ETR-1, a homologue of a protein linked to myotonic dystrophy, is essential for muscle development in Caenorhabditis elegans

Curr Biol. 1999 Nov 4;9(21):1243-6. doi: 10.1016/s0960-9822(99)80504-1.

Abstract

Post-transcriptional gene processing by RNA-binding proteins (RBPs) has crucial roles during development [1] [2]. Here, we report the identification of ETR-1 (ELAV-type RNA-binding protein), a muscle-specific RBP in the nematode Caenorhabditis elegans. ETR-1 is related to the family of RBPs defined by the protein ELAV, which is essential for neurogenesis in the fruit fly Drosophila; members of the family possess two consecutive RNA recognition motifs (RRMs) separated from a third, carboxy-terminal RRM by a tether region of variable length [3] [4] [5] [6]. Its closest homologue, CUG-binding protein (CUG-bp), is a human RBP that has been implicated in the disease myotonic dystrophy and binds CUG repeats in the 3' untranslated region (UTR) of the mRNA for myotonic dystrophy protein kinase (DMPK) [7] [8]. Inactivation of etr-1 by RNA-mediated interference resulted in embryonic lethality. Embryos failed to elongate and became paralysed, a phenotype characteristic of C. elegans Pat mutants, which are defective in muscle formation and function [9]. The data indicate that etr-1 is essential for muscle development in C. elegans, perhaps by playing a role in post-transcriptional processing of some muscle component, and thus suggesting a possible conservation of gene function with human CUG-bp.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • CELF1 Protein
  • Caenorhabditis elegans / growth & development
  • Caenorhabditis elegans / physiology*
  • ELAV Proteins
  • Humans
  • Muscle Development*
  • Muscle Proteins / isolation & purification
  • Muscle Proteins / physiology*
  • Muscles / physiology
  • Myotonic Dystrophy / metabolism*
  • RNA-Binding Proteins / chemistry
  • RNA-Binding Proteins / isolation & purification
  • RNA-Binding Proteins / metabolism
  • RNA-Binding Proteins / physiology*
  • Ribonucleoproteins / chemistry
  • Ribonucleoproteins / metabolism
  • Xenopus Proteins*

Substances

  • CELF1 Protein
  • CELF1 protein, human
  • CELF3 protein, Xenopus
  • ELAV Proteins
  • Muscle Proteins
  • RNA-Binding Proteins
  • Ribonucleoproteins
  • Xenopus Proteins