Pumping the brakes: A noncanonical RNA-binding domain in FMRP stalls elongating ribosomes

J Biol Chem. 2023 Jan;299(1):102773. doi: 10.1016/j.jbc.2022.102773. Epub 2022 Dec 5.

Abstract

Loss of function of the RNA-binding protein FMRP causes fragile X syndrome, the most common inherited form of intellectual disability and autism spectrum disorders. FMRP is suggested to modulate synaptic plasticity by regulating the synthesis of proteins involved in neuronal and synaptic function; however, the mechanism underlying FMRP mRNA targeting specificity remains unclear. Intriguing recent work published in JBC by Scarpitti and colleagues identifies and characterizes a noncanonical RNA-binding domain that is required for FMRP-mediated translation regulation, shedding light on FMRP function.

Keywords: FMRP; RNA-binding protein; fragile X mental retardation protein; fragile X syndrome; protein synthesis; translational control.

MeSH terms

  • Fragile X Mental Retardation Protein* / genetics
  • Fragile X Mental Retardation Protein* / metabolism
  • Fragile X Syndrome / genetics
  • Fragile X Syndrome / metabolism
  • Humans
  • RNA Recognition Motif* / genetics
  • Ribosomes / metabolism

Substances

  • Fragile X Mental Retardation Protein