Phylogenetic Analysis of Kindlins Suggests Subfunctionalization of an Ancestral Unduplicated Kindlin into Three Paralogs in Vertebrates
Author(s) -
Ammad Aslam Khan,
Axel Janke,
Takashi Shimokawa,
Hongquan Zhang
Publication year - 2011
Publication title -
evolutionary bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.502
H-Index - 32
ISSN - 1176-9343
DOI - 10.4137/ebo.s6179
Subject(s) - subfunctionalization , gene duplication , biology , phylogenetics , ferm domain , phylogenetic tree , evolutionary biology , genetics , gene , functional divergence , protein family , gene family , protein domain , genome , computational biology , membrane protein , integral membrane protein , membrane
Kindlin proteins represent a newly discovered family of evolutionarily conserved FERM domain-containing proteins. This family includes three highly conserved proteins: Kindlin-1, Kindlin-2 and Kindlin-3. All three Kindlin proteins are associated with focal adhesions and are involved in integrin activation. The FERM domain of each Kindlin is bipartite and plays a key role in integrin activation. We herein explore for the first time the evolutionary history of these proteins. The phylogeny of the Kindlins suggests a single ancestral Kindlin protein present in even the earliest metazoan ie, hydra. This protein then underwent duplication events in insects and also experienced genome duplication in vertebrates, leading to the Kindlin family. A comparative study of the Kindlin paralogs showed that Kindlin-2 is the slowest evolving protein among the three family members. The analysis of synonymous and non-synonymous substitutions in orthologous Kindlin sequences in different species showed that all three Kindlins have been evolving under the influence of purifying selection. The expression pattern of Kindlins along with phylogenetic studies supports the subfunctionalization model of gene duplication.
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