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Título

Kon-tiki enhances PS2 integrin adhesion and localizes its ligand, Thrombospondin, in the myotendinous junction

AutorPérez-Moreno, Juan J. ; Espina-Zambrano, Agueda G.; García-Calderón, Clara B.; Estrada, Beatriz
Palabras claveExtracellular matrix
Perdido
NG2
Myotendinous junction
Myogenesis
Muscle
Kon-tiki
Integrin
Chondroitin sulfate proteoglycan
CSPG4
Adhesion
Fecha de publicación2017
EditorCompany of Biologists
CitaciónJournal of Cell Science 130(5): 950-962 (2017)
ResumenCell-extracellular-matrix adhesion is mediated by cell receptors, mainly integrins and transmembrane proteoglycans, which can functionally interact. How these receptors are regulated and coordinated is largely unknown. We show that the conserved transmembrane Drosophila proteoglycan Kon-tiki (Kon, also known as Perdido) interacts with the αPS2βPS integrin (αPS2 is encoded by inflated and βPS by myospheroid) to mediate muscle-tendon adhesion. kon and inflated double mutant embryos show a synergistic increase in muscle detachment. Furthermore, Kon modulates αPS2βPS signaling at the muscle attachment, since phosphorylated Fak is reduced in kon mutants. This reduction in integrin signaling can be rescued by the expression of a truncated Kon protein containing its transmembrane and extracellular domains, suggesting that these domains are sufficient to mediate this signaling. We show that these domains are sufficient to properly localize the αPS2βPS ligand, Thrombospondin, to the muscle attachment, and to partially rescue Kon-dependent muscle-tendon adhesion.We propose that Kon can engage in a protein complex with αPS2βPS and enhance integrin-mediated signaling and adhesion by recruiting its ligand, which would increase integrin-binding affinity to the extracellular matrix, resulting in the consolidation of the myotendinous junction.
Versión del editorhttps://doi.org/10.1242/jcs.197459
URIhttp://hdl.handle.net/10261/163570
Identificadoresdoi: 10.1242/jcs.197459
e-issn: 1477-9137
issn: 0021-9533
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