Christopher D. Lima

Memorial Sloan Kettering Cancer Center


Primary Section: 21, Biochemistry
Membership Type: Member (elected 2020)

Biosketch

Christopher Lima is a biochemist and structural biologist. He is recognized for his work characterizing macromolecules involved in post-translational protein modification by ubiquitin and ubiquitin-like proteins. He is also regarded for his work studying molecular complexes that contribute to co- and post-transcriptional RNA maturation, processing, and decay. Lima was born in Willoughby, Ohio and raised in Mentor, Ohio. He graduated from Ohio State University with a B.A. degree in Biochemistry in 1989, and in 1994 with a Ph.D. in Biochemistry and Biophysics from Northwestern University where he studied with Alfonso Mondragon. After postdoctoral studies as a Helen Hay Whitney Fellow at Columbia University with Wayne Hendrickson he joined the faculty at the Weill Medical College of Cornell University in 1998 before moving to the Sloan Kettering Institute in 2003. Lima has been named a Beckman Young Investigator, a Rita Allan Scholar and an Investigator of the Howard Hughes Medical Institute. He is an elected member of the American Academy of Arts and Sciences and the National Academy of Sciences.

Research Interests

Christopher Lima’s laboratory is focused on revealing molecular mechanisms in RNA processing and decay pathways and in post-translational modification by ubiquitin-like proteins. His lab employs biochemistry to reconstitute pathways and structural approaches to determine molecular architectures that illuminate function. Ubiquitin (Ub) and SUMO are members of the ubiquitin-like (Ubl) protein family and their conjugation to protein substrates is required for nearly every cellular process from protein degradation to cell-cycle progression to DNA repair. His lab investigates enzyme-substrate and receptor-substrate complexes representing key steps in Ub/Ubl pathways and Ub/Ubl-mediated signaling. In studies related to RNA processing, decay and repair his interests included characterization of RNA ligase and enzymes that catalyze 5’ mRNA cap formation. His lab pioneered methods to reconstitute eukaryotic RNA exosomes, essential multi-subunit 3’ to 5’ exoribonucleases whose activities are often coordinated by RNA helicases and a variety of upstream factors. His lab’s studies continue to define biochemical activities, architectures and functions for eukaryotic RNA exosomes in a variety of processes that control gene expression through cytoplasmic and nuclear RNA processing, decay, and surveillance.

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