Principal Research Interests
As one of the most abundant proteins in the cell, actin participates in many important cellular processes including cell motility, maintenance of cell shape, cell division, and muscle
contraction. Coordination of these diverse cellular processes therefore requires responsive regulation of actin. Currently over 150 actin-binding proteins have been identified which influence
localization, polymerization dynamics, crosslinking, and organization of actin.
- Structure-function relationships
- Application of high-field NMR to study protein-protein interactions and dynamics
- Regulation of actin cytoskeleton
Palladin is a recently identified protein from a novel family of actin binding proteins that has emerged as a key player in organizing actin arrays within migrating cells. Palladin family
members utilize immunoglobulin-like (Ig) domains to bind and crosslink actin, highlighting a new role for Ig domains. Our preliminary results suggest yet another novel role for palladin
that may include both promoting actin polymerization and/or modifying the structure of actin filaments.
Current research interests in the Beck group are to investigate the mechanisms by which palladin, through both direct and indirect molecular mechanisms, affects actin dynamics.
Specifically, we will use biochemical and cell biological approaches, coupled with protein structural studies to elucidate the role and mechanisms for how the novel, actin crosslinking
protein palladin influences the actin cytoskeleton. We intend to elucidate in detail the biochemical mechanisms of actin regulation and organization using kinetic assays of actin
polymerization coupled with studies of protein-protein interactions via NMR.
Beck MR, DeKoster GT, Cistola DP, Goldman WE (2009) NMR structure of a fungal virulence factor reveals structural homology with mammalian saposin B. Mol. Micro. 72(2):
344-53. *Selected by Biology Faculty of 1000 as a "Must Read."
Beck MR, DeKoster GT, Hambly DM, Gross ML, Cistola DP, Goldman WE (2008) Structural features responsible for biological stability of Histoplasma's virulence factor CBP.
Biochemistry 47: 4427-4438.
Beck MR, Morgan EA, Strand SS, Woolsey TA (2006) Volunteers bring passion to science outreach. Science 314:1246-1247.
- Yeo HJ, Yuan Q, Beck MR, Baron C, Waksman G (2003) Structural and functional characterization of the VirB5 protein from the type IV secretion system encoded by the conjugative
plasmid pKM101. PNAS 100:15947-15952.