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Title

Structural and functional analysis of LIM domain-dependent recruitment of paxillin to αvβ3 integrin-positive focal adhesions

Authors
Azizi, Latifeh
Bouvard, Daniel
Hytönen, Vesa P
Published in Communications biology. 2021, vol. 4, no. 1, 380
Abstract The LIM domain-dependent localization of the adapter protein paxillin to β3 integrin-positive focal adhesions (FAs) is not mechanistically understood. Here, by combining molecular biology, photoactivation and FA-isolation experiments, we demonstrate specific contributions of each LIM domain of paxillin and reveal multiple paxillin interactions in adhesion-complexes. Mutation of β3 integrin at a putative paxillin binding site (β3VE/YA) leads to rapidly inward-sliding FAs, correlating with actin retrograde flow and enhanced paxillin dissociation kinetics. Induced mechanical coupling of paxillin to β3VE/YA integrin arrests the FA-sliding, thereby disclosing an essential structural function of paxillin for the maturation of β3 integrin/talin clusters. Moreover, bimolecular fluorescence complementation unveils the spatial orientation of the paxillin LIM-array, juxtaposing the positive LIM4 to the plasma membrane and the β3 integrin-tail, while in vitro binding assays point to LIM1 and/or LIM2 interaction with talin-head domain. These data provide structural insights into the molecular organization of β3 integrin-FAs.
Identifiers
PMID: 33782527
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Structures
Research group Migration cellulaire (645)
Projects
FNS: 31003A_166384
FNS: 310030_185261
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(ISO format)
RIPAMONTI, Marta et al. Structural and functional analysis of LIM domain-dependent recruitment of paxillin to αvβ3 integrin-positive focal adhesions. In: Communications Biology, 2021, vol. 4, n° 1, p. 380. doi: 10.1038/s42003-021-01886-9 https://archive-ouverte.unige.ch/unige:153894

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Deposited on : 2021-08-17

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