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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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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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The Role of Actin and Myosin in Non-muscle Cells01:10

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Actin and myosin or actomyosin filaments also play a significant role in cells other than those involved in muscle contraction (which occurs within the sarcomere of muscle cells). The mechanism of non-muscle cell contractile bundles was first observed in Dictyostelium and Acanthamoeba. In non-muscle cells, two bundles are commonly found: stress fibers and actomyosin adherence belts. These contractile bundles are smaller and less organized than the ones found in muscle cells. They  are held...
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The Sarcomere01:08

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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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ATP Driven Pumps III: V-type Pumps01:30

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V-type pumps are ATP-driven pumps found in the vacuolar membranes of plants, yeast, endosomal and lysosomal membranes of animal cells, plasma membranes of a few specialized eukaryotic cells, and some prokaryotes. They are also known as the V1Vo-ATPase, that couple ATP hydrolysis to transport protons against a concentration gradient.
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Myosins are multimeric motor proteins involved in various cellular processes such as migration, adhesion, and proliferation. Myosin II is the most common type in animal cells, which binds and cross-links actin filaments.
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Myosin-Specific Adaptations of In vitro Fluorescence Microscopy-Based Motility Assays
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Myosin XVIII.

Manuel H Taft1, Sharissa L Latham2,3

  • 1Institute for Biophysical Chemistry, Hannover Medical School, Hannover, Germany. Taft.Manuel@mh-hannover.de.

Advances in Experimental Medicine and Biology
|May 27, 2020
PubMed
Summary
This summary is machine-generated.

Class XVIII myosins, including Myo18A and Myo18B, function structurally, not as motors. Their role is vital for organizing cellular contractile machinery, and their dysregulation is linked to cancer and myopathies.

Keywords:
CancerGOLPH3GolgiMyofibrillogenesisMyosin-18SarcomereSurfactant protein A receptorTransportTumor suppressor

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Class XVIII myosins possess unique N- and C-terminal extensions, differing from conventional myosins.
  • They exhibit sequence similarity to class II myosins but function beyond typical contractile structures.

Purpose of the Study:

  • To elucidate the functional and structural roles of Class XVIII myosins.
  • To investigate the implications of Class XVIII myosin dysregulation in disease.

Main Methods:

  • Sequence comparison of active-site residues.
  • Biochemical data analysis.
  • Review of existing evidence on myosin function and disease association.

Main Results:

  • Class XVIII myosins lack ATPase-driven motor activity, indicating a structural function.
  • These myosins are found in diverse cellular locations, including lamella, focal adhesions, and the Golgi apparatus.
  • Myosin-18A (Myo18A) and Myo18B (Myo18B) dysregulation is associated with cancer and myopathies.

Conclusions:

  • Class XVIII myosins act as structural proteins essential for cellular contractile machinery organization.
  • Understanding their structural roles is crucial for comprehending muscle and nonmuscle cell function.
  • Myosin-18A and Myo18B are implicated in disease pathogenesis, highlighting their clinical relevance.