Reference : The 67-kDa laminin receptor originated from a ribosomal protein that acquired a dual fun...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
Human health sciences : Oncology
http://hdl.handle.net/2268/24096
The 67-kDa laminin receptor originated from a ribosomal protein that acquired a dual function during evolution.
English
Ardini, E. [> > > >]
Pesole, G. [> > > >]
Tagliabue, E. [> > > >]
Magnifico, A. [> > > >]
Castronovo, Vincenzo mailto [Université de Liège - ULg > Département des sciences biomédicales et précliniques > Biologie générale et cellulaire - GIGA-R : Labo de recherche sur les métastases >]
Sobel, M. E. [> > > >]
Colnaghi, M. I. [> > > >]
Menard, S. [> > > >]
1998
Molecular Biology and Evolution
Oxford University Press
15
8
1017-25
Yes (verified by ORBi)
International
0737-4038
1537-1719
New York
NY
[en] Amino Acid Sequence ; Animals ; Binding Sites/genetics ; Evolution, Molecular ; Humans ; Laminin/metabolism ; Molecular Sequence Data ; Molecular Weight ; Neoplasms/genetics ; Phylogeny ; Protein Precursors/chemistry/genetics/metabolism ; Receptors, Laminin/chemistry/genetics/metabolism ; Ribosomal Proteins/chemistry/genetics ; Sequence Homology, Amino Acid
[en] 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.
AIRC/FIRC ; EU Project BIO4-CT95-0130
http://hdl.handle.net/2268/24096

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