PMID- 19738442 OWN - NLM STAT- MEDLINE DCOM- 20100104 LR - 20190516 IS - 1554-8635 (Electronic) IS - 1554-8627 (Linking) VI - 5 IP - 7 DP - 2009 Oct TI - The complexity in regulation of MEF2D by chaperone-mediated autophagy. PG - 1073-4 AB - Chaperone-mediated autophagy (CMA) targets specific cytoplasmic proteins for degradation by lysosomes and has been implicated to play a role in neurodegeneration. Our recent studies identify neuronal survival factor MEF2D as a direct substrate of CMA and show that dysregulation of this process may contribute to the pathogenesis of Parkinson disease. One interesting finding presented in our study is the apparent loss of DNA binding capacity by the accumulated MEF2D following inhibition of CMA. The possibilities and implication of this finding are discussed. FAU - Yang, Qian AU - Yang Q AD - Department of Pharmacology and Neurology, Emory University School of Medicine, Atlanta, GA 30322, USA. FAU - Mao, Zixu AU - Mao Z LA - eng GR - AG023695/AG/NIA NIH HHS/United States GR - ES015317/ES/NIEHS NIH HHS/United States GR - NS048254/NS/NINDS NIH HHS/United States PT - Journal Article PT - Research Support, N.I.H., Extramural DEP - 20091015 PL - United States TA - Autophagy JT - Autophagy JID - 101265188 RN - 0 (MADS Domain Proteins) RN - 0 (MEF2 Transcription Factors) RN - 0 (MEF2D protein, human) RN - 0 (Molecular Chaperones) RN - 0 (Myogenic Regulatory Factors) SB - IM MH - Autophagy/*physiology MH - Humans MH - MADS Domain Proteins/*metabolism MH - MEF2 Transcription Factors MH - Molecular Chaperones/*metabolism MH - Myogenic Regulatory Factors/*metabolism MH - Neurons/metabolism MH - Parkinson Disease/physiopathology EDAT- 2009/09/10 06:00 MHDA- 2010/01/05 06:00 CRDT- 2009/09/10 06:00 PHST- 2009/09/10 06:00 [entrez] PHST- 2009/09/10 06:00 [pubmed] PHST- 2010/01/05 06:00 [medline] AID - 9824 [pii] AID - 10.4161/auto.5.7.9824 [doi] PST - ppublish SO - Autophagy. 2009 Oct;5(7):1073-4. doi: 10.4161/auto.5.7.9824. Epub 2009 Oct 15.