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Molecular Biology and Evolution, Vol 15, 1017-1025, Copyright © 1998 by Society for Molecular Biology and Evolution

ORIGINAL ARTICLE

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

E Ardini, G Pesole, E Tagliabue, A Magnifico, V Castronovo, ME Sobel, MI Colnaghi and S Menard
Division of Experimental Oncology E, Istituto Nazionale Tumori, Milan, Italy.

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 37LR/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.
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