Ana María Cuervo on the Science of Ageing

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Ana María Cuervo on the Science of Ageing

SCIENCE Ana María Cuervo on the NEW YORK science of ageing Mon, November 14, 2016 8:00 pm – 9:00 pm Venue 92Y, 1395 Lexington Ave, New York, NY 10128 View map Phone: 212-415-5500 Admission Buy tickets (from $32) More information 92Y Spanish biologist Ana María Cuervo discusses the cutting- edge science of human longevity with Jamie Metzl, Nir Barzilai and David Sinclair. The 92Y hosts some of the world’s leading experts on ageing: Harvard University’s David Sinclair and Nir Barzilai, Ana Maria Cuervo of Albert Einstein College of Medicine, and Science fiction writer and futurist Jamie Metzl –all gathered together to explore the prospects for the future of life. Scientists are trying to make human lives healthier and longer. Is that possible? How? Can we live to 150? Ana Maria Cuervo is a Spanish cell biologist. She studied medicine at the University of Valencia. She currently holds the Robert and Renee Belfer professorship for the study of neurodegenerative diseases. She is considered an expert in the field of autophagy, the process by which cells recycle their waste and the molecular biology of aging. Her work focuses on the causes of neurodegenerative disorders such as Alzheimer’s and Parkinson’s. Her objective is to develop therapies which can restore normal cell cleaning service and therefore prevent the accumulation of toxic proteins of dead cells and cells affected by the disease. Embassy of Spain – Cultural Office | 2801 16th Street, NW, Washington, D.C. 20009 | Tel: (202) 728-2334 View this event online: https://www.spainculture.us/city/new-york/ana-maria-cuervo-on-the-science-of-ageing/ Created on 09/24/2021 | Page 1 of 1.

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Chaperone-Mediated Autophagy: Roles in Disease and Aging Cell Research (2014) 24:92-104
npg Chaperone-mediated autophagy: roles in disease and aging Cell Research (2014) 24:92-104. 92 © 2014 IBCB, SIBS, CAS All rights reserved 1001-0602/14 $ 32.00 npg REVIEW www.nature.com/cr Chaperone-mediated autophagy: roles in disease and aging Ana Maria Cuervo1, Esther Wong2 1Department of Developmental and Molecular Biology, Institute for Aging Studies, Marion Bessin Liver Research Center, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Chanin Building 504, Bronx, NY 10461, USA; 2School of Biological Sci- ences, Nanyang Technological University, SBS-03n-05, 60 Nanyang Drive, Singapore 637551, Singapore This review focuses on chaperone-mediated autophagy (CMA), one of the proteolytic systems that contributes to degradation of intracellular proteins in lysosomes. CMA substrate proteins are selectively targeted to lysosomes and translocated into the lysosomal lumen through the coordinated action of chaperones located at both sides of the membrane and a dedicated protein translocation complex. The selectivity of CMA permits timed degradation of spe- cific proteins with regulatory purposes supporting a modulatory role for CMA in enzymatic metabolic processes and subsets of the cellular transcriptional program. In addition, CMA contributes to cellular quality control through the removal of damaged or malfunctioning proteins. Here, we describe recent advances in the understanding of the mo- lecular dynamics, regulation and physiology of CMA, and discuss the evidence in support of the contribution of CMA dysfunction to severe human disorders such as neurodegeneration and cancer. Keywords: chaperone-mediated autophagy; neurodegeneration; cancer; aging Cell Research (2014) 24:92-104. doi:10.1038/cr.2013.153; published online 26 November 2013 Introduction the lysosomal membrane and then gain access to the lu- men of this organelle by directly crossing its membrane.
