| First Author | Destaing O | Year | 2010 |
| Journal | Mol Biol Cell | Volume | 21 |
| Issue | 23 | Pages | 4108-19 |
| PubMed ID | 20926684 | Mgi Jnum | J:182932 |
| Mgi Id | MGI:5317095 | Doi | 10.1091/mbc.E10-07-0580 |
| Citation | Destaing O, et al. (2010) beta1A integrin is a master regulator of invadosome organization and function. Mol Biol Cell 21(23):4108-19 |
| abstractText | Invadosomes are adhesion structures involved in tissue invasion that are characterized by an intense actin polymerization-depolymerization associated with beta1 and beta3 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 beta1/ or beta3/ cells, it seemed that beta1A but not beta3 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 beta1A tail. Moreover, our study clearly showed that beta1A links actin dynamics and ECM degradation in invadosomes. Finally, a new strategy based on fusion of the photosensitizer KillerRed to the beta1A cytoplasmic domain allowed specific and immediate loss of function of beta1A, resulting in disorganization and disassembly of invadosomes and formation of focal adhesions. |
