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. 2021 Sep 14;43(2):329–365. doi: 10.1210/endrev/bnab030

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© The Author(s) 2021. Published by Oxford University Press on behalf of the Endocrine Society.

This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs licence (https://creativecommons.org/licenses/by-nc-nd/4.0/), which permits non-commercial reproduction and distribution of the work, in any medium, provided the original work is not altered or transformed in any way, and that the work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 4. — Dystrophin/costamere functional relationship. The costamere is composed of 2 protein complexes: the dystrophin-associated glycoprotein complex (DGC) and the integrin complex (IC). (A) Structural components of the DGC using color-coded labels for individual proteins or protein classes (DG, dystroglycan; DTNA, dystrobrevin-a; FKRP, Fukutin-related protein; NOS, nitric oxide synthase; SYCN, syncoilin). Dystrophin binds filamentous (F)-actin that in turn binds Z-line components of sarcomeres, physically linking the contractile machinery to the costamere and the extracellular matrix. Anchoring the costamere to the basement membrane depends upon proper glycosylation of different proteins including α-dystroglycan and the sarcoglycans. (B, C) Model for longitudinal and lateral force transmission based on contractile studies of healthy and dystrophic (mdx) mice. Color-coded labels in panel B apply to all panels representing the eccentric (lengthening) contraction cycle (Dys, dystrophin; ECM, extracellular matrix). The percentage of total specific force (numbers on right) transmitted laterally or longitudinally are represented by upper and lower yellow arrows, respectively, in each panel.