Molecular Biology and Evolution, Vol 9, 216-234, Copyright © 1992 by Society for Molecular Biology and Evolution
AL Hughes
The integrin receptors are heterodimers whose alpha and beta subunits are
encoded by separate, evolutionarily unrelated multigene families.
Phylogenetic analysis of DNA sequences from these two gene families showed
that they have not always evolved in a parallel fashion. The integrin alpha
chains that can form heterodimers with beta 1 do not constitute a
monophyletic group, nor do the beta chains which can form heterodimers with
alpha V. On the other hand, the vertebrate alpha chains associating with
beta 2 are a monophyletic group. In the metal cation-binding region of the
alpha chain, an exon exchange took place between human alpha M and alpha X
approximately 40-50 Mya, homogenizing this functionally important region in
these two alpha chains. When integrin beta chains of different functional
classes are compared, nonsynonymous (amino acid altering) nucleotide
substitutions that alter amino acid residue charge in the central region of
the molecule occur at a rate significantly higher than that expected under
random replacement. By contrast, when closely related beta 1 chains are
compared, residue charge is conserved in this region. These results
pinpoint the central region as a focus of functional divergence among
integrin beta chains, perhaps relating to the ability of each beta integrin
class to associate with a specific array of alpha integrins. Furthermore,
they imply that positive, directional selection on this region has occurred
in the evolution of the integrin beta-chain gene family.
ORIGINAL ARTICLE
Coevolution of the vertebrate integrin alpha- and beta-chain genes
Department of Biology and Institute of Molecular Evolutionary Genetics, Pennsylvania State University, University Park 16802.
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