Your browser doesn't support javascript.
loading
Functionally distinct roles for eEF2K in the control of ribosome availability and p-body abundance.
Smith, Patrick R; Loerch, Sarah; Kunder, Nikesh; Stanowick, Alexander D; Lou, Tzu-Fang; Campbell, Zachary T.
Afiliación
  • Smith PR; The University of Texas at Dallas, Department of Biological Sciences, Richardson, TX, USA.
  • Loerch S; Janelia Research Campus, Howard Hughes Medical Institute, Ashburn, VA, USA.
  • Kunder N; University of California, Santa Cruz, Department of Chemistry and Biochemistry, Santa Cruz, CA, USA.
  • Stanowick AD; The University of Texas at Dallas, Department of Biological Sciences, Richardson, TX, USA.
  • Lou TF; The University of Texas at Dallas, Department of Biological Sciences, Richardson, TX, USA.
  • Campbell ZT; The University of Texas at Dallas, Department of Biological Sciences, Richardson, TX, USA.
Nat Commun ; 12(1): 6789, 2021 11 23.
Article en En | MEDLINE | ID: mdl-34815424
Processing bodies (p-bodies) are a prototypical phase-separated RNA-containing granule. Their abundance is highly dynamic and has been linked to translation. Yet, the molecular mechanisms responsible for coordinate control of the two processes are unclear. Here, we uncover key roles for eEF2 kinase (eEF2K) in the control of ribosome availability and p-body abundance. eEF2K acts on a sole known substrate, eEF2, to inhibit translation. We find that the eEF2K agonist nelfinavir abolishes p-bodies in sensory neurons and impairs translation. To probe the latter, we used cryo-electron microscopy. Nelfinavir stabilizes vacant 80S ribosomes. They contain SERBP1 in place of mRNA and eEF2 in the acceptor site. Phosphorylated eEF2 associates with inactive ribosomes that resist splitting in vitro. Collectively, the data suggest that eEF2K defines a population of inactive ribosomes resistant to recycling and protected from degradation. Thus, eEF2K activity is central to both p-body abundance and ribosome availability in sensory neurons.
Asunto(s)
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ribosomas / Factor 2 de Elongación Peptídica / Quinasa del Factor 2 de Elongación / Cuerpos de Procesamiento Límite: Animals / Humans / Male Idioma: En Revista: Nat Commun Asunto de la revista: BIOLOGIA / CIENCIA Año: 2021 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ribosomas / Factor 2 de Elongación Peptídica / Quinasa del Factor 2 de Elongación / Cuerpos de Procesamiento Límite: Animals / Humans / Male Idioma: En Revista: Nat Commun Asunto de la revista: BIOLOGIA / CIENCIA Año: 2021 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido