HDAC6 mediates the acetylation of TRIM50 |
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| Affiliation: | 1. Medical Genetics Unit, IRCCS Casa Sollievo Della Sofferenza Hospital, 71013 San Giovanni Rotondo, Italy;2. Telethon Institute of Genetics and Medicine, Via P. Castellino 111, 80131 Naples, Italy;3. CEINGE Advanced Biotechnology and Department of Organic Chemistry and Biochemistry, Federico II University, 80131 Napoli, Italy;4. Scienze della Riproduzione e dello Sviluppo, University of Trieste, Italy;2. Department of Cell and Developmental Biology, University College London, London WC1E 6BT, UK;1. Department of Neurology, Drum Tower Hospital, Medical School and The State Key Laboratory of Pharmaceutical Biotechnology, Nanjing University, Nanjing 210008, China;2. Institute of Brain Science, Nanjing University, Nanjing 210008, China;3. Department of Neurology, Nanjing Hospital of Chinese Medicine Affiliated to Nanjing University of Chinese Medicine, Nanjing 210001, China |
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| Abstract: | The E3 Ubiquitin ligase TRIM50 promotes the formation and clearance of aggresome-associated polyubiquitinated proteins through HDAC6 interaction, a tubulin specific deacetylase that regulates microtubule-dependent aggresome formation. In this report we showed that TRIM50 is a target of HDAC6 with Lys-372 as a critical residue for acetylation. We identified p300 and PCAF as two TRIM50 acetyltransferases and we further showed that a balance between ubiquitination and acetylation regulates TRIM50 degradation. |
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