Spire-1 contributes to the invadosome and its associated invasive properties.

Abstract : Cancer cells have an increased ability to squeeze through extracellular matrix gaps that they create by promoting proteolysis of its components. Major sites of degradation are specialized micro-domains in the plasma membrane collectively named invadosomes where the Arp2/3 complex and formin proteins cooperate to spatio-temporally control actin nucleation and the folding of a dynamic F-actin core. At invadosomes, proper coupling of exo-endocytosis allows polarized delivery of proteases that facilitate degradation of ECM and disruption of the cellular barrier. We investigated the contribution of the actin nucleator Spire-1 to invadosome structure and function, using Src-activated cells and cancer cells. We found that Spire-1 is specifically recruited at invadosomes and is part of a multi-molecular complex containing Src kinase, the formin mDia1 and actin. Spire-1 interacts with the Rab3A GTPase, a key player in the regulation of exocytosis that is present at invadosomes. Finally, over- and under-expression of Spire-1 resulted in cells with an increased or decreased potential for matrix degradation, respectively, therefore suggesting a functional interplay of Spire-1 with both actin nucleation and vesicular trafficking that might impact on cell invasive and metastatic behavior.
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Journal of Cell Science, Company of Biologists, 2014, 127 (Pt 2), pp.328-40. 〈10.1242/jcs.130161〉
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Vanessa Lagal, Marie Abrivard, Virginie Gonzalez, Audrey Perazzi, Sonam Popli, et al.. Spire-1 contributes to the invadosome and its associated invasive properties.. Journal of Cell Science, Company of Biologists, 2014, 127 (Pt 2), pp.328-40. 〈10.1242/jcs.130161〉. 〈inserm-01068991〉

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