Carboxy-terminal truncation activates glp-1 protein to specify vulval fates in Caenorhabditis elegans

Nature. 1991 Aug 29;352(6338):811-5. doi: 10.1038/352811a0.


The glp-1 and lin-12 genes encode homologous transmembrane proteins that may act as receptors for cell interactions during development. The glp-1 product is required for induction of germ-line proliferation and for embryogenesis. By contrast, lin-12 mediates somatic cell interactions, including those between the precursor cells that form the vulval hypodermis (VPCs). Here we analyse an unusual allele of glp-1, glp-1(q35), which displays a semidominant multivulva phenotype (Muv), as well as the typical recessive, loss-of-function Glp phenotypes (sterility and embryonic lethality). We find that the effects of glp-1(q35) on VPC development mimic those of dominant lin-12 mutations, even in the absence of lin-12 activity. The glp-1(q35) gene bears a nonsense mutation predicted to eliminate the 122 C-terminal amino acids, including a ProGluSerThr (PEST) sequence thought to destabilize proteins. We suggest that the carboxy terminus bears a negative regulatory domain which normally inactivates glp-1 in the VPCs. We propose that inappropriate glp-1(q35) activity can substitute for lin-12 to determine vulval fate, perhaps by driving the VPCs to proliferate.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Caenorhabditis / embryology
  • Caenorhabditis / genetics
  • Caenorhabditis / growth & development*
  • Caenorhabditis elegans Proteins*
  • Cell Division
  • Female
  • Germ Cells / cytology
  • Membrane Glycoproteins / chemistry
  • Membrane Glycoproteins / genetics
  • Membrane Glycoproteins / physiology*
  • Membrane Proteins / chemistry
  • Membrane Proteins / genetics
  • Membrane Proteins / physiology*
  • Molecular Sequence Data
  • Mutation
  • Phenotype
  • Receptors, Notch
  • Vulva / embryology
  • Vulva / growth & development


  • Caenorhabditis elegans Proteins
  • Glp-1 protein, C elegans
  • Membrane Glycoproteins
  • Membrane Proteins
  • Receptors, Notch