tailieunhanh - Pin1 is involved in HDAC6-mediated cancer cell motility

Histone deacetylase 6 (HDAC6), a member of the HDAC enzymes, has been reported to play substantial roles in many cellular processes. Evidence shows that deregulation of HDAC6 may be involved in the progression of some cancers, neurodegenerative diseases, and inflammatory disorders. | Int. J. Med. Sci. 2018 Vol. 15 1573 ivyspring international publisher Research Paper InternationalJournal ofMedicalSciences 2018 15 13 1573-1581. doi Pin1 Is Involved in HDAC6-mediated Cancer Cell Motility Hsiang-Hao Chuang1 Ming-Shyan Huang2 3 Pei-Hui Wang1 Yu-Peng Liu4 Michael Hsiao5 and Chih-Jen Yang1 67 1. Division of Pulmonary and Critical Care Medicine and Department of Internal Medicine Kaohsiung Medical University Hospital Kaohsiung Medical University Kaohsiung Taiwan 2. Department of Internal Medicine E-DA Cancer Hospital Kaohsiung Taiwan 3. School of Medicine I-Shou University Kaohsiung Taiwan 4. Graduate Institute of Clinical Medicine Kaohsiung Medical University Kaohsiung Taiwan 5. Genomics Research Center Academia Sinica Taipei Taiwan 6. Department of Internal Medicine Kaohsiung Municipal Ta-Tung Hospital Kaohsiung Medical University Kaohsiung Taiwan 7. Faculty of Medicine Department of Respiratory Therapy College of Medicine Kaohsiung Medical University Taiwan These authors contributed equally to this work. El Corresponding author Dr. Chih-Jen Yang Tel 886-7-3121101 Fax 886-7-3161210 E-mail chjeya@ Ivyspring International Publisher. This is an open access article distributed under the terms of the Creative Commons Attribution CC BY-NC license https licenses by-nc . See http terms for full terms and conditions. Received Accepted Published Abstract Histone deacetylase 6 HDAC6 a member of the HDAC enzymes has been reported to play substantial roles in many cellular processes. Evidence shows that deregulation of HDAC6 may be involved in the progression of some cancers neurodegenerative diseases and inflammatory disorders. However little is known regarding the effect of post-translational modification of HDAC6 on cellular localization and biological functions. In the present study we identified four phosphorylation sites on HDAC6 under normal .