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Kevin Foskett, Ph.D.


Professor, Dept of Physiology
B39 Anatomy-Chemistry Bldg./6085
215-898-1354 (fax 215-573-6808)
email: foskett@mail.med.upenn.edu



http://www.med.upenn.edu/camb/faculty/cbp/foskett.html

http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=PureSearch&db=PubMed&details_term=Foskett JK


Click here for selected publications since Dr. Foskett's arrival at Penn

RESEARCH INTERESTS

Molecular physiology of the inositol trisphosphate receptor calcium release channel and the cystic fibrosis chloride channel.

RESEARCH TECHNIQUES

Molecular, biochemical and biophysical characterization of ion channels and associated interacting proteins: cloning and mutagenesis; recombinant protein purification; chromatography; bacterial, insect, frog and mammalian cell expression; yeast two-hybrid screens; patch clamp electrophysiology of single channels in native intracellular membranes; two-electrode and transepithelial voltage clamp; confocal fluorescence

RESEARCH SUMMARY

Our laboratory is interested in calcium signaling mediated by the inositol trisphosphate (IP3) pathway, a system that becomes engaged by a wide variety of cellular stimuli. At the heart of this ubiquitous system is the IP3 receptor, a calcium ion channel localized in the endoplasmic reticulum. Mutation of this channel in animal models causes neurological defects, including epilepsy; and alterations of this pathway have been associated with Alzheimer's Disease, programmed cell death and viral infection. We use novel electrophysiological methods we developed to study the gating and regulation and structural features of native and recombinant IP3 receptor channels. Because calcium signals are highly localized in both space and time, we are engaged in discovering proteins that interact with this channel, because association of the channel in protein complexes may provide a mechanism to ensure spatial, temporal and target specificity in calcium signaling. We recently discovered interactions of the channel with proteins that regulate cell death (bcl-2 proteins) and are involved in Alzheimer's Disease (presenilins). The biophysical and cell biological aspects of these are current foci in the lab.

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