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 language | English |
|---|---|
| Pages (from-to) | 1017-1025 |
| Number of pages | 9 |
| Journal | Molecular Biology and Evolution |
| Volume | 15 |
| Issue number | 8 |
| Publication status | Published - Aug 1998 |
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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
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 journal › Article
}
TY - JOUR
T1 - The 67-kDa laminin receptor originated from a ribosomal protein that acquired a dual function during evolution
AU - Ardini, Elena
AU - Pesole, Graziano
AU - Tagliabue, Elda
AU - Magnifico, Alessandra
AU - Castronovo, Vincent
AU - Sobel, Mark E.
AU - Colnaghi, Maria I.
AU - Ménard, Sylvie
PY - 1998/8
Y1 - 1998/8
N2 - 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.
AB - 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.
KW - Adhesion molecules
KW - Evolution
KW - Metastasis
KW - Monomeric laminin receptor
KW - Ribosomal proteins
KW - Tumor aggressiveness
UR - http://www.scopus.com/inward/record.url?scp=0031880124&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0031880124&partnerID=8YFLogxK
M3 - Article
VL - 15
SP - 1017
EP - 1025
JO - Molecular Biology and Evolution
JF - Molecular Biology and Evolution
SN - 0737-4038
IS - 8
ER -