Research
Thrusts
..... Nanostructures
..... Biomimetics
..... Bio-Nano
Daniel Purich - The lace-like cytoskeletal network is formed from supramolecular assemblages, including microtubules and the actin microfilaments which self-assemble from tubulin heterodimers and actin monomers, respectively. The cytoskeleton is an organelle that endows cells with the ability to attain and maintain their unique anisometry, to locomote, and to divide. We seek to understand the structural and dynamic properties of tubulin and actin that govern their basic assembly and disassembly processes. Much of our research is predicated on a long-term interest in learning how the tubulin GTPase and actin ATPase activities manage the free energy changes driving polymerization and depolymerization. We are also interested in the role(s) of microtubule-associated proteins (MAPs) as well as actin-regulatory
proteins in specifying cytoskeletal function.
- dGTP-MICROTUBULES IN NEURITES OF NGF-TREATED NEURONS --- We are exploring neuronal signal transduction mechanisms underlying the entry of 2'-deoxyGTP into neuritic microtubules after treating PC12 pheochromocytoma cells or embryonic chick dorsal ganglion neurons with nerve growth factor (NGF).
- REGULATION OF MAP-2 INTERACTIONS WITH MICROTUBULES-- Our group continues with its characterization of the interactions of brain-specific MAP-2 with microtubules. We are particularly interested in defining the action of signal transduction protein kinases in modulating MAP-2 binding to microtubules.
- MAP-2 POLYMERIZATION & NEUROFIBRILLARY TANGLES-- We recently discovered the polymerization of MAP-2 into filament structures resembling components of neurofibrillary tangles oberved in autopsy brain of patients with Alzheimer's Disease .
- ACTIN-BASED MOTILITY OF INTRACELLULAR PATHOGENS--- In collaboration with Professor Fred Southwick, we are examining actin- based motility of Listeria and Shigella to identify host cell components necessary for the intracellular locomotion of these microbial pathogens.