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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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Actin and Myosin in Muscle Contraction01:16

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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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Generation of Straight or Branched Actin Filaments01:14

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The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
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Overview of Myosin Structure and Function01:15

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Myosins are a family of molecular motor proteins, first identified in the skeletal muscles, where they are responsible for muscle contraction. Along with their role in muscle contraction, these proteins also play a role in the intracellular transport of molecules and vesicles. There are twenty-four classes of myosins based on their domain sequence and organization. Of the twenty-four, six classes (Myosin I, Myosin II, Myosin V, Myosin VI, Myosin VII, and Myosin X)  have been well...
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Overview of Skeletal Muscle01:15

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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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Microscopic Anatomy of Skeletal Muscles01:13

Microscopic Anatomy of Skeletal Muscles

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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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Methods to Study Mrp4-containing Macromolecular Complexes in the Regulation of Fibroblast Migration
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Probing muscle ankyrin-repeat protein (MARP) structure and function.

Alexander Shiang Lun1, Ju Chen, Stephan Lange

  • 1School of Medicine, University of California San Diego, La Jolla, California.

Anatomical Record (Hoboken, N.J. : 2007)
|August 16, 2014
PubMed
Summary
This summary is machine-generated.

Muscle ankyrin-repeat proteins (MARPs) dimerize antiparallelly via their coiled-coil domains and bind titin

Keywords:
MARPkinasemusclephosphorylationtitin

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Area of Science:

  • Muscle biology
  • Protein structure and function
  • Molecular cell biology

Background:

  • Muscle ankyrin-repeat proteins (MARPs) are crucial for cardiac and skeletal muscle function.
  • MARPs interact with sarcomeric proteins and modulate nuclear transcription factors.
  • MARP deregulation is linked to cardiac and skeletal myopathies, making them potential biomarkers.

Purpose of the Study:

  • To investigate the dimerization of MARPs and their interaction with titin.
  • To elucidate the structural basis of MARP-titin complex formation.
  • To understand the impact of MARP binding on titin phosphorylation and MARP posttranslational modifications.

Main Methods:

  • Coiled-coil domain analysis for MARP dimerization.
  • Protein complementation assays for MARP-titin interaction.
  • Analysis of PKA and PKC mediated phosphorylation of MARPs and titin.

Main Results:

  • MARPs homo- and hetero-dimerize in an antiparallel fashion through their coiled-coil domains.
  • MARP ankyrin repeats bind antiparallelly to titin's N2A region.
  • MARP binding influences PKA-mediated phosphorylation of titin and MARPs themselves are phosphorylated by PKA and PKC.

Conclusions:

  • The study clarifies the antiparallel structural organization of the MARP/titin complex in muscle.
  • Posttranslational modifications of MARPs and titin by kinases like PKA and PKC may alter muscle compliance.
  • Findings provide insights into disease mechanisms in myopathies related to MARP and titin function.