James Monypenny

TL;DR: It is provided the first evidence that PKCα or a PKC α‐associated serine/threonine kinase can phosphorylate the ERM C‐terminal threonine residue within a kinase–ezrin molecular complex in vivo.

TL;DR: Single-molecule imaging revealed fast directional movement of mDia1 FH1-FH2 for tens of microns in living cells and suggested that mDIA1 probably moves processively along the growing end of actin filaments in cells, and Formins may be a molecular motility machinery that is independent from motor proteins.

TL;DR: The Rho-mDia1 pathway regulates polarization and adhesion turnover by aligning microtubules and actin filaments and delivering Apc/Cdc42 and c-Src to their respective sites of action.

TL;DR: Transformed rat fibroblasts expressing two variants of green fluorescent protein, each fused to β-actin, were used to study actin dynamics during cell protrusion and found that actin was delivered to protruding zones of the leading edge of the cell at speeds that exceeded 5 micrometers per second.

TL;DR: The data presented here demonstrate the localization of interactions by using multiphoton time-domain fluorescence lifetime imaging microscopy (FLIM) and establish that activated Cdc42 interacts withPAK1 in a nucleotide-dependent manner in the cell periphery, leading to Thr-423 phosphorylation of PAK1, particularly along the lengths of cell protrusion structures.