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Protein Disordered in Neurodegeneration and Neurotransmission: Alpha-Synuclein and Complexin

Weekly Seminar
Who Should Attend: 


Guest Speaker
David Eliezer, Ph.D.
Professor of Biochemestry and Neuroscience
Weill Cornell Medicine


Disordered proteins mediate critical functions at neuronal synaptic junctions, including the fusion of synaptic vesicles with the presynaptic plasma membrane. The disordered proteins complexin and synuclein regulate vesicle exocytosis in ways that remain poorly understood, and both proteins are involved in neurodegenerative and neurological disorders. I will present results from our investigations of the structural properties of these proteins and their interactions with lipid membranes in order to shed further light on their functional mechanisms in regulating neurotransmission, as well as on the role of membrane interactions in the aggregation of alpha-synuclein in Parkinson’s disease.

David Eliezer, Ph.D. Figure 


Snead D, Lai AL, Wragg RT, Parisotto DA, Ramlall TF, Dittman JS, Freed JH, Eliezer D.
Unique Structural Features of Membrane-Bound C-Terminal Domain Motifs Modulate Complexin Inhibitory Function.
Front Mol Neurosci. 2017 May 24;10:154. doi: 10.3389/fnmol.2017.00154. eCollection 2017.
Igor Dikiy, Bruno Fauvet, Ana Jovičić, Anne-Laure Mahul-Mellier, Carole Desobry, Farah El-Turk, Aaron D. Gitler, Hilal A. Lashuel, and David Eliezera.
Semisynthetic and in vitro phosphorylation of alpha-synuclein at Y39 promotes functional partly-helical membrane-bound states resembling those induced by PD mutations.
ACS Chem Biol. 2016 Sep 16;11(9):2428-37. doi: 10.1021/acschembio.6b00539.
Snead D, Eliezer D.
Alpha-synuclein function and dysfunction on cellular membranes.
Exp Neurobiol. 2014 Dec;23(4):292-313. doi: 10.5607/en.2014.23.4.292. Epub 2014 Dec 12.


Tuesday, December 12, 2017 - 12:30pm


Burke Medical Research Institute
785 Mamaroneck Avenue
White Plains, NY 10605
United States
Conference Room: 
Billings Building – Rosedale

Research Methods