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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) Left, table summarizing the presence of β-integrins, talins, and kindlins in metazoans and premetazoans. Database search was performed only for species with fully sequenced genomes. Right, schematic outline showing the phylogenetic positions of premetazoans expressing integrins (in red). The phylogenetic relationships are based on several recent phylogenetic studies (Sebe-Pedros et al., 2010, 2011; Suga et al., 2013). (B) Alignment of β-integrin cytoplasmic domains, emphasizing the membrane-proximal and the membrane-distant NPXY/F motifs responsible for interactions with talin and kindlin, respectively.
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Figure 1: (A) Left, table summarizing the presence of β-integrins, talins, and kindlins in metazoans and premetazoans. Database search was performed only for species with fully sequenced genomes. Right, schematic outline showing the phylogenetic positions of premetazoans expressing integrins (in red). The phylogenetic relationships are based on several recent phylogenetic studies (Sebe-Pedros et al., 2010, 2011; Suga et al., 2013). (B) Alignment of β-integrin cytoplasmic domains, emphasizing the membrane-proximal and the membrane-distant NPXY/F motifs responsible for interactions with talin and kindlin, respectively.

Mentions: There is accumulating evidence that some premetazoan organisms possess homologues of metazoan integrins. Thus four β-integrin–encoding genes have been found in the genome of Capsaspora owczarzaki (Sebe-Pedros et al., 2010; Sebe-Pedros and Ruiz-Trillo, 2010), one β-integrin in Thecamonas trahens (Sebe-Pedros et al., 2011), and one in Sphaeroforma arctica (Figure 1B). The functions of integrins in these organisms are not clear; however, it was hypothesized that together with intracellular components of the cell adhesion complex (α-actinin, vinculin, and talin), these were forerunners of integrin signaling in unicellular protists (Sebe-Pedros and Ruiz-Trillo, 2010). Although it is not known how the integrin functions evolved from unicellular to multicellular organisms, it is likely that this transition required an upgrade of intracellular integrin adhesion machinery.


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) Left, table summarizing the presence of β-integrins, talins, and kindlins in metazoans and premetazoans. Database search was performed only for species with fully sequenced genomes. Right, schematic outline showing the phylogenetic positions of premetazoans expressing integrins (in red). The phylogenetic relationships are based on several recent phylogenetic studies (Sebe-Pedros et al., 2010, 2011; Suga et al., 2013). (B) Alignment of β-integrin cytoplasmic domains, emphasizing the membrane-proximal and the membrane-distant NPXY/F motifs responsible for interactions with talin and kindlin, respectively.
© Copyright Policy - creative-commons
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC4325847&req=5

Figure 1: (A) Left, table summarizing the presence of β-integrins, talins, and kindlins in metazoans and premetazoans. Database search was performed only for species with fully sequenced genomes. Right, schematic outline showing the phylogenetic positions of premetazoans expressing integrins (in red). The phylogenetic relationships are based on several recent phylogenetic studies (Sebe-Pedros et al., 2010, 2011; Suga et al., 2013). (B) Alignment of β-integrin cytoplasmic domains, emphasizing the membrane-proximal and the membrane-distant NPXY/F motifs responsible for interactions with talin and kindlin, respectively.
Mentions: There is accumulating evidence that some premetazoan organisms possess homologues of metazoan integrins. Thus four β-integrin–encoding genes have been found in the genome of Capsaspora owczarzaki (Sebe-Pedros et al., 2010; Sebe-Pedros and Ruiz-Trillo, 2010), one β-integrin in Thecamonas trahens (Sebe-Pedros et al., 2011), and one in Sphaeroforma arctica (Figure 1B). The functions of integrins in these organisms are not clear; however, it was hypothesized that together with intracellular components of the cell adhesion complex (α-actinin, vinculin, and talin), these were forerunners of integrin signaling in unicellular protists (Sebe-Pedros and Ruiz-Trillo, 2010). Although it is not known how the integrin functions evolved from unicellular to multicellular organisms, it is likely that this transition required an upgrade of intracellular integrin adhesion machinery.

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