RT Journal Article
T1 Kon-tiki enhances PS2 integrin adhesion and localizes its ligand, Thrombospondin, in the myotendinous junction.
A1 Pérez-Moreno, Juan J
A1 Espina-Zambrano, Agueda G
A1 García-Calderón, Clara B
A1 Estrada, Beatriz
K1 Adhesion
K1 CSPG4
K1 Chondroitin sulfate proteoglycan
K1 Extracellular matrix
K1 Integrin
K1 Kon-tiki
K1 Muscle
K1 Myogenesis
K1 Myotendinous junction
K1 NG2
K1 Perdido
AB Cell-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.
YR 2017
FD 2017-01-19
LK http://hdl.handle.net/10668/10792
UL http://hdl.handle.net/10668/10792
LA en
DS RISalud
RD Apr 12, 2025