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Contact-dependent Signaling

Contact-dependent signaling, as the name suggests, requires that communicating cells be in direct contact with each other. This is achieved either through receptor-ligand interactions or by specialized cytoplasmic channels that allow the flow of small molecules between cells. In animal cells, channels called gap junctions facilitate contact-dependent signaling in certain tissues, whereas, plasmodesmata perform a similar function in plants.
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Detection of Signaling Effector-Complexes Downstream of BMP4 Using in situ PLA, a Proximity Ligation Assay
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Published on: March 4, 2011

Bases estructurales de la señalización de las semáforinas-plexinas.

Bert J C Janssen1, Ross A Robinson, Francesc Pérez-Brangulí

  • 1Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford OX3 7BN, UK.

Nature
|September 30, 2010
PubMed
Resumen

La señalización celular semaphorin-plexin se basa en complejos 2:2 bivalentes. Este estudio revela la base estructural de las interacciones semaphorin-plexina, aclarando los mecanismos de señalización en el desarrollo y la enfermedad.

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Área de la Ciencia:

  • Biología Molecular Biología Molecular
  • Biología celular Biología celular.
  • Biología Estructural Biología estructural.

Sus antecedentes:

  • La comunicación célula-célula a través de los ligandos de semaphorina y los receptores de plexina es crucial para la homeostasis tisular, la morfogénesis, el desarrollo neuronal, el cáncer y las respuestas inmunes.
  • SEMA4D y Sema6A son semaforinas de vertebrados que envían señales a través de los receptores de plexina-B y plexina-A, respectivamente.
  • La base estructural de las interacciones semaphorina-plexina y la especificidad de la señalización de la plexina era desconocida anteriormente.

Objetivo del estudio:

  • Para dilucidar los mecanismos estructurales que subyacen a las interacciones y la señalización semaphorin-plexina.
  • Para determinar la especificidad extracelular y el mecanismo que controla la señalización de las plexinas.

Principales métodos:

  • La cristalografía de rayos X se utilizó para determinar las estructuras de los complejos semaphorin-plexin y componentes individuales.
  • Se emplearon ensayos biofísicos y celulares para investigar las consecuencias funcionales de estas interacciones.

Principales resultados:

  • Las estructuras cristalinas revelaron cómo los dímeros de semaphorina se unen a dos moléculas de plexina, formando un complejo bivalente 2:2 esencial para la señalización.
  • La semaforina monomérica que se une a la plexina no desencadena la señalización, lo que pone de relieve la importancia de la avidez.
  • Una arquitectura estructural conservada que involucra los dominios de unión a las semáforinas (beta-hélice de siete palas) media los modos de interacción comunes, mientras que las variaciones dictan la especificidad.

Conclusiones:

  • La señalización semaphorina-plexina se desencadena por la dimerización de la plexina estabilizada por semaphorina, potencialmente seguida por el agrupamiento.
  • Los hallazgos proporcionan un marco estructural para la comprensión de las interacciones semaphorin-plexina y sus roles en diversos procesos biológicos.
  • Los elementos estructurales conservados y variables explican tanto el mecanismo de señalización común como las especificidades observadas en diferentes pares de semaphorinas-plexinas.