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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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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
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Actin filaments (F-actin) are composed of actin subunits. The dissociation of actin monomers can occur from either end of F-actin. The rate of dissociation is faster from the minus-end or the pointed end, where the actin subunits exist with a bound ADP, together known as ADP-actin. The depolymerization of F-actin is aided by proteins, including the actin-depolymerizing factor (ADF) and cofilin family of proteins, gelsolin, and glia maturation factor (GMF).
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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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The cytoskeleton is a complex dynamic structure performing varied functions based on cellular requirements. The adaptability of the individual filaments in the cytoskeleton determines their ability to perform various functions within the cell. It can undergo rapid reorganization during processes like cell division or remain stable for several hours as in the interphase. The adaptability of these filaments depends on stringent regulatory mechanisms. The microfilament and microtubules of the...
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Updated: Jun 13, 2025

Myosin-Specific Adaptations of In vitro Fluorescence Microscopy-Based Motility Assays
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Modulation of Filopodial Myosin Function.

Amy Crawford1,2, Jessica K Schwartz1,2, Emerson Hall1

  • 1Department of Genetics, Cell Biology, and Development, University of Minnesota, Minneapolis, MN.

Biorxiv : the Preprint Server for Biology
|June 12, 2025
PubMed
Summary
This summary is machine-generated.

MyTH-FERM myosins are crucial for filopodia initiation. A conserved mutation impacting their actin interaction impairs filopodia formation by disrupting cortical actin reorganization during the critical initiation step.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • MyTH-FERM (MF) myosins are vital for filopodia formation across diverse organisms.
  • Their precise roles in filopodia dynamics, particularly the myosin-actin interaction, remain incompletely understood.

Purpose of the Study:

  • To investigate the impact of altering the myosin-actin binding interface on filopodia formation.
  • To elucidate the function of MF myosins (DdMyo7 and Myo10) in filopodia initiation and elongation.

Main Methods:

  • Introduction of a conserved 'jordan' (jd) mutation (D to G substitution) into DdMyo7 and Myo10.
  • Quantitative analysis of filopodia number, length, and myosin tip enrichment in mutant and wild-type cells.
  • Assessment of Myo10 intrafilopodial motility velocity.

Main Results:

  • The 'jd' mutation significantly reduced filopodia initiation and myosin tip intensity for both DdMyo7 and Myo10.
  • DdMyo7 'jd' mutation did not affect filopodia length.
  • Myo10 'jd' mutation reduced motility velocity and tip levels but did not consistently alter filopodia length, challenging proposed roles in elongation.

Conclusions:

  • MF myosins primarily function in reorganizing actin filaments at the membrane-cortex interface during filopodia initiation.
  • The myosin-actin interaction is critical for the initiation step, rather than solely for filopodia elongation or membrane tension reduction.