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Dopamine-Modified Α-Synuclein Blocks Chaperone-Mediated Autophagy
Dopamine-modified α-synuclein blocks chaperone-mediated autophagy Marta Martinez-Vicente, … , David Sulzer, Ana Maria Cuervo J Clin Invest. 2008;118(2):777-788. https://doi.org/10.1172/JCI32806. Research Article Neuroscience Altered degradation of α-synuclein (α-syn) has been implicated in the pathogenesis of Parkinson disease (PD). We have shown that α-syn can be degraded via chaperone-mediated autophagy (CMA), a selective lysosomal mechanism for degradation of cytosolic proteins. Pathogenic mutants of α-syn block lysosomal translocation, impairing their own degradation along with that of other CMA substrates. While pathogenic α-syn mutations are rare, α-syn undergoes posttranslational modifications, which may underlie its accumulation in cytosolic aggregates in most forms of PD. Using mouse ventral medial neuron cultures, SH-SY5Y cells in culture, and isolated mouse lysosomes, we have found that most of these posttranslational modifications of α-syn impair degradation of this protein by CMA but do not affect degradation of other substrates. Dopamine-modified α-syn, however, is not only poorly degraded by CMA but also blocks degradation of other substrates by this pathway. As blockage of CMA increases cellular vulnerability to stressors, we propose that dopamine-induced autophagic inhibition could explain the selective degeneration of PD dopaminergic neurons. Find the latest version: https://jci.me/32806/pdf Research article Dopamine-modified α-synuclein blocks chaperone-mediated autophagy Marta Martinez-Vicente,1,2 Zsolt Talloczy,3,4 Susmita Kaushik,1,2 Ashish C. Massey,1,2 Joseph Mazzulli,5 Eugene V. Mosharov,3,4 Roberto Hodara,5 Ross Fredenburg,6 Du-Chu Wu,4,7 Antonia Follenzi,2 William Dauer,4 Serge Przedborski,4,7 Harry Ischiropoulos,5 Peter T.
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Ana Maria Cuervo MD Phd
Ana Maria Cuervo MD PhD CONTENTS I. C.V. Personal and professional information Awards and Honors Scientific Review Editorial Tasks Organization of meetings Advisory groups Invited presentations II. Publication List III. Teaching and Related Activities IV. Administration V. Research Support (past and active) Wikipedia: #1day#1women initiative: Ana Maria Cuervo February 20 Ana Maria Cuervo, MD PhD CURRICULUM VITAE PERSONAL INFORMATION Date of Birth: July 14, 1966 Place of Birth: Barcelona, Spain Citizenship: American Address: Department of Developmental and Molecular Biology, Chanin Building R. 504, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461 Phone: (718) 430 2689 Fax: (718) 430 8975 e-mail: ana-maria. [email protected] POSITION TITLE Robert and Renee Belfer Chair for the Study of Neurodegenerative Diseases Professor Dept. of Development and Molecular Biology (with tenure) Professor Dept. of Medicine (with tenure) Professor Dept. of Anatomy and Structural Biology (with tenure) Co-Director of the Einstein Institute for Aging Research Member of the Marion Bessin Liver Research Center of the Albert Einstein College of Medicine. Member of the Albert Einstein Cancer Center Member of the Diabetes Research Center EDUCATION/TRAINING Institution and Location Degree Year Field of Study University of Valencia, Spain M.D. 1990 Medicine University of Valencia, Spain Ph.D. 1994 Biochem. & Mol. Biol. Tufts University, Boston, USA Postdoc 1995/8 Physiology Professional employment and Hospital appointments 1985/90 Research Fellow-Medical Student, Department of Physiology, School of Medicine, University of Valencia, Spain. 1991/94 Predoctoral Fellow, Instituto de Investigaciones Citologicas, Valencia, Spain. 1995/97 Postdoctoral Fellow, Department of Physiology, Tufts University, Boston MA, USA.
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ORIGINAL RESEARCH ARTICLE 1359 JournalJournal ofof Cellular Phosphorylation-Regulated Physiology Degradation of the Tumor- Suppressor Form of PED by Chaperone-Mediated Autophagy in Lung Cancer Cells CRISTINA QUINTAVALLE,1,2 STEFANIA DI COSTANZO,1 CIRO ZANCA,1 IMMACULADA TASSET,3 ALESSANDRO FRALDI,4 MARIAROSARIA INCORONATO,5 PEPPINO MIRABELLI,5 MARIA MONTI,6 ANDREA BALLABIO,4 PIERO PUCCI,6 3 1,2 ANA MARIA CUERVO, AND GEROLAMA CONDORELLI * 1Department of Molecular Medicine and Medical Biotechnology, ‘‘Federico II” University of Naples, Naples, Italy 2Institute of Endocrinology and Experimental Oncology ‘‘G. Salvatore” (IEOS), Consiglio Nazionale delle Ricerche (CNR), Naples, Italy 3Department of Developmental and Molecular Biology, Albert Einstein College of Medicine, New York, New York 4Telethon Institute of Genetics and Medicine (TIGEM), Naples, Italy 5IRCCS, SDN Foundation Institute of Diagnostic and Nuclear Development (SDN), Naples, Italy 6Department of Chemical Science, ‘‘Federico II” University of Naples, Naples, Italy PED/PEA-15 is a death effector domain (DED) family member with a variety of effects on cell growth and metabolism. To get further insight into the role of PED in cancer, we aimed to find new PED interactors. Using tandem affinity purification, we identified HSC70 (Heat Shock Cognate Protein of 70 kDa)—which, among other processes, is involved in chaperone-mediated autophagy (CMA)—as a PED-interacting protein. We found that PED has two CMA-like motifs (i.e., KFERQ), one of which is located within a phosphorylation site, and demonstrate that PED is a bona fide CMA substrate and the first example in which phosphorylation modifies the ability of HSC70 to access KFERQ-like motifs and target the protein for lysosomal degradation.
