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Activación del receptor alostérico por la hormona péptida vegetal fitosulfokina

Jizong Wang¹, Hongju Li², Zhifu Han¹

¹Ministry of Education Key Laboratory of Protein Science, Center for Structural Biology, School of Life Sciences, Tsinghua-Peking Joint Center for Life Sciences, Tsinghua University, Beijing 100084, China.

|August 27, 2015

Resumen

El reconocimiento de la hormona vegetal de la fitosulfoquina (PSK) por su receptor (PSKR) implica cambios estructurales. La unión de PSK estabiliza el receptor, promoviendo la interacción con los co-receptores para la regulación del crecimiento de las plantas.

Área de la Ciencia:

Biología molecular de las plantas
Biología estructural
La bioquímica

Sus antecedentes:

La fitosulfoquina (PSK) es una hormona peptídica crucial que regula el crecimiento y el desarrollo de las plantas.
La PSK ejerce su función al unirse a su receptor, el receptor de fitosulfoquinas (PSKR), una quinasa receptora de repetición rica en leucina (LRR-RK).
Los mecanismos precisos de la percepción de PSK, la activación de PSKR y la señalización descendente siguen siendo en gran medida desconocidos.

Objetivo del estudio:

Para aclarar la base estructural del reconocimiento de Phytosulfokine (PSK) por su receptor, Phytosulfokine Receptor (PSKR).
Comprender el mecanismo de activación alostérica de la PSKR tras la unión de la PSK.
Identificar el papel de los co-receptores en la señalización mediada por PSK.

Principales métodos:

Se utilizó la cristalografía de rayos X para determinar las estructuras del dominio LRR extracelular de PSKR en varios estados (libre, ligado a PSK, ligado al co-receptor).
Se emplearon análisis bioquímicos y genéticos para validar los hallazgos estructurales e investigar las interacciones proteicas.
Los datos estructurales se combinaron con pruebas bioquímicas y genéticas para mapear las interfaces de interacción y las consecuencias funcionales.

Principales resultados:

Las estructuras cristalinas revelan que PSK se une a una hebra β dentro del dominio de la isla PSKR, formando una hoja anti-β.
Los grupos sulfatados de PSK interactúan directamente con PSKR, mejorando el reconocimiento del ligando.
La unión de PSK promueve la heterodimerización de PSKR con las quinasas similares a los receptores de embriogénesis somática (SERK) mediante la estabilización del dominio de la isla PSKR para el reclutamiento de SERK.

Conclusiones:

El estudio proporciona la base estructural de cómo el PSKR reconoce el PSK y se somete a la activación alostérica.
La unión al PSK modula alostericamente la PSKR, facilitando la interacción con el co-receptor sin participar directamente en ella.
Estos hallazgos allanan el camino para el diseño de pequeñas moléculas específicas para modular la actividad de PSKR para aplicaciones agrícolas.

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