lin-35/Rb cooperates with the SWI/SNF complex to control Caenorhabditis elegans larval development

Genetics. 2004 Jul;167(3):1177-85. doi: 10.1534/genetics.103.024554.

Abstract

Null mutations in lin-35, the Caenorhabditis elegans ortholog of the mammalian Rb protein, cause no obvious morphological defects. Using a genetic approach to identify genes that may function redundantly with lin-35, we have isolated a mutation in the C. elegans psa-1 gene. lin-35; psa-1 double mutants display severe developmental defects leading to early larval arrest and adult sterility. The psa-1 gene has previously been shown to encode a C. elegans homolog of yeast SWI3, a critical component of the SWI/SNF complex, and has been shown to regulate asymmetric cell divisions during C. elegans development. We observed strong genetic interactions between psa-1 and lin-35 as well as a subset of the class B synMuv genes that include lin-37 and lin-9. Loss-of-function mutations in lin-35, lin-37, and lin-9 strongly enhanced the defects of asymmetric T cell division associated with a psa-1 mutation. Our results suggest that LIN-35/Rb and a certain class B synMuv proteins collaborate with the SWI/SNF protein complex to regulate the T cell division as well as other events essential for larval growth.

Publication types

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

MeSH terms

  • Animals
  • Caenorhabditis elegans / genetics*
  • Caenorhabditis elegans / growth & development*
  • Caenorhabditis elegans Proteins / genetics
  • Caenorhabditis elegans Proteins / metabolism*
  • Cell Lineage
  • Larva / cytology
  • Larva / growth & development
  • Mutation / genetics
  • Nuclear Proteins / genetics
  • Phenotype
  • RNA Interference
  • Repressor Proteins / genetics
  • Repressor Proteins / metabolism*
  • Saccharomyces cerevisiae Proteins / genetics
  • Trans-Activators / genetics

Substances

  • Caenorhabditis elegans Proteins
  • Nuclear Proteins
  • Repressor Proteins
  • SWI3 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Trans-Activators
  • lin-35 protein, C elegans