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Albert Einstein College Finds Parkinson Gene
Albert Einstein college finds Parkinson gene 04 March 2013 | News | By BioSpectrum Bureau Singapore: Researchers at Albert Einstein College of Medicine of Yeshiva University, US, have discovered how the most common genetic mutations in familial Parkinson's disease damage brain cells. The most common mutations responsible for the familial form of Parkinson's disease affect a gene called leucine-rich repeat kinase-2 (LRRK2). The mutations cause the LRRK2 gene to code for abnormal versions of the LRRK2 protein. But it hasn't been clear how LRRK2 mutations lead to the defining microscopic sign of Parkinson's: the formation of abnormal protein aggregates inside dopamine-producing nerve cells of the brain. The study involved mouse neurons in tissue culture from four different animal models, neurons from the brains of patients with Parkinson's with LRRK2 mutations, and neurons derived from the skin cells of Parkinson's patients via induced pluripotent stem (iPS) cell technology. All the lines of research confirmed the researchers' discovery. "Our study found that abnormal forms of LRRK2 protein disrupt an important garbage-disposal process in cells that normally digests and recycles unwanted proteins including one called alpha-synuclein - the main component of those protein aggregates that gunk up nerve cells in Parkinson's patients," said study leader Dr Ana Maria Cuervo, professor of developmental and molecular biology, of anatomy and structural biology, and of medicine and the Robert and Renee Belfer chair for the study of neurodegenerative diseases at the college. Dr Cuervo, "We showed that when LRRK2 inhibits chaperone-mediated autophagy, alpha-synuclein doesn't get broken down and instead accumulates to toxic levels in nerve cells.
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Ana Maria Cuervo, M.D., Ph.D
Ana Maria Cuervo, M.D., Ph.D. Professor, Developmental and Molecular Biology Professor, Anatomy and Structural Biology Co-Director, Institute for Aging Research Robert and Renée Belfer Chair for the Study of Neurodegenerative Diseases Dr. Ana Maria Cuervo obtained her M.D. and Ph.D. in Biochemistry and Molecular biology from the University of Valencia (Spain) in 1990 and 1994, respectively, and received postdoctoral training at Tufts University in Boston, MA. In 2002, she started her laboratory at Albert Einstein College of Medicine. She is a recognized leader in the field of protein degradation and the biology of aging. In 2019, she was elected to the National Academy of Sciences. Dr. Cuervo has been the recipient of prestigious awards, including the P. Benson Award in Cell Biology, the Keith Porter Lecture (Award), the Nathan Shock Memorial Lecture Award, the Vincent Cristofalo Aging Award, the Bennett J. Cohen Award in Aging Biology, the Marshall Horwitz Prize, and the Saul Korey Prize in Translational Medicine. Dr. Cuervo has organized and chaired international conferences on protein degradation and aging, has presented lectures at numerous national and international scientific gatherings, and is a member of several research journal editorial boards and co-editor in chief of Aging Cell. Dr. Cuervo was included in the Clarivate Analytics 2018 and 2019 Highly Cited Researchers List (ranking of top 1% cited researchers). She has been a member of the National Institute on Aging (NIA) Scientific Council, the National Institutes of Health (NIH) Council of Councils, the NIA Board of Scientific Counselors, and the Advisory Committee to the NIH Deputy Director.
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