DDX6 modulates P-body and stress granule assembly, composition, and docking. Journal Article uri icon



  • Stress granules and P-bodies are ribonucleoprotein (RNP) granules that accumulate during the stress response due to the condensation of untranslating mRNPs. Stress granules form in part by intermolecular RNA-RNA interactions and can be limited by components of the RNA chaperone network, which inhibits RNA-driven aggregation. Herein, we demonstrate that the DEAD-box helicase DDX6, a P-body component, can also limit the formation of stress granules, independent of the formation of P-bodies. In an ATPase, RNA-binding dependent manner, DDX6 limits the partitioning of itself and other RNPs into stress granules. When P-bodies are limited, proteins that normally partition between stress granules and P-bodies show increased accumulation within stress granules. Moreover, we show that loss of DDX6, 4E-T, and DCP1A increases P-body docking with stress granules, which depends on CNOT1 and PAT1B. Taken together, these observations identify a new role for DDX6 in limiting stress granules and demonstrate that P-body components can influence stress granule composition and docking with P-bodies.

publication date

  • June 3, 2024

has restriction

  • hybrid

Date in CU Experts

  • April 3, 2024 12:43 PM

Full Author List

  • Ripin N; Macedo de Vasconcelos L; Ugay DA; Parker R

author count

  • 4

Other Profiles

Electronic International Standard Serial Number (EISSN)

  • 1540-8140

Additional Document Info


  • 223


  • 6