Functional conservation of atonal and Math1 in the CNS and PNS

Development. 2000 Mar;127(5):1039-48.

Abstract

To determine the extent to which atonal and its mouse homolog Math1 exhibit functional conservation, we inserted (beta)-galactosidase (lacZ) into the Math1 locus and analyzed its expression, evaluated consequences of loss of Math1 function, and expressed Math1 in atonal mutant flies. lacZ under the control of Math1 regulatory elements duplicated the previously known expression pattern of Math1 in the CNS (i.e., the neural tube, dorsal spinal cord, brainstem, and cerebellar external granule neurons) but also revealed new sites of expression: PNS mechanoreceptors (inner ear hair cells and Merkel cells) and articular chondrocytes. Expressing Math1 induced ectopic chordotonal organs (CHOs) in wild-type flies and partially rescued CHO loss in atonal mutant embryos. These data demonstrate that both the mouse and fly homologs encode lineage identity information and, more interestingly, that some of the cells dependent on this information serve similar mechanoreceptor functions.

Publication types

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

MeSH terms

  • Animals
  • Basic Helix-Loop-Helix Transcription Factors
  • Central Nervous System / embryology*
  • DNA-Binding Proteins / genetics*
  • Drosophila / embryology
  • Drosophila Proteins
  • Embryo, Nonmammalian / embryology
  • Female
  • Gene Expression Regulation, Developmental
  • Helix-Loop-Helix Motifs
  • Male
  • Mice
  • Mice, Transgenic
  • Nerve Tissue Proteins / genetics
  • Organ Specificity
  • Peripheral Nervous System / embryology*
  • Transcription Factors / genetics*
  • beta-Galactosidase / analysis
  • beta-Galactosidase / genetics

Substances

  • Atoh1 protein, mouse
  • Basic Helix-Loop-Helix Transcription Factors
  • DNA-Binding Proteins
  • Drosophila Proteins
  • Nerve Tissue Proteins
  • Transcription Factors
  • ato protein, Drosophila
  • beta-Galactosidase