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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) Localization of K2, K3, and K2/3 chimeric proteins to focal adhesions was evaluated by colocalization with vinculin. Colocalization coefficient values ± SEM from different cells. Chimeras are numbered as in Figure 4A. (B) Diagram summarizing the contributions of different regions within K2 to its localization to focal adhesions based on the results in A. The colocalization coefficient of full-length K3 was subtracted from the coefficient of full-length K2, and the resulting value was assigned 100%. Kindlin with its domain structure is shown on top. F, FERM domain; PH, pleckstrin homology domain; V, variable domain.
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Figure 5: (A) Localization of K2, K3, and K2/3 chimeric proteins to focal adhesions was evaluated by colocalization with vinculin. Colocalization coefficient values ± SEM from different cells. Chimeras are numbered as in Figure 4A. (B) Diagram summarizing the contributions of different regions within K2 to its localization to focal adhesions based on the results in A. The colocalization coefficient of full-length K3 was subtracted from the coefficient of full-length K2, and the resulting value was assigned 100%. Kindlin with its domain structure is shown on top. F, FERM domain; PH, pleckstrin homology domain; V, variable domain.

Mentions: As anticipated, eGFP-K2 exhibited substantial colocalization with vinculin (colocalization coefficient R = 0.4). At the same time, the R values for eGFP-K3 or eGFP alone were eightfold lower (Figures 4, B–D, and 5A). Of interest, replacement of the N-terminal 241 or 441 amino acids of K3 with the corresponding sequences from K2 (1–265, construct 1; and 1– 461, construct 2; respectively) did not add to the extent of the vinculin colocalization of the resultant chimeras as compared with eGFPK3 or eGFP alone (Figures 4B and 5A). This result emphasized the importance of the remaining 261 C-terminal residues of K2 in the localization to focal adhesions. Indeed, when this C-terminal segment of K2 was fused to the N-terminal 441 amino acids of K3, the resultant chimeric protein (construct 6) gained the ability to colocalize with vinculin (R = 0.4; Figures 4C and 5A).


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) Localization of K2, K3, and K2/3 chimeric proteins to focal adhesions was evaluated by colocalization with vinculin. Colocalization coefficient values ± SEM from different cells. Chimeras are numbered as in Figure 4A. (B) Diagram summarizing the contributions of different regions within K2 to its localization to focal adhesions based on the results in A. The colocalization coefficient of full-length K3 was subtracted from the coefficient of full-length K2, and the resulting value was assigned 100%. Kindlin with its domain structure is shown on top. F, FERM domain; PH, pleckstrin homology domain; V, variable domain.
© Copyright Policy - creative-commons
Related In: Results  -  Collection

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getmorefigures.php?uid=PMC4325847&req=5

Figure 5: (A) Localization of K2, K3, and K2/3 chimeric proteins to focal adhesions was evaluated by colocalization with vinculin. Colocalization coefficient values ± SEM from different cells. Chimeras are numbered as in Figure 4A. (B) Diagram summarizing the contributions of different regions within K2 to its localization to focal adhesions based on the results in A. The colocalization coefficient of full-length K3 was subtracted from the coefficient of full-length K2, and the resulting value was assigned 100%. Kindlin with its domain structure is shown on top. F, FERM domain; PH, pleckstrin homology domain; V, variable domain.
Mentions: As anticipated, eGFP-K2 exhibited substantial colocalization with vinculin (colocalization coefficient R = 0.4). At the same time, the R values for eGFP-K3 or eGFP alone were eightfold lower (Figures 4, B–D, and 5A). Of interest, replacement of the N-terminal 241 or 441 amino acids of K3 with the corresponding sequences from K2 (1–265, construct 1; and 1– 461, construct 2; respectively) did not add to the extent of the vinculin colocalization of the resultant chimeras as compared with eGFPK3 or eGFP alone (Figures 4B and 5A). This result emphasized the importance of the remaining 261 C-terminal residues of K2 in the localization to focal adhesions. Indeed, when this C-terminal segment of K2 was fused to the N-terminal 441 amino acids of K3, the resultant chimeric protein (construct 6) gained the ability to colocalize with vinculin (R = 0.4; Figures 4C and 5A).

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