As long there are cells and fascinated scientists, then there will always be unsolved mysteries. A recent paper helps clear up discrepancies in the actin literature, using a combination of killer microscopy and a systematic look at how one protein functions.
So many cellular processes depend on a dynamic network of actin filaments, and there is a long list of proteins that associate with and regulate these networks. One of those proteins is called VASP and is found at the leading edge of migrating cells in lamellipodia and filopodia. Recent work clarifies the different modes of VASP-actin filament binding and describes the mechanism by which VASP functions in actin filament assembly. Images show stabilized actin filaments (middle, green in merged) and single tetramers of VASP (top, orange in merged) bound to the side of these filaments.
BONUS!! Cool movies from the paper can be found here.
Hansen, S., & Mullins, R. (2010). VASP is a processive actin polymerase that requires monomeric actin for barbed end association The Journal of Cell Biology, 191 (3), 571-584 DOI: 10.1083/jcb.201003014
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