Biography

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Biography

Jennifer Kohler completed her undergraduate degree in Chemistry at Bryn Mawr College.  Her Ph.D. studies, focused on the kinetics of protein-DNA interactions, were conducted in the laboratory of Prof. Alanna Schepartz, in the Chemistry Department at Yale University.  From 2000-2004, Jennifer was an American Cancer Society postdoctoral fellow with Prof. Carolyn Bertozzi at the University of California, Berkeley.  Research in the Kohler lab focuses on understanding the roles of glycoconjugates in a variety of biological systems.

Research summary

Glycosylation is the elephant in the room of biomedical research.  Estimates suggest that more than 50% of eukaryotic proteins are glycosylated, and new forms of protein glycosylation are still being discovered.  Glycosylation is also a common feature of lipids, with at least 200 distinct glycolipid structures known in eukaryotes.  Unconjugated polysaccharide chains are also abundant and diverse in structure.  In fact, about 2% of human genes are involved in carbohydrate metabolism and glycosylation.  Individual differences in glycosylation may underlie much of human variation.  Clearly, evolution has favored an emphasis on glycosylation; however, the modern research environment is less conducive to focusing on carbohydrate-containing molecules.

Unfortunately, many of the biochemical and analytical techniques that are used to study protein-protein interactions are poorly suited to the study of glycosylated molecules.  First, glycan-mediated interactions are typically low affinity and do not survive the rigorous purification steps often used to identify binding partners.  Second, protein-centric methods do not take into account that fact that glycosylated proteins typically exist as a mixture of glycoforms, each of which may have unique binding properties and activities.  Finally, in many techniques (yeast two-hybrid, heterologous expression systems) the critical glycans are either absent on altered.

My research group at UT Southwestern is committed to developing and implementing new tools that are optimized for the study of glycosylated molecules.  In particular, we invested significant effort in the development of photocrosslinking sugar analogs that can be metabolically incorporated into cellular glycoconjugates and used to covalently crosslink glycan-mediated interactions.  These tools can now be deployed to study and identify transient glycan-mediated interactions.  Our current research efforts are focused in two broad areas: (1) sialic acid-containing glycoconjugates (sialosides); and (2) O-GlcNAc-modified proteins.  We are currently using photocrosslinking sialic acid analogs to study the interactions of sialic acid-interacting proteins, particularly those involved in infectious disease and in cancer metastasis.  We are using photocrosslinking GlcNAc to investigate the interactions of nucleoporins and other O-GlcNAc-modified proteins. In addition to our photocrosslinking studies, we have developed a new two-hybrid technique that can be used to interrogate protein-protein interactions in the Golgi and eukaryotic cells. 

Education

Graduate School
Yale University , Chemistry
Graduate School
Bryn Mawr College (1994), Chemistry

Research Interest

  • carbohydrates
  • chemical biology
  • glycobiology
  • Golgi
  • membrane proteins

Publications

Featured Publications LegendFeatured Publications

Photocrosslinkers illuminate interactions in living cells.
Tanaka Y, Bond MR, Kohler JJ Mol Biosyst 2008 Jun 4 6 473-80
Chemical methods for glycoprotein discovery.
Bond MR, Kohler JJ Curr Opin Chem Biol 2007 Feb 11 1 52-8
A century at the chemistry-biology interface.
Kohler JJ Nat. Chem. Biol. 2006 Jun 2 6 288-92
Regulating cell surface glycosylation with a small-molecule switch.
Dube DH, de Graffenried CL, Kohler JJ Meth. Enzymol. 2006 415 213-29
A small-molecule switch for Golgi sulfotransferases.
de Graffenried CL, Laughlin ST, Kohler JJ, Bertozzi CR Proc. Natl. Acad. Sci. U.S.A. 2004 Nov 101 48 16715-20
Directing flux in glycan biosynthetic pathways with a small molecule switch.
Kohler JJ, Czlapinski JL, Laughlin ST, Schelle MW, de Graffenried CL, Bertozzi CR Chembiochem 2004 Oct 5 10 1455-8
Regulating cell surface glycosylation by small molecule control of enzyme localization.
Kohler JJ, Bertozzi CR Chem. Biol. 2003 Dec 10 12 1303-11
Effects of nucleic acids and polyanions on dimer formation and DNA binding by bZIP and bHLHZip transcription factors.
Kohler JJ, Schepartz A Bioorg. Med. Chem. 2001 Sep 9 9 2435-43
Kinetic studies of Fos.Jun.DNA complex formation: DNA binding prior to dimerization.
Kohler JJ, Schepartz A Biochemistry 2001 Jan 40 1 130-42
Gene regulation: protein escorts to the transcription ball.
Chin JW, Kohler JJ, Schneider TL, Schepartz A Curr. Biol. 1999 Dec 16-30 9 24 R929-32

Books

Featured Books Legend Featured Books

Mass Spectrometry of Glycoproteins: Methods and Protocols

Jennifer J. Kohler & Steven M. Patrie (Ed.) (2012). Humana Press

Honors & Awards

  • Research Fellowship
    Alfred P. Sloan Foundation (2009)
  • Basil O’Connor Starter Scholar Research Award
    March of Dimes (2007)
  • CAREER Award
    National Science Foundation (2007)
  • New Faculty Award
    Camille and Henry Dreyfus Foundation (2005)

Professional Associations/Affiliations

  • Society for Glycobiology (2007)
  • American Chemical Society (1995)