Ph.D. Johns Hopkins University. Neuroscience.
B.S. Oakland University. Biochemistry.
In the laboratory of David D. Ginty, his doctoral research investigated the ability of Nerve Growth Factor, a potent survival factor for sensory and sympathetic neurons, to support neuronal function when only activating receptors on axon terminals. His work on “retrograde” NGF signaling influenced the most widely accepted view of the field, namely that stable ligand-receptor complexes are trafficked in neurons over long distances to regulate biochemical events in the cell body necessary for survival, growth, and differentiation. Dr. Pierchala completed his postdoctoral training in the laboratory of Eugene M. Johnson, Jr. at Washington University School of Medicine in Saint Louis. There he investigated a newly discovered family of neuronal growth factors, the Glial Cell Line-derived Neurotrophic Factor (GDNF) Family Ligands (GFLs). He continued his investigation of GDNF signal transduction as an Assistant Professor at the State University of New York at Buffalo prior to his arrival to the Department of Biologic and Materials Sciences. His laboratory investigates the mechanisms of action of the GFLs in the development and maintenance of the nervous system and kidneys, as well as the therapeutic potential of the GFLs for injuries and diseases of the nervous system.
C.C. Tsui, N.A. Gabreski, S.J. Hein and B.A. Pierchala. 2014. Lipid rafts are physiologic membrane microdomains necessary for the morphogenic and developmental functions of GDNF in vivo. J. Neurosci. In press.
G.N. Calco, O.R. Stephens, L.M. Donahue, C.C. Tsui and B.A. Pierchala. 2014. CD-associated protein (CD2AP) enhances Casitas B Lineage Lymphoma-3/c (Cbl-3/c)-mediated Ret isoform-specific ubiquitination and degradation via its amino-terminal Src Homology 3 domains. J. Biol. Chem. 289: 7307-7319.
J.P. Frampton, C. Guo and B.A. Pierchala. 2012. Expression of axonal protein degradation machinery in sympathetic neurons is regulated by nerve growth factor. J. Neurosci. Res. 90: 1533-1546.
D. Bonanomi, O. Chivatakarn, G. Bai, H. Abdesselem, K. Lettieri, T. Marquardt, B.A. Pierchala and S.L. Pfaff. 2012. Ret is a multifunctional coreceptor that integrates diffusible- and contact-axon guidance signals. Cell. 148: 568-582.
C.C. Tsui and B.A. Pierchala. 2010. The differential axonal degradation of Ret accounts for cell type-specific function of Glial Cell Line-Derived Neurotrophic Factor as a retrograde survival factor. J. Neurosci. 30: 5149-5158.
B.A. Pierchala, M.R. Munoz and C.C. Tsui. 2010. Proteomic analysis of the slit diaphragm complex: CLIC5 is a protein critical for podocyte morphology and function. Kidney Intl. In press.
C.C. Tsui and B.A. Pierchala. 2008. CD2AP and Cbl-3/Cbl-c constitute a critical checkpoint in the regulation of Ret signal transduction. J. Neurosci. 28: 8789-8800.
B.A. Pierchala, C.C. Tsui, J. Milbrandt, and E.M. Johnson, Jr. 2007. NGF augments the autophosphorylation of Ret via inhibition of ubiquitin-dependent degradation. J. Neurochem. 100, 1169-1176
C.C. Tsui, S.J. Shankland, B.A. Pierchala. 2006. Glial cell line-derived neurotrophic factor and its receptor Ret is a novel ligand-receptor complex critical for survival response during podocyte injury. JASN. 17, 1543-1552.
B.A. Pierchala, J. Milbrandt, and E.M. Johnson, Jr. 2006. Glial cell line-derived neurotrophic factor-dependent recruitment of Ret into lipid rafts enhances signaling by partitioning Ret from proteasome-dependent degradation. J. Neurosci. 26: 2777-2787