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Gránulo de estrés

Dinámica de los gránulos de tensión

En la biología celular , los gránulos de estrés son condensados ​​biomoleculares en el citosol compuestos de proteínas y ARN que se ensamblan en orgánulos sin membrana de 0,1 a 2 μm cuando la célula está bajo estrés . [1] [2] Las moléculas de ARNm que se encuentran en los gránulos de estrés son complejos de preiniciación de traducción estancados asociados con subunidades ribosomales 40S, factores de iniciación de la traducción , ARNm poli(A)+ y proteínas de unión al ARN (RBP) . Si bien son orgánulos sin membrana, se ha propuesto que los gránulos de estrés están asociados con el retículo endoplasmático . [3] También hay gránulos de estrés nucleares . Este artículo trata sobre la variedad citosólica .

Funciones propuestas

La función de los gránulos de estrés sigue siendo en gran medida desconocida. Desde hace mucho tiempo se ha propuesto que estos gránulos tienen la función de proteger al ARN de condiciones nocivas, de ahí su aparición bajo estrés. [4] La acumulación de ARN en glóbulos densos podría evitar que reaccionen con sustancias químicas nocivas y salvaguardar la información codificada en su secuencia de ARN .

Los gránulos de estrés también podrían funcionar como un punto de decisión para el ARNm no traducido. Las moléculas pueden seguir uno de tres caminos: almacenamiento adicional, degradación o reinicio de la traducción . [5] Por el contrario, también se ha argumentado que los gránulos de estrés no son sitios importantes para el almacenamiento del ARNm ni sirven como ubicación intermedia para el ARNm en tránsito entre un estado de almacenamiento y un estado de degradación. [6]

Los esfuerzos para identificar todo el ARN dentro de los gránulos de estrés (el transcriptoma del gránulo de estrés ) de una manera imparcial mediante la secuenciación del ARN de los "núcleos" de gránulos de estrés purificados bioquímicamente han demostrado que el ARN no se recluta a los gránulos de estrés de una manera específica de la secuencia, sino más bien de manera genérica, enriqueciéndose las transcripciones más largas y/o traducidas de manera menos óptima. [7] Estos datos implican que el transcriptoma del gránulo de estrés está influenciado por la valencia del ARN (para proteínas u otro ARN) y por las tasas de salida del ARN de los polisomas . Esto último está respaldado además por estudios recientes de imágenes de moléculas individuales . [8] Además, se estimó que solo alrededor del 15% del ARNm total en la célula se localiza en los gránulos de estrés, [7] lo que sugiere que los gránulos de estrés solo influyen en una minoría del ARNm en la célula y pueden no ser tan importantes para el procesamiento del ARNm como se pensaba anteriormente. [7] [9] Dicho esto, estos estudios representan solo una instantánea en el tiempo, y es probable que una fracción mayor de ARNm se almacene en algún momento en gránulos de estrés debido a que el ARN entra y sale.

Las proteínas de estrés que son el componente principal de los gránulos de estrés en las células vegetales son chaperonas moleculares que secuestran, protegen y posiblemente reparan las proteínas que se despliegan durante el calor y otros tipos de estrés. [10] [11] Por lo tanto, cualquier asociación de ARNm con gránulos de estrés puede ser simplemente un efecto secundario de la asociación de proteínas de unión a ARN parcialmente desplegadas con gránulos de estrés, [12] similar a la asociación de ARNm con proteasomas . [13]

Formación

Los estresores ambientales desencadenan la señalización celular, lo que eventualmente conduce a la formación de gránulos de estrés. In vitro , estos estresores pueden incluir calor, frío, estrés oxidativo (arsenito de sodio), estrés del retículo endoplásmico ( tapsigargina ), inhibición del proteasoma ( MG132 ), estrés hiperosmótico , radiación ultravioleta , inhibición de eIF4A (pateamina A, hippuristanol o RocA ), acumulación de óxido nítrico después del tratamiento con 3-morfolinosidnonimina (SIN-1) , [14] perturbación del empalme del pre-ARNm , [15] y otros estresores, como la puromicina , que dan como resultado polisomas desensamblados . [16] Muchos de estos estresores dan como resultado la activación de quinasas asociadas al estrés particulares (HRI, PERK, PKR y GCN2), inhibición de la traducción y formación de gránulos de estrés. [16] Los gránulos de estrés también se formarán tras la activación de Gαq en un mecanismo que implica la liberación de proteínas asociadas a los gránulos de estrés de la población citosólica de la fosfolipasa C β efectora de Gαq. [17]

