Rory Fisher, Ph.D. (Affiliate)
Professor, Dept. of Pharmacology, University of Iowa

http://www.medicine.uiowa.edu/pharmacology/faculty/fisher.html

Research Interest    

Dr. Fisher's efforts have focused on molecular cloning and characterization of new members of the human RGS protein family. These efforts have revealed surprising diversity in this family, raising the intriguing possibility that RGS proteins possess diverse functional activities. Dr. Fisher and his laboratory have used RGS protein clones to characterize their role in GPCR signaling and the mechanisms underlying their subcellular trafficking. They have identified the structural organization of genes encoding numerous RGS proteins, revealing exceptional complexity in splicing of some RGS protein transcripts (e.g., 36 splice forms of RGS6) and facilitating gene knock-in and knock-out studies (functional genomics) to determine the role of these proteins in organisms. Recent studies have revealed novel signaling functions of RGS proteins in the nucleus, in neuronal differentiation and in development. These studies raise questions of considerable interest and importance concerning the role of RGS proteins in cellular regulation by mechanisms both dependent on and independent of their regulatory actions on G proteins. Some current projects include identification of novel RGS protein interaction partners, anti-sense and transgene technologies to probe physiological roles of RGS proteins and identification of mechanisms underlying regulatory effects of RGS proteins on gene expression.

Publications

Carlson, S.A., Chatterjee, T.K. and Fisher, R.A. The third intracellular domain of the platelet-activating factor receptor is a critical determinant in receptor coupling to phosphoinositide phospholipase C-activating G proteins: Studies using intracellular domain minigenes and receptor chimeras. J. Biol. Chem. 271(38): 23146-23153, 1996.

Chatterjee, T.K., Sharma, R.V. and Fisher, R.A. Molecular cloning of a novel variant of the pituitary adenylate cyclase-activating polypeptide (PACAP) receptor that stimulates calcium influx by activation of L-type calcium channels. J. Biol. Chem. 271(50): 32226-32232, 1996.

Chatterjee, T.K., Liu, X., Davisson, R.L. and Fisher, R.A. Genomic organization of the rat pituitary adenylate cyclase activating polypeptide receptor gene: Alternative splicing within the 5'-untranslated region. J. Biol. Chem. 272(18): 12122-12131, 1997.

Chatterjee, T.K., Eapen, A.K. and Fisher, R.A. A truncated form of RGS3 negatively regulates G protein-coupled receptor stimulation of adenylyl cyclase and phosphoinositide phospholipase C. J. Biol. Chem., 272(24): 15481-15487, 1997.

Chatterjee, T.K., and Fisher, R.A. Cytoplasmic, nuclear and golgi localization of RGS proteins: evidence for N-terminal and RGS domain sequences as intracellular targeting motifs. J. Biol. Chem. 275: 24013-24021, 2000.

Chatterjee, T.K., and Fisher, R.A. Novel alternative splicing and nuclear localization of human RGS12 gene products. J. Biol. Chem. 275: 29660-29671, 2000.

Chatterjee, T.K. and Fisher, R.A. RGS12TS-S localizes at nuclear matrix-associated subnuclear structures and represses transcription: structural requirements for subnuclear targeting and transcriptional repression. Mol. Cell Biol. 22: 4334-4345, 2002.

Liu, Z., Chatterjee, T.K. and Fisher, R.A. RGS6 interacts with SCG10 and promotes neuronal differentiation: role of the G-gamma subunit-like (GGL) domain of RGS6. J. Biol. Chem. 277:37832-37839, 2002.

Chatterjee, T.K., Liu, Z. and Fisher, R.A. RGS6 gene structure, complex alternative splicing, and role of N terminus and G protein g -subunit-like (GGL) domain in subcellular localization of RGS6 splice variants. J. Biol. Chem. 278: 30261-30271, 2003.

Chatterjee, T.K., and Fisher, R.A. Mild heat and proteotoxic stress promote unique subcellular trafficking and nucleolar accumulation of RGS6 and other RGS proteins: Role of the RGS domain in stress-induced trafficking of RGS proteins. J. Biol. Chem. 278: 30272-30282, 2003.

Liu, Z., and Fisher, R.A. RGS6 interacts with DMAP1 and Dnmt1 and inhibits DMAP1 transcriptional repressor activity. J. Biol. Chem. 279:14120-14128, 2004.

Publications from Gene Therapy Center

Publications from PubMed