Lisa A. Elferink, Ph.D.

301 University Blvd.

Galveston, TX 77555-1069

laelferi@utmb.edu

 

Affiliations

Associate Professor,  

Department of Physiology and Biophysics

Member, Marine Biomedical Institute

 

 

Education

B.Sc. (Biochemistry, Physiology, Pharmacology), University of Adelaide, Australia, 1981

Ph.D. (Biochemistry) University of Adelaide, Australia, 1988

Postdoctoral, Stanford University, CA

 

Graduate Program Affiliations

Associate Member, Cell Biology Graduate Program

Associate Member, Human Biological Chemistry & Genetics Graduate Program

Associate Member, Neurosciences Graduate Program

 

 

 

 

Employment Opportunities in laboratory

 

Research Interests

Trafficking and Receptor  Signaling

Our research program focuses on understanding the molecular and cellular mechanisms linking membrane trafficking with receptor- signaling.  Membrane trafficking is important for normal neural and cell function, including neurotransmitter release, neurite extension, cell migration and invasion during normal development or migration, and pathogen entry by phagocytosis. Recent studies have shown a requirement for early endocytic trafficking in ligand-activated receptor signaling.  Using a combination of molecular (e.g. mutagenesis), genetic (yeast-two hybrid), biochemical (protein-protein interactions) and cellular (recombinant viruses, confocal microscopy and digital imaging) approaches, we are examining functionally important protein-protein interactions for trafficking through early endosomes and how they regulate the signaling properties of receptor-tyrosine kinases.  Understanding these processes is critical for defining how the endocytic trafficking of receptor tyrosine kinases regulates normal cell function.  Our goal is to identify novel targets for drug development aimed at treating human diseases involving aberrant receptor signaling in vivo.

 

Selected Publications

Cohen, R., Elferink, L.A.,  and Atlas, D. (2003) The C2A domain of synaptogamin alters the kinetics of voltage-gated Ca2+ channels Cav1.2 and Cav2.3. J. Biol. Chem. 278:9258-66.

 Strick, D.J., Francescutti, D.M., Zhao, Y., and Elferink, L.A. (2002).  Mammalian suppressor of Sec4 modulates the inhibitory effect of rab15 during early endocytosis.  J. Biol. Chem, 277, 32722-32729.

Xu, W., Shy, M., Kamholtz, J., Elferink, L.A., Lilien, J., and Balsamo, J. (2001). Mutations in the cytoplasmic domain of PO reveal a role for PKC-mediated phosphorylation in adhesion and myelination. J. Cell Biol.  155, 439-446.

Zuk, P., and Elferink, L. A. (2000) Rab15 differentially regulates early endocytic trafficking. J. Biol. Chem. 275, 26754-26764.

Zuk, P., and Elferink, L. A. (1999)Rab15 mediates an early endocytic event in Chinese Hamster Ovary cells. J. Biol. Chem.274, 22303-22312.

Thomas, D.M., Ferguson, G.D., Herschman, H. R., and Elferink, L.A. (1999) Functional and biochemical analysis of the C2 domain of Synaptotagmin IV. Mol. Biol. Cell.10, 2285-2295.

Ferguson, G. D., Thomas, D. M.,Elferink, L.A., and Herschman, H. R. (1999) Synthesis, degradation and subcellular localization of synaptotagmin IV, a neuronalimmediate early gene product.  J. Neurochem. 72, 1821-1831.

Thomas, D.M., and Elferink, L.A. (1998) Functional Analysis of the C2A Domain of Synaptotagmin 1:Implications for Calcium Regulated Secretion. J. Neurosci.18, 3511-3520.

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Last updated: 09/23/04