La formación de gránulos de estrés suele producirse después de la fosforilación activada por estrés del factor de iniciación de la traducción eucariota eIF2α ; esto no es válido para todos los tipos de estresores que inducen gránulos de estrés, [16] por ejemplo, la inhibición de eIF4A. Más adelante, la agregación similar a priones de la proteína TIA-1 promueve la formación de gránulos de estrés. El término similar a priones se utiliza porque la agregación de TIA-1 depende de la concentración , es inhibida por chaperonas y porque los agregados son resistentes a las proteasas . [18] También se ha propuesto que los microtúbulos desempeñan un papel en la formación de gránulos de estrés, tal vez al transportar componentes de los gránulos. Esta hipótesis se basa en el hecho de que la interrupción de los microtúbulos con el químico nocodazol bloquea la aparición de los gránulos. [19] Además, se ha demostrado que muchas moléculas de señalización regulan la formación o la dinámica de los gránulos de estrés; Estos incluyen la proteína quinasa activada por AMP (AMPK) , un "sensor de energía maestro" , [20] la enzima transferasa O-GlcNAc (OGT) , [21] y la quinasa proapoptótica ROCK1 . [22]

Funciones potenciales de las interacciones ARN-ARN

Las transiciones de fase del ARN impulsadas en parte por interacciones intermoleculares ARN-ARN pueden desempeñar un papel en la formación de gránulos de estrés. De manera similar a las proteínas intrínsecamente desordenadas, los extractos de ARN total son capaces de experimentar una separación de fases en condiciones fisiológicas in vitro . [23] Los análisis de ARN-seq demuestran que estos ensamblajes comparten un transcriptoma en gran medida superpuesto con los gránulos de estrés, [23] [7] y el enriquecimiento de ARN en ambos se basa predominantemente en la longitud del ARN. Además, los gránulos de estrés contienen muchas helicasas de ARN , [24] incluidas las helicasas DEAD/H-box Ded1p/ DDX3 , eIF4A1 y RHAU . [25] En levadura, los alelos mutantes catalíticos ded1 dan lugar a gránulos de estrés constitutivos [26] Los alelos mutantes DDX3X deficientes en ATPasa (el homólogo mamífero de Ded1) se encuentran en el meduloblastoma pediátrico , [27] y estos coinciden con ensamblajes granulares constitutivos en células de pacientes. [28] Estas proteínas DDX3 mutantes promueven el ensamblaje de gránulos de estrés en células HeLa . [28] En células de mamíferos, los mutantes RHAU conducen a una dinámica reducida de los gránulos de estrés. [25] Por lo tanto, algunos plantean la hipótesis de que la agregación de ARN facilitada por interacciones intermoleculares ARN-ARN desempeña un papel en la formación de gránulos de estrés, y que este papel puede estar regulado por helicasas de ARN . [29] También hay evidencia de que el ARN dentro de los gránulos de estrés está más compactado, en comparación con el ARN en el citoplasma , y ​​que se ha descubierto que el ARN se modifica postraduccionalmente por la N6-metiladenosina (m 6 A) en sus extremos 5' o la acetilación del ARN ac4C. [30] [31] [32] Trabajos recientes han demostrado que el factor de iniciación de la traducción altamente abundante y la proteína DEAD-box eIF4A limita la formación de gránulos de estrés. Lo hace a través de su capacidad para unirse a ATP y ARN, actuando de manera análoga a las chaperonas proteicas como Hsp70 . [33]

Conexión con los órganos de procesamiento

Los gránulos de estrés y los cuerpos P (cuerpos de procesamiento) comparten componentes de ARN y proteínas , ambos aparecen bajo estrés y pueden asociarse físicamente entre sí. A partir de 2018, de las ~660 proteínas identificadas como localizadas en gránulos de estrés, ~11% también se han identificado como proteínas localizadas en cuerpos de procesamiento (ver a continuación). La proteína G3BP1 es necesaria para el acoplamiento adecuado de los cuerpos de procesamiento y los gránulos de estrés entre sí, lo que puede ser importante para la preservación del ARNm poliadenilado . [34]

