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First published online September 19, 2007


Journal of Cell Science 120, 1902e (2007)
© The Company of Biologists Limited
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In this issue

mDia2 – the lamella's formin'


Figure 1

Cell migration relies on the dynamics of two overlapping F-actin networks – one at the edge of the cell (the lamellipodium) and one a few micrometers below the surface (the lamella). Actin-associated proteins regulate both these networks. On p. 3475, Clare Waterman-Storer and colleagues show that one such protein, mammalian Diaphanous-related formin (mDia2), a key nucleator of actin filaments, is crucial for regulating several aspects of F-actin dynamics in the epithelial cell lamella. Studying live cells, they show that mDia2 associates with the actin network in the lamella – but not the lamellipodium. They have blocked mDia2-mediated actin polymerisation by using antibodies or dominant negative constructs and followed the dynamics of F-actin by quantitative fluorescent speckle microscopy (which tracks randomly incorporated fluorescently tagged actin within a polymer). They find that mDia2 affects the stability and organisation of the lamella and is needed to maintain a stable pool of polymerization-competent F-actin filaments at focal adhesions (the structures that link the actin network to the substrate). Interestingly, mDia2 affects the kinetics of F-actin in both the lamella and lamellipodium; mDia2 at focal adhesions might thus somehow regulate the differential polymerisation of these two networks.


Related articles in JCS:

mDia2 regulates actin and focal adhesion dynamics and organization in the lamella for efficient epithelial cell migration
Stephanie L. Gupton, Kathryn Eisenmann, Arthur S. Alberts, and Clare M. Waterman-Storer
JCS 2007 120: 3475-3487. [Abstract] [Full Text]  




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