Shelley Halpain

Research

Dr. Halpain’s research concerns the molecular basis for neural development. Her laboratory uses advanced light microscopy and quantitative cellular imaging methods to investigate neurite outgrowth and synapse formation. The lab also develops automated, high-content screening assays of neuronal morphology for use in drug discovery and identification of novel signaling pathways. Proteomics analyses are used to investigate key players in neuritogenesis. A particular focus is the role that cytoskeletal proteins, especially microtubules and actin filaments, play in establishing and maintaining neuronal networks. The laboraotory’s work is fundamentally relevant to many brain disorders, ranging from Alzheimer’s disease to mood disorders and autism.

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Publications

  • Dehmelt, L., Smart, F., Ozer, R., and Halpain, S. (2003) The role of MAP2c in the reorganization of microtubules and lamellipodia during neurite initiation, J. Neuroscienc, 23:9479-9490.
  • Roger, B., Al-Bassam, J., Dehmelt, L., Milligan, R., and Halpain, S. (2004) MAP2c, but not tau, binds and bundles F-actin via its microtubule binding domain. Current Biology 14:363-371.
  • Calabrese, B. and Halpain, S. (2005) Essential role for the PKC target MARCKS in maintaining dendritic spine morphology. Neuron 48:77-90.
  • Calabrese, B., Wilson, M., and Halpain, S. (2006) Development and regulation of dendritic spine synapses. Physiology 21:38-47.
  • Dehmelt, L., Nalbant, P., Steffan, W., and Halpain, S. (2006) A microtubule-based, dynein-dependent force induces local cell protrusions: implications for neurite initiation. Brain Cell Biology 35:43-60.
  • Al-Bassam, J., Roger, B., Halpain, S., and Milligan, R.A. (2007) Analysis of the weak interactions of ADP-Unc104 and ADP-Kinesin with microtubules and their inhibition by MAP2c. Cell Motil. Cytoskeleton 64(5):377-389.
  • Calabrese, B., Shaked, G.M., Tabarean IV, Braga, J., Koo, E.H., and Halpain, S. (2007) Rapid, concurrent alterations in pre- and postsynaptic structure induced by naturally-secreted amyloid-beta protein. Molecular Cell Neuroscience 35:183-193.