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The Abrams
laboratory is focused on phospholipid signaling in hematopoietic cells.
Ongoing projects are directed at understanding the roles of pleckstrin
and lipid kinases in platelets and leukocytes. Pleckstrin (p47) was once
solely known as an early marker of platelet activation; more recently
it has been noted to contain the prototypic Pleckstrin Homology motif.
Over the past half dozen years, work derived from our laboratory has demonstrated
that pleckstrin plays a dominant role in the reorganization of the platelet,
and lymphocyte, cytoskeleton. Furthermore, the laboratory has established
these effects are regulated by pleckstrin phosphorylation, require critical
lipid-binding residues contained with the amino-terminal Pleckstrin Homology
domain, and have implicated an effector for this process to be the small
GTP-binding protein, Rac. It has also cloned a ubiquitously expressed
paralog, pleckstrin 2, although its mechanism of regulation is unknown.
Additional work from the Abrams laboratory has helped define the role
of phospholipid kinases in the pathway that is initiated by G-protein
coupled, and T-cell, receptors and ultimately leads to actin reorganization.
These studies use molecular and cellular biologic techniques to examine
blood cell biology, and involve expression mutagenesis, single cell microinjection,
genetic library screening, and murine homologous gene targeting ("gene
knock-out"). Selected Publications: Abrams, C.S.
and M.A. Lemmon (2002) Pleckstrin homology domains and the cytoskeleton.
FEBS Letters 513:71-79. |
