addition of ubiquitin to the proteins by E3 ubiquitin ligases targets them for degradation by the 26S proteosome machinery. Discrepancies in ubiquitination and/or proteosome degradation might lead to multiple genetic disorders in humans. It is reported that CUL1 and BRCA1 ubiquitin ligases localize on centrosome region and regulate the centrosome duplication cycle for genomic stability. In the current study, we predicted the possible interaction of E3 ubiquitin ligase CUL4A complex with γ-tubulin, a centrosome-specific protein, using bioinformatic protein-protein docking analysis. We also confirmed their interaction by performing co-immunoprecipitation studies using endogenous CUL4A/B and stable cell lines that overexpress Flag-CUL4A or Flag-CUL4B. We additionally noted that the γ-tubulin was polyubiquitinated by CUL4A or 4B immune complex indicating that CUL4A or CUL4B may regulate the stability of γ-tubulin. Furthermore, the inhibition of proteosomal degradation pathway using MG132 or LLNV drugs resulted in accumulation and co-localization of CUL4A with γ-tubulin in the centrosome region. Overall, our observation has identified γ-tubulin as a novel target for E3 ubiquitin ligase CUL4 complex, and might lead to the establishment of a unique mechanism for controlling centrosome stability.
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