Ron Kopito

Title
Associate Professor

Department
Biological Sciences

Research Interests

Email
kopito@stanford.edu

Phone
723-7581

Fax
723-8475

Address
Gilbert Rm 304A
Mail Code: 5020

Faculty Research Description
Research in Professor Kopito's laboratory is concerned with understanding the molecular basis of ion transport and intracellular protein folding. Biophysical and biochemical studies focus on the quaternary structure, ion permeation pathway and gating mechanisms of anion transporting channels and exchangers. Professor Kopito's lab is also investigating the process of intracellular folding and biogenesis of these proteins. Current work includes:
1) Determining the molecular mechanism of ATP-dependent gating of CFTR, a chloride channel that is defective in individuals with the hereditary disease cystic fibrosis.
2) Investigating the intracellular "quality control" apparatus that distinguishes and destroys improperly folded membrane proteins.
3) Studying the role of the membrane skeleton in restricting the mobility of integral membrane anion exchangers in neuronal plasma membranes; identifying the molecular determinants of the site of interaction between anion exchangers and the membrane skeleton.

Ward, C.L. and R.R. Kopito. 1995. Degradation of CFTR by the ubiquitin proteosome pathway. Cell 83:121-127.

Gunderson, K.L., and R.R. Kopito. 1995. Conformational states of CFTR associated with channel gating: The role of ATP binding and hydrolysis. Cell 82:231-239.

Sekler, I., R.R. Koptio, and J.R. Casey. 1995. High level expression, partial purification, and functional reconstitution of the human AE1 anion exchanger in Saccharomyces cerevisiae. J. Biol. Chem. 270:21028-21034.

Casey, J.R., Y. Ding, and R.R. Kopito. 1995. The role of cysteine residues in the arythrocyte plasma membrane anion exchanger, AE1. J. Biol. Chem. 270:8521-8527.

Kobayashi, S., C.W. Morgans, J.R. Casey, and R.R. Kopito. 1994. AE3 anion exchanger isoforms in the vertebrate retina: Developmental regulation and differential expression in neurons and glia. J. Neurosci. 14:6266-6279.

Areas of Study
Cellular Neurobiology
Membrane Excitability
Molecular Neurobiology
SBRC
Ph.D.