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EMBO Rep ; 20(9): e46238, 2019 09.
Artículo en Inglés | MEDLINE | ID: mdl-31347268

RESUMEN

The protein p62/Sequestosome 1 (p62) has been described as a selective autophagy receptor and independently as a platform for pro-inflammatory and other intracellular signaling. How these seemingly disparate functional roles of p62 are coordinated has not been resolved. Here, we show that TAK1, a kinase involved in immune signaling, negatively regulates p62 action in autophagy. TAK1 reduces p62 localization to autophagosomes, dampening the autophagic degradation of both p62 and p62-directed autophagy substrates. TAK1 also relocalizes p62 into dynamic cytoplasmic bodies, a phenomenon that accompanies the stabilization of TAK1 complex components. On the other hand, p62 facilitates the assembly and activation of TAK1 complexes, suggesting a connection between p62's signaling functions and p62 body formation. Thus, TAK1 governs p62 action, switching it from an autophagy receptor to a signaling platform. This ability of TAK1 to disable p62 as an autophagy receptor may allow certain autophagic substrates to accumulate when needed for cellular functions.


Asunto(s)
Autofagia/fisiología , Quinasas Quinasa Quinasa PAM/metabolismo , Proteínas de Unión al ARN/metabolismo , Proteína Sequestosoma-1/metabolismo , Autofagosomas/metabolismo , Autofagia/genética , Células HEK293 , Células HeLa , Humanos , Immunoblotting , Inmunoprecipitación , Quinasas Quinasa Quinasa PAM/genética , Microscopía Confocal , ARN Interferente Pequeño/genética , ARN Interferente Pequeño/metabolismo , Proteínas de Unión al ARN/genética , Proteína Sequestosoma-1/genética , Transducción de Señal/genética , Transducción de Señal/fisiología
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