Two-piconewton slip bond between fibronectin and the cytoskeleton depends on talin.

Guoying Jiang, Grégory Giannone, David R. Critchley, Emiko Fukumoto, Michael P. Sheetz
Nature. 2003-07-01; 424(6946): 334-337
DOI: 10.1038/nature01805

Read on PubMed

1. Nature. 2003 Jul 17;424(6946):334-7.

Two-piconewton slip bond between fibronectin and the cytoskeleton depends on

Jiang G(1), Giannone G, Critchley DR, Fukumoto E, Sheetz MP.

Author information:
(1)Department of Biological Sciences, Columbia University, 1212 Amsterdam Avenue,
New York, New York 11027, USA.

Mechanical forces on matrix-integrin-cytoskeleton linkages are crucial for cell
viability, morphology and organ function. The production of force depends on the
molecular connections from extracellular-matrix-integrin complexes to the
cytoskeleton. The minimal matrix complex causing integrin-cytoskeleton
connections is a trimer of fibronectin’s integrin-binding domain FNIII7-10 (ref.
4). Here we report a specific, molecular slip bond that was broken repeatedly by
a force of 2 pN at the cellular loading rate of 60 nm x s(-1); this occurred with
single trimer beads but not with monomer. Talin1, which binds to both integrins
and actin filaments in vitro, is required for the 2-pN slip bond and rapid
cytoskeleton binding. Further, inhibition of fibronectin binding to alpha(v)beta3
and deletion of beta3 markedly decreases the 2-pN force peak. We suggest that
talin1 initially forms a molecular slip bond between closely packed
fibronectin-integrin complexes and the actin cytoskeleton, which can apply a low
level of force to fibronectin until many bonds form or a signal is received to
activate a force response.

DOI: 10.1038/nature01805
PMID: 12867986 [Indexed for MEDLINE]

Know more about