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. 2018 Nov 29;131(23):jcs222042. doi: 10.1242/jcs.222042

Fig. 8.

Fig. 8.

Tpm3.5 plays an important role in lens biomechanical properties by maintaining mechanically stable F-actin networks. (A) In Tpm3/Δexon9d−/− mature lens fibers with reduced Tpm3.5, Tmod1 (green) is dissociated from the cell membrane and appears as cytoplasmic puncta. Loss of Tpm3.5 and Tmod1 from F-actin at the membrane likely leads to expansion of the β2-spectrin (blue) and α-actinin (red) F-actin networks. Competition between fimbrin and α-actinin may also lead to the loss of fimbrin from F-actin at the membrane. WT, wild-type. (B) In normal fiber cells, there is a balance between Tpm3.5- and Tmod1-mechanically-stabilized F-actin, the β2-spectrin–F-actin network and the α-actinin- or fimbrin-crosslinked F-actin networks. (C) In contrast, decreased levels of Tpm3.5 lead to depolymerization of Tmod1-capped F-actin. G-actin is then redistributed to other F-actin structures resulting in an expansion of the β2-spectrin and α-actinin networks. Not drawn to scale.