R. Tyler Miller

Professor

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RESEARCH DESCRIPTION

General Description: Many of the signals that regulate cell functions act via heterotrimeric G proteins and their heptahelical receptors. These signals include light that activates rhodopsin and transducin, odorant molecules that activate receptors in the nose, receptors for catecholamines and autacoids, and receptors for peptide hormones. Heterotrimeric G proteins have been arranged in four families based on structure, and loosely on function, the Gs, Gi, Gq and G12/13 families. Receptors are able to discriminate among these G proteins in part by their structures. However, there is greater specificity and speed of signaling in vivo than can be explained solely on the basis of receptor and G protein structure, suggesting that additional factors contribute to the specificity that is seen in vivo. My laboratory is working on a number of projects that relate to the mechanisms by which signaling specificity is determined by the extracellular Ca-sensing receptor (CaR). These include determining which signaling pathways the CaR activates (focusing on phospholipases, kinases, and the Na/H exchanger), characterizing the interaction of the CaR with filamin, a cytoskeletal protein that also acts as a scaffold for signaling proteins, and additional proteins that interact with the CaR including members of the inwardly-rectifying potassium channel family. We are also beginning to study the effects of mechanical force on the cytoskeletal structure and behavior of glomerular podocytes. Our studies focus on filamin because it is the principal determinant of cytoskeletal rigidity and strength, and because its levels are reduced in models of glomerular injury.

RELATED RESEARCH AREAS

View R. Tyler Miller's Publications on PubMed