Faculty Detail   
Name WILLIS ANNE BURTON THEIBERT
  
Campus Address SHEL 910 Zip 2182
Phone  (205) 934-7278
E-mail  theibert@nrc.uab.edu
Other websites
    

Faculty Appointment(s)
Appointment Type Department Division Rank
Primary  Neurobiology  Neurobiology Professor
Secondary  Cell, Developmntl, & Integrative Biology  Cell, Developmntl, & Integrative Biology Professor
Center  Cell Adhesion & Matrix Research Center  Cell Adhesion & Matrix Research Center Professor
Center  Civitan International Research Center  Civitan International Research Center Professor
Center  Comprehensive Neuroscience Center  Comprehensive Neuroscience Center Professor
Center  Med - Cardiovascular Disease  Ctr Cardiovasc Bio (Org Ret) Professor
Center  Ctr for Glial Bio in Med  Ctr for Glial Bio in Med Professor
Center  GL Ctr for Craniofacial, Oral, & Dental Disorders  GL Ctr for Craniofacial, Oral, & Dental Disorders Professor

Graduate Biomedical Sciences Affiliations
Cell, Molecular, & Developmental Biology 
Medical Scientist Training Program 

Biographical Sketch 
Anne Theibert received her Ph.D. from The Johns Hopkins University School of Medicine in 1985. She is an Associate Professor of Neurobiology, and Adjunct Assistant Professor of Cell Biology and Physiology and Biophysics.

Research/Clinical Interest
Title
Role of phosphoinositides in developmental neurobiology
Description
Many diseases are linked to dysregulation of second messenger signaling cascades. One important second messenger system is the phosphoinositide (PI) system, in which inositol lipids function as second messengers and cofactors for many cellular activities stimulated by growth and trophic factors, hormones, cytokines, and neurotransmitters. My research focuses on investigating the intracellular targets for several of the PI second messengers in the nervous system. We are particularly interested in the function of PtdInsP3 in neurons and glia, since we have demonstrated that this lipid is required for cells to extend processes, termed neurites, in response to trophic factors and extracellular matrix. Neurites eventually form mature axons and dendrites, which contact each other at synapses, and allow for information transfer between neurons. Using biochemical and molecular techniques, we have isolated and cloned several novel phosphoinositide receptors from brain. One of these receptors is involved in regulating vesicle trafficking and the actin cytoskeleton, two activities which are involved in neurite outgrowth and new synapse formation. Studies are underway to determine the role of these receptors in neuronal development and synapse formation, and the molecular mechanisms which regulate receptor expression, targeting to intracellular compartments, and modulation of activity. Several potential homologues of these receptors are present in the genetically tractable organism, Saccharomyces cerevisiae, which allows us to use yeast genetics to complement the biochemical and molecular approaches in dissecting the function of these brain phosphoinositide receptors.

Selected Publications 
Sims, B., Powers, R.E., Sabina, R.L., Theibert, A.B. (1998) Elevated adenosine monophosphate deaminase activity in Alzheimer's disease brain. Neurobiol. Aging 19: 385-391.    
Zachor, D.A., Moore, J.F., Jin, J., Theibert, A.B., Percy, A.K. (1998) C-fos mediates cocaine inhibition of NGF-induced PC12 cell differentiation. Mol. Genet. Metab. 64: 62-69.   
Zachor, D.A., Moore, J.F., Theibert, A.B., Percy, A.K. (1998) Cocaine-inhibited neuronal differentiation in NGF-induced PC12 cells and altered c-fos expression are reversed by C-fos antisense oligonucleotide. Ann N Y Acad. Sci. 846: 427-430.   
Oh, E.S., Woods, A., Lim, S.T., Theibert, A.B., Couchman, J.R. (1998) Syndecan-4 proteoglycan cytoplasmic domain and phosphatidylinositol 4,5-bisphosphate coordinately regulate protein kinase C activity. J. Biol. Chem. 273: 10624-10629.   
Blader, I.J., Cope, M.J., Jackson, T.R., Profit, A.A., Greenwood, A.F., Drubin, D.G., Prestwich, G.D., Theibert, A.B. (1999) GCS1, an Arf guanosine triphosphatase-activating protein in Saccharomyces cerevisiae, is required for normal actin cytoskeletal organization in vivo and stimulates actin polymerization in vitro. Mol. Biol. Cell 10: 581-596.