The 67-kDa laminin receptor originated from a ribosomal protein that acquired a dual function during evolution |
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Authors: | Ardini E; Pesole G; Tagliabue E; Magnifico A; Castronovo V; Sobel ME; Colnaghi MI; Menard S |
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Institution: | Division of Experimental Oncology E, Istituto Nazionale Tumori, Milan, Italy. |
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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 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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