Abstract
Dystrophin is a cytoskeleton-linked membrane protein that binds to a larger multiprotein assembly called the dystrophin-associated glycoprotein complex (DGC). The deficiency of dystrophin or the components of the DGC results in the loss of connection between the cytoskeleton and the extracellular matrix with significant pathophysiological implications in skeletal and cardiac muscle as well as in the nervous system. Although the DGC plays an important role in maintaining membrane stability, it can also be considered as a versatile and flexible molecular complex that contribute to the cellular organization and dynamics of a variety of proteins at specific locations in the plasma membrane. This review deals with the role of the DGC in transmembrane signaling by forming supramolecular assemblies for regulating ion channel localization and activity. These interactions are relevant for cell homeostasis, and its alterations may play a significant role in the etiology and pathogenesis of various disorders affecting muscle and nerve function.
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Acknowledgements
This work was partially supported by funds from The National Council for Science and Technology (Conacyt, Mexico; Grant No. 221660) to R.F.
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232_2018_36_MOESM1_ESM.jpg
Suppl Fig 1. Molecular organization of voltage-gated Ca2+ (CaV), Na+ (NaV) and inward rectifying K+ (Kir) channels. The pore-forming α-subunit of NaV channels contains four domains each with six transmembrane segments with the N- and C-termini located in the cytoplasm. Ancillary β-subunits are single transmembrane proteins that co-assembles with the NaV α-subunit. CaV channels show a similar topology to NaV channels in their α-subunits but can be associated with different auxiliary subunits named α2δ, β and occasionally a γ-subunit with four transmembrane segments. BK channels comprise four ion-conducting α-subunits and in some tissues β auxiliary subunits. The α-subunits alone are sufficient to form a functional channel. These channels have an extra transmembrane domain that places its amino-terminal outside the cell. It also has a large intracellular carboxyl-terminus region that confers Ca2+ sensitivity to the channel complex. Kir channels contain two transmembrane (2 TM) and one pore-forming domain. The 2 TM domains assemble into a tetrameric ion-conducting Kir channel. Last, the membrane topology of cation channels of the transient receptor potential canonical (TRPC) family consists of six transmembrane spanning segments that are linked by short extracellular or intracellular loops (JPG 136 KB)
232_2018_36_MOESM2_ESM.jpg
Suppl Fig 2. Molecular organization of voltage-gated Ca2+ (CaV), Na+ (NaV) and inward rectifying K+ (Kir) channels. The pore-forming α-subunit of NaV channels contains four domains each with six transmembrane segments with the N- and C-termini located in the cytoplasm. Ancillary β-subunits are single transmembrane proteins that co-assembles with the NaV α-subunit. CaV channels show a similar topology to NaV channels in their α-subunits but can be associated with different auxiliary subunits named α2δ, β and occasionally a γ-subunit with four transmembrane segments. BK channels comprise four ion-conducting α-subunits and in some tissues β auxiliary subunits. The α-subunits alone are sufficient to form a functional channel. These channels have an extra transmembrane domain that places its amino-terminal outside the cell. It also has a large intracellular carboxyl-terminus region that confers Ca2+ sensitivity to the channel complex. Kir channels contain two transmembrane (2 TM) and one pore-forming domain. The 2 TM domains assemble into a tetrameric ion-conducting Kir channel. Last, the membrane topology of cation channels of the transient receptor potential canonical (TRPC) family consists of six transmembrane spanning segments that are linked by short extracellular or intracellular loops (JPG 54 KB)
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Leyva-Leyva, M., Sandoval, A., Felix, R. et al. Biochemical and Functional Interplay Between Ion Channels and the Components of the Dystrophin-Associated Glycoprotein Complex. J Membrane Biol 251, 535–550 (2018). https://doi.org/10.1007/s00232-018-0036-9
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DOI: https://doi.org/10.1007/s00232-018-0036-9