Genome-Wide Identification and Characterization of Tyrosine Kinases in the Silkworm, Bombyx mori

Int J Mol Sci. 2018 Mar 21;19(4):934. doi: 10.3390/ijms19040934.

Abstract

The tyrosine kinases (TKs) are important parts of metazoan signaling pathways and play significant roles in cell growth, development, apoptosis and disease. Genome-wide characterization of TKs has been conducted in many metazoans, however, systematic information about this family in Lepidoptera is still lacking. We retrieved 33 TK-encoding genes in silkworm and classified them into 25 subfamilies by sequence analysis, without members in AXL, FRK, PDGFR, STYK1 and TIE subfamilies. Although domain sequences in each subfamily are conserved, TKs in vertebrates tend to be remarkably conserved and stable. Our results of phylogenetic analysis supported the previous conclusion for the second major expansion of TK family. Gene-Ontology (GO) analysis revealed that a higher proportion of BmTKs played roles in binding, catalysis, signal transduction, metabolism, biological regulation and response to stimulus, compared to all silkworm genes annotated in GO. Moreover, the expression profile analysis of BmTKs among multiple tissues and developmental stages demonstrated that many genes exhibited stage-specific and/or sex-related expression during embryogenesis, molting and metamorphosis, and that 8 BmTKs presented tissue-specific high expression. Our study provides systematic description of silkworm tyrosine kinases, and may also provide further insights into metazoan TKs and assist future studies addressing their functions.

Keywords: characterization; expression pattern; metazoans; silkworm; tyrosine kinase.

MeSH terms

  • Animals
  • Bombyx / enzymology*
  • Bombyx / genetics*
  • Chromosomes / genetics
  • Gene Expression Profiling
  • Gene Ontology
  • Genes, Insect
  • Genome, Insect*
  • Insect Proteins / genetics
  • Multigene Family
  • Phylogeny
  • Protein-Tyrosine Kinases / genetics*
  • Protein-Tyrosine Kinases / metabolism
  • Time Factors

Substances

  • Insect Proteins
  • Protein-Tyrosine Kinases