Related Experiment Video
Updated: Aug 3, 2026

08:57
Myosin-Specific Adaptations of In vitro Fluorescence Microscopy-Based Motility Assays
Published on: February 4, 2021
Myosin superfamily evolutionary history
Reid F Thompson1, George M Langford
1Department of Biological Sciences, Dartmouth College, Hanover, New Hampshire 03755, USA.
The Anatomical Record
|October 17, 2002
Summary
The myosin superfamily evolved early myosin groups (I and II), with later specialized classes emerging across diverse organisms. This evolutionary analysis reveals myosin gene distribution and loss patterns in eukaryotes.
Area of Science:
- Molecular Biology
- Evolutionary Biology
- Cell Biology
Background:
- The myosin superfamily comprises at least 18 classes in eukaryotic cells.
- Classification is based on phylogenetic analysis of head domains, offering functional insights but not evolutionary history.
Purpose of the Study:
- To establish the evolutionary history of the myosin superfamily.
- To analyze the representation of myosin gene families across a broad taxonomic spectrum.
Main Methods:
- Phylogenetic analysis of 232 myosin heavy chain amino acid sequences.
- Inclusion of 65 organisms from protist, plant, and animal kingdoms.
- Construction of an organismal phylogenetic tree using complementary taxonomic schemes.
Main Results:
- Myosins II and I are hypothesized as the earliest evolving myosin groups.
- Myosins V (animal) and XI (plant) diverged from a common myosin II-like ancestor.
- Specific myosin classes emerged at different evolutionary stages, with some having limited organismal distribution.
Conclusions:
- Early myosin families likely function as generalists, while later families evolved as specialists with restricted roles.
- Evolutionary data can predict the presence or absence of myosin genes in species.
- The study provides a framework for understanding myosin evolution and gene distribution.
Related Concept Videos
Protein Families
Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein families usually occur because of gene duplication, where an additional copy of a gene is inserted into the genome of an organism. Mutations that change the amino acids but still allow the protein to be properly synthesized, will lead to new protein family members. If these new proteins contain similar amino acids in key locations, protein...
Overview of Myosin Structure and Function
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 characterized.
Actin and Myosin in Muscle Contraction
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...
Role of Myosin in Cell Migration
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.
Myosin II is a hexamer comprising two heavy chains with globular heads and coiled-coil tails, two regulatory light chains, and two essential light chains. The ATPase sites on the myosin heads hydrolyze ATP, and the released phosphate generates the force for contraction. It is...
Myosin II is a hexamer comprising two heavy chains with globular heads and coiled-coil tails, two regulatory light chains, and two essential light chains. The ATPase sites on the myosin heads hydrolyze ATP, and the released phosphate generates the force for contraction. It is...
Protein Families
Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein families usually occur because of gene duplication, where an additional copy of a gene is inserted into the genome of an organism. Mutations that change the amino acids but still allow the protein to be properly synthesized, will lead to new protein family members. If these new proteins contain similar amino acids in key locations, protein...
The Sarcomere
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.
Each myosin...
Each myosin...

