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Related Concept Videos

The Sarcomere01:08

The Sarcomere

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A sarcomere is a microscopic segment repeating in a myofibril. The sarcomere fundamentally consists of two main myofilaments: thick filaments called myosin and thin filaments called actin. These filaments interact by sliding past each other in response to stimulus. In addition to myosin and actin, several other proteins, such as tropomyosin, troponin, titin, nebulin, myomesin, α-actinin, and dystrophin, play crucial roles in regulating, structuring, and functioning of the sarcomere.
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Excitation-Contraction Coupling in Skeletal Muscles01:20

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Excitation-contraction coupling is a series of events that occur between generating an action potential and initiating a muscle contraction. It occurs at the triad, a structure found in skeletal muscle fibers that comprise a T-tubule and terminal cisternae of the sarcoplasmic reticulum on each side. These triads are visible in longitudinally sectioned muscle fibers. They are typically located at the A-I junction — the junction between the A and I bands of the sarcomere.
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Actin and Myosin in Muscle Contraction01:16

Actin and Myosin in Muscle Contraction

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Actin and myosin are contractile proteins that form the sarcomere found in skeletal muscle tissues for regulating muscle contraction. Actin, a globular contractile protein, interacts with myosin for muscle contraction. The skeletal tissue appears striped or striated under a microscope due to the repeated arrangement of contractile proteins actin and myosin along the length of myofibrils. Dark A bands and light I bands repeat along myofibrils, and the alignment of myofibrils in the cell causes...
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Microscopic Anatomy of Skeletal Muscles01:13

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Skeletal muscle cells, also called muscle fibers, are distinctly elongated, multi-nucleated, slender biological units. They are packed with specialized structures designed to facilitate their primary function, which is contraction.
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Overview of Skeletal Muscle

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Skeletal muscles are composed of a bundle of muscle fibers and are attached to bones through tendons. Each skeletal muscle fiber is a single muscle cell. The sarcolemma, the plasma membrane of a skeletal muscle cell, consists of a lipid bilayer and glycocalyx that supports muscle fibers. The sarcolemma extends into the muscle cells to form tubular structures called transverse or T-tubules. Each side of the T-tubules consists of a membrane-bound structure called the sarcoplasmic reticulum,...
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Cross-bridge Cycle01:26

Cross-bridge Cycle

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As muscle contracts, the overlap between the thin and thick filaments increases, decreasing the length of the sarcomere—the contractile unit of the muscle—using energy in the form of ATP. At the molecular level, this is a cyclic, multistep process that involves binding and hydrolysis of ATP, and movement of actin by myosin.
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SUMO system - a key regulator in sarcomere organization.

Arnab Nayak1, Mamta Amrute-Nayak1

  • 1Institute of Molecular and Cell Physiology, Hannover Medical School, Hannover, Germany.

The FEBS Journal
|February 26, 2020
PubMed
Summary

Small ubiquitin-like modifiers (SUMO) are crucial for muscle sarcomere assembly and maintenance. This pathway regulates protein homeostasis, impacting muscle function and preventing diseases like cardiomyopathies.

Keywords:
SENPSUMOepigeneticsmuscle atrophymyosin heavy chainsarcomere

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Area of Science:

  • Muscle physiology
  • Molecular biology
  • Biochemistry

Background:

  • Skeletal muscles, comprising 40% of body mass, generate force via actin-myosin interactions within sarcomeres.
  • Sarcomere organization is vital for muscle function; disruptions cause diseases like cardiomyopathies and cachexia.
  • Post-translational modifications (PTMs) regulate sarcomere formation and maintenance, adapting cells to environmental changes.

Purpose of the Study:

  • To review the small ubiquitin-like modifiers (SUMO) pathway's role in sarcomere assembly.
  • To explore the connection between SUMO-mediated protein homeostasis and sarcomere organization.
  • To discuss the implications for muscle-related pathologies.

Main Methods:

  • Literature review of the SUMOylation pathway.
  • Analysis of studies on protein homeostasis and sarcomere organization.
  • Examination of research linking SUMOylation to muscle diseases.

Main Results:

  • SUMOylation is a critical PTM for sarcomere assembly and maintenance.
  • The SUMO pathway influences protein homeostasis, essential for sarcomere structure.
  • Dysregulation of SUMOylation is implicated in muscle pathologies.

Conclusions:

  • The SUMO pathway is integral to sarcomere organization and muscle health.
  • Understanding SUMOylation's role offers insights into treating muscle diseases.
  • Targeting SUMOylation may present therapeutic strategies for muscle disorders.