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Emergence and subsequent functional specialization of kindlins during evolution of cell adhesiveness.

Meller J, Rogozin IB, Poliakov E, Meller N, Bedanov-Pack M, Plow EF, Qin J, Podrez EA, Byzova TV - Mol. Biol. Cell (2014)

Bottom Line: Among the analyzed species, all metazoan lineages—but none of the premetazoans—had at least one kindlin-encoding gene, whereas talin was present in several premetazoan lineages.The presence of this segment enables K2 but not K3 to localize to focal adhesions.Thus emergence and subsequent functional specialization of kindlins allowed multicellular organisms to develop additional tissue-specific adaptations of cell adhesiveness.

View Article: PubMed Central - PubMed

Affiliation: Department of Molecular Cardiology, Joseph J. Jacobs Center for Thrombosis and Vascular Biology, Lerner Research Institute, Cleveland Clinic, Cleveland, OH 44195.

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(A) Alignment of human talin 1, human kindlin 2, and human AFAP1L2 genes. The region of similarity with AFAP1L2 is shown in green. Intron positions are shown by arrows. aa, α-helixes; bb, β-strands. Asterisks indicate identity of amino acids in a position of the alignment; dots indicate functional similarity of amino acids in a position. (B) Domain structure of talins and kindlins, F, FERMT domain; PH, pleckstrin homology domain; V, variable loop.
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Figure 2: (A) Alignment of human talin 1, human kindlin 2, and human AFAP1L2 genes. The region of similarity with AFAP1L2 is shown in green. Intron positions are shown by arrows. aa, α-helixes; bb, β-strands. Asterisks indicate identity of amino acids in a position of the alignment; dots indicate functional similarity of amino acids in a position. (B) Domain structure of talins and kindlins, F, FERMT domain; PH, pleckstrin homology domain; V, variable loop.

Mentions: The results of BLASTP searches demonstrated that kindlin is a chimeric protein consisting of the N-terminal part of talin and the fragment of a PH domain–containing protein (Figure 2). With the exception of the PH domain–containing sequence, kindlins are homologous to talins (Figure 2 and Supplemental Figure S2). Sequence similarity between human talin 1 and K2 is highly significant (e < 10−18; Supplemental Figure S2). Moreover, in BLASTP searches for kindlins, metazoan talins appear as the next-most-similar family. This similarity suggests that kindlins originated from an ancestor of metazoan talins. This result is in agreement with another recently published study proposing that the FERM domain originated from a proto-talin protein in a unicellular or proto-multicellular organism (Ali and Khan, 2014).


Emergence and subsequent functional specialization of kindlins during evolution of cell adhesiveness.

Meller J, Rogozin IB, Poliakov E, Meller N, Bedanov-Pack M, Plow EF, Qin J, Podrez EA, Byzova TV - Mol. Biol. Cell (2014)

(A) Alignment of human talin 1, human kindlin 2, and human AFAP1L2 genes. The region of similarity with AFAP1L2 is shown in green. Intron positions are shown by arrows. aa, α-helixes; bb, β-strands. Asterisks indicate identity of amino acids in a position of the alignment; dots indicate functional similarity of amino acids in a position. (B) Domain structure of talins and kindlins, F, FERMT domain; PH, pleckstrin homology domain; V, variable loop.
© Copyright Policy - creative-commons
Related In: Results  -  Collection

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getmorefigures.php?uid=PMC4325847&req=5

Figure 2: (A) Alignment of human talin 1, human kindlin 2, and human AFAP1L2 genes. The region of similarity with AFAP1L2 is shown in green. Intron positions are shown by arrows. aa, α-helixes; bb, β-strands. Asterisks indicate identity of amino acids in a position of the alignment; dots indicate functional similarity of amino acids in a position. (B) Domain structure of talins and kindlins, F, FERMT domain; PH, pleckstrin homology domain; V, variable loop.
Mentions: The results of BLASTP searches demonstrated that kindlin is a chimeric protein consisting of the N-terminal part of talin and the fragment of a PH domain–containing protein (Figure 2). With the exception of the PH domain–containing sequence, kindlins are homologous to talins (Figure 2 and Supplemental Figure S2). Sequence similarity between human talin 1 and K2 is highly significant (e < 10−18; Supplemental Figure S2). Moreover, in BLASTP searches for kindlins, metazoan talins appear as the next-most-similar family. This similarity suggests that kindlins originated from an ancestor of metazoan talins. This result is in agreement with another recently published study proposing that the FERM domain originated from a proto-talin protein in a unicellular or proto-multicellular organism (Ali and Khan, 2014).

Bottom Line: Among the analyzed species, all metazoan lineages—but none of the premetazoans—had at least one kindlin-encoding gene, whereas talin was present in several premetazoan lineages.The presence of this segment enables K2 but not K3 to localize to focal adhesions.Thus emergence and subsequent functional specialization of kindlins allowed multicellular organisms to develop additional tissue-specific adaptations of cell adhesiveness.

View Article: PubMed Central - PubMed

Affiliation: Department of Molecular Cardiology, Joseph J. Jacobs Center for Thrombosis and Vascular Biology, Lerner Research Institute, Cleveland Clinic, Cleveland, OH 44195.

Show MeSH
Related in: MedlinePlus