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Mol Biol Cell. 2010 Dec;21(23):4108-19. doi: 10.1091/mbc.E10-07-0580. Epub 2010 Oct 6.

β1A integrin is a master regulator of invadosome organization and function.

Author information

1
Institut Albert Bonniot, Université Joseph Fourier, Centre National de la Recherche Scientifique, and Institute National de la Santé et de la Recherche Médicale-Université Joseph Fourier U823 Site Santé BP 170, Grenoble 38042, Cedex 9, France.

Abstract

Invadosomes are adhesion structures involved in tissue invasion that are characterized by an intense actin polymerization-depolymerization associated with β1 and β3 integrins and coupled to extracellular matrix (ECM) degradation activity. We induced the formation of invadosomes by expressing the constitutive active form of Src, SrcYF, in different cell types. Use of ECM surfaces micropatterned at the subcellular scale clearly showed that in mesenchymal cells, integrin signaling controls invadosome activity. Using β1⁻/⁻ or β3⁻/⁻ cells, it seemed that β1A but not β3 integrins are essential for initiation of invadosome formation. Protein kinase C activity was shown to regulate autoassembly of invadosomes into a ring-like metastructure (rosette), probably by phosphorylation of Ser785 on the β1A tail. Moreover, our study clearly showed that β1A links actin dynamics and ECM degradation in invadosomes. Finally, a new strategy based on fusion of the photosensitizer KillerRed to the β1A cytoplasmic domain allowed specific and immediate loss of function of β1A, resulting in disorganization and disassembly of invadosomes and formation of focal adhesions.

PMID:
20926684
PMCID:
PMC2993740
DOI:
10.1091/mbc.E10-07-0580
[Indexed for MEDLINE]
Free PMC Article

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