posted on 2012-10-24, 08:58authored byDavid R. Critchley, Alexandre R. Gingras
Cell migration, growth and differentiation
all require the assembly and disassembly of
cellular junctions with the extracellular
matrix (ECM). These large multiprotein
complexes assemble around the integrin
family of cell adhesion molecules
(transmembrane αβ heterodimers) that are
typically linked to the actin cytoskeleton,
with the exception of integrin α6β4, which
is coupled to intermediate filaments.
Talin is one of several proteins that link the
cytoplasmic domains of integrin β subunits
to actin filaments (others include α-actinin,
filamin, tensin, integrin-linked kinase,
melusin and skelemin) (Critchley, 2004;
Nayal et al., 2004). Moreover, binding of
talin to β-integrin cytoplasmic domains
triggers a conformational change in the
αβ-integrin extracellular domain that
increases its affinity for ECM proteins
(Calderwood, 2004) and promotes the
assembly of focal adhesions (FAs), cellECM
junctions that are formed by cells
in culture. However, studies in flies
expressing mutant integrin alleles show
that there is not a simple 1:1 relationship
between integrins and talin in cell-ECM
junctions, and there must be additional
mechanisms that recruit talin to these sites
(Devenport et al., 2007).
Funding
D.R.C. is supported by the Wellcome Trust, Cancer
Research UK and the NIH Cell Migration Consortium
Grant U54 GM64346 from the National Institute of
General Medical Sciences (NIGMS).
History
Citation
Journal of Cell Science, 2008, 121 (Pt 9), pp. 1345-1347