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Faculty Detail Faculty Entry   
Name STUART J FRANK  
Campus Address BDB 720 Zip 0012
Phone 205-934-9877
E-mail sjfrank@uab.edu" id="FacultyDetail1EmailAddress"><a href="mailto:sjfrank@uab.edu">sjfrank@uab.edu</a>
URL
 
 

Department Affiliations(s)
Appointment Type Department Division Rank
Center  Arthritis & Musculoskeletal Diseases Center  Arthritis & Musculoskeletal Diseases Center Professor
Center  Center for Aging  Center for Aging Professor
Center  Center for Metabolic Bone Disease  Center for Metabolic Bone Disease Professor
Center  Comprehensive Cancer Center  Comprehensive Cancer Center Professor
Center  Medicine  Comprehensive Diabetes Ctr Professor
Center  General Clinical Research Center  Ctr for Clinical & Translational Sci Professor
Primary  Medicine  Med - Endocrinology, Diabetes & Metabolism Professor
Secondary  Cell, Developmntl, & Integrative Biology  Cell, Developmntl, & Integrative Biology Professor

Biographical Sketch 
Stuart J. Frank (b. 1958, Wilkes-Barre, PA), Professor of Medicine, Cell Biology, and Physiology, received his B.A. summa cum laude in 1980 as a Benjamin Franklin Scholar at the University of Pennsylvania. He earned his M.D. in 1984 from Harvard Medical School. After residency in Internal Medicine at Washington University in St. Louis, Dr. Frank began fellowship training at the National Institutes of health from 1987 to 1991. His research there in Dr. Richard Klausner’s laboratory focused on T-cell antigen receptor signal transduction. Dr. Frank has been a UAB faculty member since 1991 in the Division of Endocrinology and Metabolism in the Department of Medicine, where his studies are aimed at understanding growth hormone (GH) receptor signal transduction and structure/function relationships and mechanisms of generation of the GH binding protein. He is also Chief of the Endocrinology Section in the Medical Service at the Birmingham Veterans Affairs Medical Center. His research is supported by grants from NIH and the Department of Veterans Affairs.

Society Memberships
Organization Name Position Held Org Link
AAAS  Member   
Endocrine Society  Member   
Massachusetts Medical Society  Member   
Southern Society for Clinical Investigation  Member   
 

Research/Clinical Interest
Title
Growth Hormone Action and GH Receptor Structure and Function
Description
The focus of research in my laboratory is understanding mechanisms of action of growth hormone (GH), an important metabolic and growth promoting hormone. In particular, I am interested in various aspects of GH receptor (GHR) structure and signal transduction. Our studies have examined the interaction of the GHR with a critical non-receptor cytoplasmic tyrosine kinase, JAK2, which is required for initiation of GHR signaling. We have explored the downstream signaling pathways (STAT, MAP kinase, and PI-3 kinase) activated by GH and their effects on GH-induced gene expression. Further, we are interested in the cellular determinants of sensitivity to GH and modulation of GHR availability and function. Current efforts include: 1) molecular studies of mechanisms of GH-induced activation of the JAK2 tyrosine kinase and the role of JAK2 in GHR stability and trafficking; 2) studies of mechanisms of generation of GH binding protein (GHBP), the shed extracellular domain of the GHR found in the circulation of humans, rabbits, and rodents that may modulate GH signaling; 3) studies of the role of a GH-induced disulfide-linked form of the GHR in signaling and receptor trafficking; 4) crosstalk between the GH and epidermal growth factor (EGF) signaling pathways, particularly EGF receptor and the oncogene, ErbB-2; and 5) crosstalk between the GH and insulin-like growth factor-1 (IGF-1) signaling systems. Multiple techniques including molecular and cell biological and protein chemistry approaches are being employed to achieve these goals.

Postdoc Positions Available
Date Posted Position Title
No records
 

Selected Publications 
Publication PUBMEDID
Wang, X., Cowan, J.W., Gerhart, M., Zelickson, B.R., Jiang, J., He, K., Wolfe, M.S., Black, R.A., Frank, S.J. gamma-Secretase-mediated growth hormone receptor proteolysis: mapping of the intramembranous cleavage site. Bioch. Biophys. Res. Comm. 408(3): 432-436, 2011  21514282 
Xu, J., Zhang, Y., Berry, P.A., Jiang, J., Lobie, P.E., Langenheim J.F., Chen, W.Y., Frank, S.J. Growth hormone signaling in human T47D breast cancer cells: potential role for a growth hormone receptor-prolactin receptor complex. Mol. Endocrinol. 25(4): 597-610, 2011.  21310852 
Li, X., Huang, Y., Jiang, J., Frank, S.J. Synergy in ERK activation by cytokine receptors and tyrosine kinase growth factor receptors. Cellular Signalling, 23(2):417-424, 2011.  20946955 
Mavalli, M.D., DiGirolamo, D.J., Riddle, R.C., Fan, Y., Campbell, K.S., Sperling, M.A., van Groen, T., Frank, S.J., Bamman, M.M., Clemens, T.L. Distinct growth hormone receptor signaling modes control skeletal muscle development and insulin sensitivity. J. Clin. Invest., 120(11): 4007-4020, 2010.   20921627 
Gan, Y., Zhang, Y., DiGirolamo, D., Jiang, J., Wang, X., Cao, X., Zinn, K.R., Carbone, D.P., Clemens, T.L., Frank, S.J. Deletion of Insulin-like Growth Factor-1 Receptor (IGF-1R) in primary osteoblasts reduces GH-induced STAT5 signaling. Mol. Endocrinol. 24(3): 644-656, 2010.   20133448 
Yang, N., Jiang, J., Deng, L., Waters, M.J., Wang, X., Frank, S.J. Growth hormone receptor targeting to lipid rafts requires extracellular subdomain 2. Bioch. Biophys. Res. Comm., 391(1): 414-418, 2010.   19914217 
Wang, X., Yang, N., Deng, L., Li, X., Jiang, J., Gan, Y., Frank, S.J. Interruption of growth hormone signaling via SHC and ERK in 3T3-F442A preadipocytes upon knockdown of insulin receptor substrate-1. Mol. Endocrinol. 23(4): 486-496, 2009.   19164446 
Li, X., Huang, Y., Jiang, J., Frank, S.J. ERK-mediated threonine phosphorylation of EGF receptor: impact on receptor downregulation and signaling. Cellular Signalling, 20(11):2145-2155, 2008.  18762250 
Wang, X., Jiang, J., Warram, J., Baumann, G., Gan, Y., Menon, R.K., Denson, L.A., Zinn, K.R., Frank, S.J. Endotoxin-induced proteolytic reduction in hepatic growth hormone (GH) receptor: a novel mechanism for GH insensitivity. Mol. Endocrinol., 22(6):1427-1437, 2008.  18323468 
Frank, S.J. Mechanistic Aspects of Crosstalk Between GH and PRL and ErbB Receptor Family Signaling. J Mammary Gland Biol Neoplasia 13(1):119-29, 2008  18236142 
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Keywords
growth hormone, signaling, prolactin, IGF-1, growth factors

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