Jaya Pal Gangopadhyay, Ph.D.
Postdoctoral research fellow

Education
Calcutta University, India, 1999

Lab
Noriaki Ikemoto

Research Interests
E-C coupling in skeletal muscle---Calmodulin Regulation of Ryanodine Receptor Ca2+ channel

The overall goal of this project is to resolve the molecular mechanism of calmodulin (CaM)-mediated regulation of excitation-contraction (e-c) coupling in normal and diseased muscles.  CaM regulates calcium channel functions of the ryanodine receptor (RyR, the most important molecular component of e-c coupling) in a Ca2+-dependent manner, but little is known about the underlying molecular mechanism.  Based upon recently obtained preliminary data, we hypothesize that (1) CaM produces local conformational changes in the CaM-binding domain of RyR, (2) this conformational signal is transmitted to the Ca2+ channel by mediation of intra-molecular domain-domain interaction to open or close the channel at low Ca2+ and at high Ca2+, respectively, and (3) dissociation of CaM from RyR will make Ca2+ channels leaky, causing elevated cytoplasmic Ca2+, the condition that occur in some muscle disease. This project will likely resolve the basic mechanisms underlying the Ca2+-dependent regulation of RyR Ca2+ channels by CaM, and will provide a new clue for the better understanding of abnormal channel regulation in muscle disease.

Recent Publications:
Gangopadhyay JP, Grabarek Z, Ikemoto N. (2004) Fluorescence probe study of Ca2+- dependent interactions of calmodulin with calmodulin-binding peptides of the ryanodine receptor. Biochem Biophys Res Commun. 323:760-768.

Contact Details:
email:jaya@bbri.org, tel. 617-658-7796