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Ron Kopito
Email:
Profile: http://med.stanford.edu/profiles/Ron_Kopito/
Alternate Contact: Academic Appointments
Appointment
Organization
Professor
Member
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Honors & Awards
Title
Organization
Date(s)
Established Investigator
American Heart Association
1993
Presidential Young Investigator
National Science Foundation
1989
Scholar in Biomedical Science
Lucille P. Markey Foundation
1985
Basil O'Connor Award
March of Dimes
1989
Professional Education
Degree
Awarding Institution
Field of Study
Year of Graduation
A.B.
Bowdoin College
Biochemistry
1976
Ph.D.
MIT
Biochemistry
1982
Web Site Links
Research/Lab website:
Kopito Lab
Research Interests
Our lab studies the cellular mechanisms that monitor protein biogenesis and ensure that only properly folded and assembled proteins are deployed within the cell. Proteins that fail to fold or assemble correctly can acquire alternative conformations that may give rise to highly toxic products. Therefore, cells contain machinery to recognize and destroy malfolded proteins. Mutations and genetic polymorphisms can result in the synthesis of misfolded polypeptides. Human genetic diseases therefore constitute a fertile source of naturally occurring mutants that provide insight into the nature of these “quality control” mechanisms. Both cis-acting mutations that directly affect the production of correctly assembled proteins and trans-acting mutations that affect the function of the cellular quality control machinery are linked to such diverse genetic disorders as cystic fibrosis and Lou Gehrig’s and Huntington’s diseases.
Research in the Kopito lab is focused on two general questions:
(1) How do cells make sure that only structurally “correct” proteins are deployed? How do cells discriminate between folded and misfolded
proteins? Genetic biochemical and cell biological approaches are used to identify the machinery involved in recognizing and destroying misfolded proteins.
(2) How do misfolded proteins acquire toxic properties that lead to cell death and ultimately to neurodegeneration? What mechanisms do neurons have to suppress the formation of such toxic conformers and why in some cases do these mechanisms fail? Biochemical biophysical and genetic approaches ranging from fluorescence spectroscopy to the creation of transgenic and knockout mice are applied to address these
questions.
proteins? Genetic biochemical and cell biological approaches are used to identify the machinery involved in recognizing and destroying misfolded proteins.
questions.
Publications
- Bruns CK, Kopito RR "Impaired post-translational folding of familial ALS-linked Cu, Zn superoxide dismutase mutants." EMBO J 2007; More »
- Bennett EJ, Shaler TA, Woodman B, Ryu KY, Zaitseva TS, Becker CH, Bates GP, Schulman H, Kopito RR "Global changes to the ubiquitin system in Huntington's disease." Nature 2007; 448: 7154: 704-8 More »
- Ryu KY, Sinnar SA, Reinholdt LG, Vaccari S, Hall S, Garcia MA, Zaitseva TS, Bouley DM, Boekelheide K, Handel MA, Conti M, Kopito RR "The Mouse Polyubiquitin Gene Ubb is Essential for Meiotic Progression." Mol Cell Biol 2007; More »
- Ryu KY, Maehr R, Gilchrist CA, Long MA, Bouley DM, Mueller B, Ploegh HL, Kopito RR "The mouse polyubiquitin gene UbC is essential for fetal liver development, cell-cycle progression and stress tolerance." EMBO J 2007; 26: 11: 2693-706 More »
- Ryu KY, Baker RT, Kopito RR "Ubiquitin-specific protease 2 as a tool for quantification of total ubiquitin levels in biological specimens." Anal Biochem 2006; More »
45 publications: view full list
