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Part of the myosin structure, atoms in the heavy chain are colored red on the left-hand side, and atoms in the light chains are colored orange and yellow.

Myosins are a large family of motor proteins found in eukaryotic tissues. They are responsible for actin-based motility.

Structure and Function

Sliding filament model of muscle contraction.

Domains

Most myosin molecules are composed of a head, neck, and tail domain.

• The head domain binds the filamentous actin, and uses ATP hydrolysis to generate force and to "walk" along the filament towards the (+) end (with the exception of one family member, myosin VI, which moves towards the (-) end).

• the neck domain acts as a linker and as a lever arm for transducing force generated by the catalytic motor domain. The neck domain can also serve as a binding site for myosin light chains which are distinct proteins that form part of a macromolecular complex and generally have regulatory functions.

• The tail domain generally mediates interaction with cargo molecules and/or other myosin subunits.

Nomenclature, evolution, and the family tree

The wide variety of myosin genes found throughout the eukaryotic phyla were named according to different schemes as they were discovered. The nomenclature can therefore be somewhat confusing when attempting to compare the functions of myosin proteins within and between organisms. Skeletal muscle myosin, the most conspicuous of the myosin superfamily due to its abundance in muscle fibers, was the first to be discovered. This protein makes up part of the sarcomere and forms macromolecular filaments composed of multiple myosin proteins. Similar filament-forming myosin proteins were found in cardiac muscle, smooth muscle, and non-muscle cells. However, beginning in the 1970s researchers began to discover new myosin genes encoding proteins that acted as monomers and were therefore entitled Class I myosins. These "unconventional myosins" were found in many tissues other than muscle and they contained divergent tail domains. These new superfamily members have been grouped according to phylogenetic relationships derived from a comparison of the amino acid sequences of their head domains, with each class being assigned a Roman numeral (see phylogenetic tree). The now diverse array of myosins has evolved from an ancestral precursor (see picture).

Myosin unrooted phylogenetic tree — click on image to see larger version (Source: http://www.mrc-lmb.cam.ac.uk/myosin/trees/trees.html)

Analysis of the amino acid sequences of different myosins shows great variability among the tail domains but strong conservation of head domain sequences. Presumably this is so the myosins may interact, via their tails, with a large number of different cargoes, while the goal in each case - to move along actin filaments - remains the same and therefore requires the same machinery in the motor. For example, the human genome contains over 40 different myosin genes.

These differences in shape also determine the speed at which myosins can move along actin filaments. The hydrolysis of ATP and the subsequent release of the phosphate group causes the "power stroke," in which the "lever arm" or "neck" region of the heavy chain is dragged forward. Since the power stroke always moves the lever arm by the same angle, the length of the lever arm determines how fast the cargo will move. A longer lever arm will cause the cargo to traverse a greater distance even though the lever arm undergoes the same angular displacement - just as a person with longer legs can move farther with each individual step. Myosin V, for example, has a much longer neck region than myosin II, and therefore moves 30-40 nanometers with each stroke as opposed to only 5-10.

Myosin I

Myosin I's function is unknown, but it is believed to be responsible for vesicle transport or the contraction vacuole of cells.^[1]

Myosin II

Myosin II is perhaps the best-studied example of these properties.

• Myosin II contains two heavy chains, each about 2000 amino acids in length, which constitute the head and tail domains. Each of these heavy chains contains the N-terminal head domain, while the C-terminal tails take on a coiled-coil morphology, holding the two heavy chains together (imagine two snakes wrapped around each other, such as in a caduceus). Thus, myosin II has two heads.

• It also contains 4 light chains (2 per head), which bind the heavy chains in the "neck" region between the head and tail.

In muscle cells, it is myosin II that is responsible for producing the contractile force. Here, the long coiled-coil tails of the individual myosin molecules join together, forming the thick filaments of the sarcomere. The force-producing head domains stick out from the side of the thick filament, ready to walk along the adjacent actin-based thin filaments in response to the proper chemical signals.

Genes in humans

Note that not all of these genes are active.

• Class I: MYO1A, MYO1B, MYO1C, MYO1D, MYO1E, MYO1F, MYO1G, MYO1H
• Class II: MYH1, MYH2, MYH3, MYH4, MYH6, MYH7, MYH7B, MYH8, MYH9, MYH10, MYH11, MYH13, MYH14, MYH15, MYH16
• Class III: MYO3A, MYO3B
• Class V: MYO5A, MYO5B, MYO5C
• Class VI: MYO6
• Class VII: MYO7A, MYO7B
• Class IX: MYO9A, MYO9B
• Class X: MYO10
• Class XV: MYO15A
• Class XVIII: MYO18A, MYO18B

Myosin light chains are distinct and have their own properties. They are not considered "myosins" but are components of the macromolecular complexes that make up the functional myosin enzymes.

• Light chain: MYL1, MYL2, MYL3, MYL4, MYL5, MYL6, MYL6B, MYL7, MYL9, MYLIP, MYLK, MYLK2, MYLL1

References

1. ^ Sutherland Macive (6/4/03). "Myosin I". Retrieved on 2007-05-23.

• T. Hodge and M.J.T.V. Cope (2000). "A Myosin Family Tree". Journal of Cell Science 113: 3353–3354.  Entrez PubMed 10984423
• Molecular Biology of the Cell. Alberts, Johnson, Lewis, Raff, Roberts, and Walter. 4th Edition. 949-952.

External links

Additional images

Phase 1	Phase 2	Phase 3	Phase 4
Myosin-painting	Myosin powerstroke

See also

• Motor protein
• Actin

External links

• Myosin Video A video of a moving myosin motor protein.
• MeSH Myosins
• The Myosin Homepage
• EC 3.6.4.1

Wikipedia content modification information:

• This page was last modified on 8 July 2008, at 22:32.

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