Rory Fisher, PhD

Neuroscience and Pharmacology

Office: 2-512 BSB
Office Phone: 319-335-8330

Lab: 2-505 BSB

Lab Website:

Molecular biology and signal transduction of G protein-coupled receptors (GPCRs) and RGS proteins

Our research focuses on the molecular/cell biology and signaling/physiological roles of RGS proteins. RGS proteins function as essential negative regulators of heterotrimeric G protein signaling by virtue of their GTPase-activating protein activity on G subunits. By cloning members of the human RGS protein family, we identified surprising differences in RGS protein structure and found that such differences are important for localization of RGS proteins and their interactions with other proteins involved in their signaling. We have studied RGS protein roles in G protein signaling, identified exceptional complexity in processing of RGS protein transcripts, and recently provided the first description of how an RGS gene is transcriptionally activated. Our studies have revealed that some RGS proteins are localized to the nucleus, where G proteins are not found, and exhibit signaling activities not involving G proteins. Our current focus is on RGS6, which we originally identified and cloned. We recently discovered, using mice lacking RGS6, an important physiological role of RGS6 as an essential negative modulator of parasympathetic signaling in heart. Also, we recently found that RGS6 plays an essential role as a novel mediator of p53 activation and apoptosis during DNA damage and as a tumor suppressor. These studies raise questions of considerable interest and importance concerning the role of RGS proteins in cellular regulation and human disease. Some current projects include characterizing novel signaling actions of RGS proteins, transgene technologies to probe physiological roles of RGS proteins and cloning and characterizing undiscovered forms of RGS6 we have identified.

PubMed link

Department/Program Affiliations:
Internal Medicine
Molecular Medicine
Neuroscience and Pharmacology