Las enzimas Ubp2 y Rsp5 controlan la actividad de receptores de proteasomas

Todas las células eucariotas tienen un sistema para destruir las proteínas defectuosas o las que, tras ser usadas, ya no son necesarias, pero aún se sabe muy poco sobre cómo funciona.

El equipo de Bernat Crosas, del Consejo Superior de Investigaciones Científicas, en Madrid, ha hallado un mecanismo por el que se regularía: dos enzimas, Rsp5 y Ubp2, activan o desactivan la actividad del proteasoma, el complejo multiproteico encargado de destruir las proteínas.

Los resultados del trabajo, que se publican en el último número de Molecular Cell, permitirán entender cómo se regula el equilibrio celular y la génesis de algunos tipos de cáncer y neurodegeneraciones.

En la destrucción de proteínas hay dos actores principales: los proteasomas y la ubicuitina. Éstas son reconocidas entonces por alguno de los receptores del proteasoma y, tras retirar la ubicuitina, son degradadas y sus restos expulsados para ser utilizados en otras funciones celulares. “Si este mecanismo destructor falla, se acumulan en el interior de la célula muchas proteínas que deberían ser eliminadas, la célula se colapsa y puede desarrollar múltiples patologías”, ha explicado Bernat Crosas.

Mediante el estudio de células de levadura, han descubierto que dos enzimas, Ubp2 y Rsp5, son responsables de abrir y bloquear respectivamente uno de los receptores del proteasoma, el Rpn10.

Se creía que la ubicuitina sólo interactuaba con el proteasoma mediante las cadenas de varias moléculas que marcan las proteínas a eliminar, pero no de forma monomérica.

Desregulación
“Se trata de un sistema de regulación muy fino, por lo que cualquier alteración en las funciones de Rsp5 o Ubp2 puede conducir a una desregulación de los proteasomas, lo cual afecta a una gran cantidad de vías celulares que necesitan de ellos para reciclar sus componentes; de ahí la amplia conexión con patologías moleculares”.

Se cree que algunas enfermedades neurodegenerativas caracterizadas por una acumulación anómala de proteínas que no se degradan podrían estar relacionadas con una disminución de la actividad de los proteasomas. Un ejemplo es el Alzheimer, caracterizado por la formación de agregados de proteína amiloide. La investigación del proteasoma es también una línea puntera en el tratamiento de algunos cánceres y se sabe además que algunos tipos de cáncer interfieren sobre la actividad del proteasoma.

Además, en condiciones de estrés ambiental los Rnp10 tienen un menor nivel de bloqueo. Por eso es esperable que haya más proteínas dañadas.

Fuente: www.diariomedico.com

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