Products of the unc-52 gene in Caenorhabditis elegans are homologous to the core protein of the mammalian basement membrane heparan sulfate proteoglycan

Teresa M. Rogalski, Benjamin D. Williams, Gregory P. Mullen, Donald G. Moerman

Research output: Contribution to journalArticlepeer-review

Abstract

Mutations in the unc-52 gene of Caenorhabditis elegans affect attachment of the myofilament lattice to the muscle cell membrane. Here, we demonstrate that the unc-52 gene encodes a nematode homolog of perlecan, the mammalian basement membrane heparan sulfate proteoglycan. The longest potential open reading frame of this gene encodes a 2482-amino-acid protein with a signal peptide and four domains. The first domain is unique to the unc-52 polypeptide, whereas the three remaining domains contain sequences found in the LDL receptor (domain II) laminin (domain III) and N-CAM (domain IV). We have identified three alternatively spliced transcripts that encode different carboxy-terminal sequences. The two larger transcripts encode proteins containing all or part of domain IV, whereas the smaller transcript encodes a shortened polypeptide that completely lacks domain IV. We have determined that the disorganized muscle phenotype observed in unc-52(st196) animals is caused by the insertion of a Tc1 transposon into domain IV. Two monoclonal antibodies that recognize an extracellular component of all contractile tissues in C. elegans fail to stain embryos homozygous for a lethal unc-52 allele. We have mapped the epitopes recognized by both monoclonal antibodies to a region of domain IV in the unc-52-encoded protein sequence.

Original languageEnglish (US)
Pages (from-to)1471-1484
Number of pages14
JournalGenes and Development
Volume7
Issue number8
DOIs
StatePublished - 1993
Externally publishedYes

Keywords

  • Basement membrane
  • Myofilament lattice
  • Perlecan
  • Unc-52 gene-, C.elegans-, muscle

ASJC Scopus subject areas

  • Genetics
  • Developmental Biology

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