Aunque algunos componentes proteicos son compartidos entre los gránulos de estrés y los cuerpos de procesamiento, la mayoría de las proteínas en cualquiera de las estructuras están localizadas de forma única en cada una de ellas. [35] Aunque tanto los gránulos de estrés como los cuerpos P están asociados con el ARNm , se ha propuesto desde hace tiempo que los cuerpos de procesamiento son sitios de degradación del ARNm porque contienen enzimas como DCP1/2 y XRN1 que se sabe que degradan el ARNm. [36] Sin embargo, otros han demostrado que el ARNm asociado con los cuerpos de procesamiento se reprime en gran medida a nivel traduccional, pero no se degrada. [35] También se ha propuesto que el ARNm seleccionado para la degradación pasa de los gránulos de estrés a los cuerpos de procesamiento, [36] aunque también hay datos que sugieren que los cuerpos de procesamiento preceden y promueven la formación de los gránulos de estrés. [37]

Composición proteica de los gránulos de estrés

El proteoma completo de los gránulos de estrés aún se desconoce, pero se han hecho esfuerzos para catalogar todas las proteínas que se ha demostrado experimentalmente que transitan hacia los gránulos de estrés. [38] [39] [40] Es importante destacar que diferentes factores de estrés pueden dar lugar a gránulos de estrés con diferentes componentes proteicos. [16] Se han identificado muchas proteínas asociadas a los gránulos de estrés estresando transitoriamente células cultivadas y utilizando microscopía para detectar la localización de una proteína de interés, ya sea expresando esa proteína fusionada a una proteína fluorescente (es decir, proteína fluorescente verde (GFP)) y/o fijando células y utilizando anticuerpos para detectar la proteína de interés junto con marcadores proteicos conocidos de gránulos de estrés ( inmunocitoquímica ). [41]

En 2016, se identificaron experimentalmente "núcleos" de gránulos de estrés y luego se purificaron bioquímicamente por primera vez. Las proteínas en los núcleos se identificaron de manera imparcial mediante espectrometría de masas . Este avance técnico condujo a la identificación de cientos de nuevas proteínas localizadas en gránulos de estrés. [42] [24] [43]

El proteoma de los gránulos de estrés también se ha determinado experimentalmente utilizando dos enfoques de etiquetado de proximidad ligeramente diferentes . Uno de estos enfoques de etiquetado de proximidad es el método de ascorbato peroxidasa (APEX), en el que las células se diseñan para expresar una proteína de gránulo de estrés conocida, como G3BP1 , fusionada a una enzima ascorbato peroxidasa modificada llamada APEX. [38] [44] Al incubar las células en biotina y tratarlas con peróxido de hidrógeno , la enzima APEX se activará brevemente para biotinilar todas las proteínas cercanas a la proteína de interés, en este caso G3BP1 dentro de los gránulos de estrés. Las proteínas que están biotiniladas se pueden aislar a través de estreptavidina e identificar mediante espectrometría de masas . La técnica APEX se utilizó para identificar ~260 proteínas asociadas a gránulos de estrés en varios tipos de células, incluidas las neuronas , y con varios estresores. De las 260 proteínas identificadas en este estudio, ~143 no se había demostrado previamente que estuvieran asociadas a gránulos de estrés. [44]

Otro método de etiquetado de proximidad utilizado para determinar el proteoma de los gránulos de estrés es BioID. [45] BioID es similar al enfoque APEX, en el que una proteína biotinilada (BirA* en lugar de APEX) se expresó en células como una proteína de fusión con varias proteínas asociadas a los gránulos de estrés conocidas. Las proteínas en estrecha proximidad a BirA* serán biotiniladas y luego se identificarán mediante espectrometría de masas . Youn et al. utilizaron este método para identificar/predecir 138 proteínas como asociadas a los gránulos de estrés y 42 como asociadas al cuerpo de procesamiento. [45]

Aquí se puede encontrar una base de datos seleccionada de proteínas asociadas a los gránulos de estrés [1]. [40]

La siguiente es una lista de proteínas que se ha demostrado que se localizan en gránulos de estrés (compilada de [38] [39] [24] [44] [45] [46] ):

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