2013
DOI: 10.1091/mbc.e12-09-0695
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Two modes of integrin activation form a binary molecular switch in adhesion maturation

Abstract: Talin-mediated integrin activation drives integrin-based adhesions. A simple binary switch—vinculin competitively displacing RIAM from talin—is found to play a central role in the maturation and evolving functions of integrin-based adhesions.

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Cited by 68 publications
(84 citation statements)
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“…This additional mechanism fits well with the discovery of other IAPs that cooperate with talin to activate integrins, such as kindlins, although the mechanism is still unclear and kindlins also cluster integrins (Moser et al, 2009;Calderwood et al, 2013;Ye et al, 2013;Rognoni et al, 2016;Georgiadou et al, 2017). Additional IAPs enhancing talinmediated activation are RIAM (Han et al, 2006;Yang et al, 2014), zasp (also known as LDB3) (Bouaouina et al, 2012) and vinculin (Lee et al, 2013), whereas other IAPs compete with talin and reduce activation, including ICAP1 (also known as ITGB1BP1) (Bouvard et al, 2003), filamin A (Kiema et al, 2006) and moesin (Vitorino et al, 2015). Alternatively, SHANK proteins can sequester Rap1, reducing talin-mediated integrin activation .…”
Section: Talin In Integrin Activationsupporting
confidence: 79%
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“…This additional mechanism fits well with the discovery of other IAPs that cooperate with talin to activate integrins, such as kindlins, although the mechanism is still unclear and kindlins also cluster integrins (Moser et al, 2009;Calderwood et al, 2013;Ye et al, 2013;Rognoni et al, 2016;Georgiadou et al, 2017). Additional IAPs enhancing talinmediated activation are RIAM (Han et al, 2006;Yang et al, 2014), zasp (also known as LDB3) (Bouaouina et al, 2012) and vinculin (Lee et al, 2013), whereas other IAPs compete with talin and reduce activation, including ICAP1 (also known as ITGB1BP1) (Bouvard et al, 2003), filamin A (Kiema et al, 2006) and moesin (Vitorino et al, 2015). Alternatively, SHANK proteins can sequester Rap1, reducing talin-mediated integrin activation .…”
Section: Talin In Integrin Activationsupporting
confidence: 79%
“…2A; Goult et al, 2013b;Lee et al, 2013), which makes sense if it helps recruit talin to integrins. Thus, talin rod domains can function as switches, binding one protein in a folded state, and a different protein when unfolded by force.…”
Section: Box 2 Testing the Importance Of Inside-out Integrin Activatmentioning
confidence: 99%
“…Simultaneously, R3 unfolding leads to the recruitment of vinculin and strengthening of the connection to actin. This allows two different ligands to engage the same talin domain under different conditions and explains the different localisation of RIAM and vinculin in cells 100. In the case of R3, a force of ~ 5 pN is required for it to unfold, disrupting the RIAM‐binding sites and recruiting vinculin, driving the maturation of nascent adhesions into FAs.…”
Section: The Mechanical Properties Of Talinmentioning
confidence: 99%
“…The MRL-talin-integrin complex drives migratory protrusions RIAM is abundant at the cell edge and at the lamellipodium, where it promotes protrusion (48). Protrusive activity is likely due to the ability of RIAM to increase actin polymerization, most likely due to its interaction with profilin and Ena/VASP family proteins.…”
Section: Riam Is An Integral Part Of the Integrin Activation Machinerymentioning
confidence: 99%