The 67-kDa laminin receptor originated from a ribosomal protein that acquired a dual function during evolution

Elena Ardini, Graziano Pesole, Elda Tagliabue, Alessandra Magnifico, Vincent Castronovo, Mark E. Sobel, Maria I. Colnaghi, Sylvie Ménard

Research output: Contribution to journalArticle

105 Citations (Scopus)

Abstract

The 67-kDa laminin receptor (67LR) is a nonintegrin cell surface receptor that mediates high-affinity interactions between cells and laminin. Overexpression of this protein in tumor cells has been related to tumor invasion and metastasis. Thus far, only a full-length gene encoding a 37-kDa precursor protein (37LRP) has been isolated. The finding that the cDNA for the 37LRP is virtually identical to a cDNA encoding the ribosomal protein p40 has suggested that 37LRP is actually a component of the translational machinery, with no laminin-binding activity. On the other hand, a peptide of 20 amino acids deduced from the sequence of 37LRP/p40 was shown to exhibit high laminin-binding activity. The evolutionary relationship between 23 sequences of 37LRP/p40 proteins was analyzed. This phylogenetic analysis indicated that all of the protein sequences derive from orthologous genes and that the 37LRP is indeed a ribosomal protein that acquired the novel function of laminin receptor during evolution. The evolutionary analysis of the sequence identified as the laminin-binding site in the human protein suggested that the acquisition of the laminin-binding capability is linked to the palindromic sequence LMWWML, which appeared during evolution concomitantly with laminin.

Original languageEnglish
Pages (from-to)1017-1025
Number of pages9
JournalMolecular Biology and Evolution
Volume15
Issue number8
Publication statusPublished - Aug 1998

Fingerprint

Laminin Receptors
laminin
Ribosomal Proteins
ribosomal proteins
Laminin
receptors
protein
Tumors
tumor
Proteins
Complementary DNA
Gene encoding
Protein Precursors
proteins
Cell Surface Receptors
gene
Cell Communication
Genes
Machinery
Sequence Analysis

Keywords

  • Adhesion molecules
  • Evolution
  • Metastasis
  • Monomeric laminin receptor
  • Ribosomal proteins
  • Tumor aggressiveness

ASJC Scopus subject areas

  • Genetics
  • Biochemistry
  • Genetics(clinical)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Ecology, Evolution, Behavior and Systematics
  • Agricultural and Biological Sciences (miscellaneous)
  • Molecular Biology

Cite this

Ardini, E., Pesole, G., Tagliabue, E., Magnifico, A., Castronovo, V., Sobel, M. E., ... Ménard, S. (1998). The 67-kDa laminin receptor originated from a ribosomal protein that acquired a dual function during evolution. Molecular Biology and Evolution, 15(8), 1017-1025.

The 67-kDa laminin receptor originated from a ribosomal protein that acquired a dual function during evolution. / Ardini, Elena; Pesole, Graziano; Tagliabue, Elda; Magnifico, Alessandra; Castronovo, Vincent; Sobel, Mark E.; Colnaghi, Maria I.; Ménard, Sylvie.

In: Molecular Biology and Evolution, Vol. 15, No. 8, 08.1998, p. 1017-1025.

Research output: Contribution to journalArticle

Ardini, E, Pesole, G, Tagliabue, E, Magnifico, A, Castronovo, V, Sobel, ME, Colnaghi, MI & Ménard, S 1998, 'The 67-kDa laminin receptor originated from a ribosomal protein that acquired a dual function during evolution', Molecular Biology and Evolution, vol. 15, no. 8, pp. 1017-1025.
Ardini, Elena ; Pesole, Graziano ; Tagliabue, Elda ; Magnifico, Alessandra ; Castronovo, Vincent ; Sobel, Mark E. ; Colnaghi, Maria I. ; Ménard, Sylvie. / The 67-kDa laminin receptor originated from a ribosomal protein that acquired a dual function during evolution. In: Molecular Biology and Evolution. 1998 ; Vol. 15, No. 8. pp. 1017-1025.
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