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Research Paper on The Assembly of the Sarcoplasmic Reticulum-Plasma Membrane Junctions in Striated Muscle: Roles of Junctophilin1 and Junctophilin2

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Research Paper on The Assembly of the Sarcoplasmic Reticulum-Plasma Membrane Junctions in Striated Muscle: Roles of Junctophilin1 and Junctophilin2

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Title: The Assembly of the Sarcoplasmic Reticulum-Plasma Membrane Junctions in Striated Muscle: Roles of Junctophilin1 and Junctophilin2

Abstract: A massive release of calcium from the sarcoplasmic reticulum (SR) into the cytoplasm causes contraction of striated muscle. The voltage-gated calcium channels CaV1.1 (in skeletal muscle) and CaV1.2 (in cardiac muscle) in the plasma membrane (PM) sense membrane depolarization, which then activates the calcium-releasing channel ryanodine receptor (RyR) embedded in the SR membrane. At specialized locations, the SR-PM junctions, where these two compartments are in close proximity, cross-communication between channels in the PM and the SR occurs. The SR-PM junctions in striated muscle are formed and stabilized by the proteins Junctophilin1 and Junctophilin2, which also actively take part in the recruitment of CaV and RyR, the two key players in intracellular calcium release. In light of recently published data and recent developments in protein structure prediction, this brief review focuses on the functions of junctophilins 1 and 2 in the formation and organization of SR-PM junctions in skeletal and cardiac muscle as well as the functional ramifications of their absence or dysfunction in striated muscle.

Keywords: striated muscle; ER-PM junctions; junctophilins; excitation-contraction coupling

Paper Quality: SCOPUS / Web of Science Level Research Paper

Subject: Biomolecules

Writer Experience: 20+ Years

Plagiarism Report: Turnitin Plagiarism Report will be less than 10%

Restriction: Only one author may purchase a single paper. The paper will then indicate that it is out of stock.

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A turnitin plagiarism report of less than 10% in a pdf file and a full research paper in a word document.

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