PolyQ-dependent RNA-protein assemblies control symmetry breaking

J Cell Biol. 2015 Mar 2;208(5):533-44. doi: 10.1083/jcb.201407105. Epub 2015 Feb 23.

Abstract

Dendritic growth in fungi and neurons requires that multiple axes of polarity are established and maintained within the same cytoplasm. We have discovered that transcripts encoding key polarity factors including a formin, Bni1, and a polarisome scaffold, Spa2, are nonrandomly clustered in the cytosol to initiate and maintain sites of polarized growth in the fungus Ashbya gossypii. This asymmetric distribution requires the mRNAs to interact with a polyQ-containing protein, Whi3, and a Pumilio protein with a low-complexity sequence, Puf2. Cells lacking Whi3 or Puf2 had severe defects in establishing new sites of polarity and failed to localize Bni1 protein. Interaction of mRNAs with Whi3 and Puf2 promotes enrichment of transcripts at established sites of polarized growth and clustering of polarity transcripts throughout the cell body. Thus, aggregation-prone proteins make functional assemblies to position polarity transcripts, and nonrandom positioning of transcripts is required for symmetry-breaking events. This reveals a physiological function for polyQ-driven assemblies in regulating cell polarity.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Cytosol / metabolism
  • Fungal Proteins / genetics
  • Fungal Proteins / metabolism*
  • Microfilament Proteins / genetics
  • Microfilament Proteins / metabolism*
  • Multiprotein Complexes / genetics
  • Multiprotein Complexes / metabolism
  • Peptides / genetics
  • Peptides / metabolism*
  • RNA, Fungal / genetics
  • RNA, Fungal / metabolism*
  • RNA-Binding Proteins / genetics
  • RNA-Binding Proteins / metabolism*
  • Saccharomycetales / genetics
  • Saccharomycetales / metabolism*

Substances

  • Fungal Proteins
  • Microfilament Proteins
  • Multiprotein Complexes
  • Peptides
  • RNA, Fungal
  • RNA-Binding Proteins
  • polyglutamine