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Lisa A. Elferink, Ph.D.
Department of Neuroscience and Cell Biology
Edna Seinsheimer Levin Endowed Professorship in Cancer Studies
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.
Thomas DM, Elferink LA. Functional Analysis of the C2A Domain of Synaptotagmin
1:Implications for Calcium Regulated Secretion. J Neurosci 18:3511-3520, 1998.
Zuk P, Elferink LA. Rab15 mediates an early endocytic event in Chinese hamster
ovary cells. J Biol Chem 274:22303-22312, 1999.
Thomas DM, Ferguson GD, Herschman HR, Elferink LA. Functional and biochemical
analysis of the C2 domain of Synaptotagmin IV. Mol Biol Cell 10:2285-2295, 1999.
Ferguson GD, Thomas DM, Elferink LA, Herschman HR. Synthesis, degradation and
subcellular localization of synaptotagmin IV, a neuronalimmediate early gene product. J
Neurochem 72:1821-1831, 1999.
Zuk P, Elferink LA. Rab15 differentially regulates early endocytic trafficking. J
Biol Chem 275:26754-26764, 2000.
Xu W, Shy M, Kamholtz J, Elferink LA, Lilien J, Balsamo J. Mutations in the
cytoplasmic domain of PO reveal a role for PKC-mediated phosphorylation in adhesion and
myelination. J Cell Biol 155:439-446, 2001.
Strick DJ, Francescutti DM, Zhao Y, Elferink LA. Mammalian suppressor of Sec4
modulates the inhibitory effect of rab15 during early endocytosis. J Biol Chem 277:32722-32729,
Cohen R, Elferink LA, Atlas D. The C2A domain of synaptogamin alters the kinetics of
voltage-gated Ca2+ channels Cav1.2 and Cav2.3. J Biol Chem