Regulation and expression of metazoan unconventional myosins

doi:10.1016/S0074-7696(00)00005-X

International Review of Cytology

Volume 200, 2000, Pages 197-304

https://doi.org/10.1016/S0074-7696(00)00005-X Get rights and content

Abstract

Unconventional myosins are molecular motors that convert adenosine triphosphate (ATP) hydrolysis into movement along actin filaments. On the basis of primary structure analysis, these myosins are represented by at least 15 distinct classes (classes 1 and 3–16), each of which is presumed to play a specific cellular role. However, in contrast to the conventional myosins-2, which drive muscle contraction and cytokinesis and have been studied intensively for many years in both uni- and multicellular organisms, unconventional myosins have only been subject to analysis in metazoan systems for a short time. Here we critically review what is known about unconventional myosin regulation, function, and expression. Several points emerge from this analysis. First, in spite of the high relative conservation of motor domains among the myosin classes, significant differences are found in biochemical and enzymatic properties of these motor domains. Second, the idea that characteristic distributions of unconventional myosins are solely dependent on the myosin tail domain is almost certainly an oversimplication. Third, the notion that most unconventional myosins function as transport motors for membranous organelles is challenged by recent data. Finally, we present a scheme that clarifies relationships between various modes of myosin regulation.

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Regulation and expression of metazoan unconventional myosins

Abstract

J. Biol. Chem.

J. Biol. Chem.

J. Biol. Chem.

Curr. Opin. Cell Biol.

J. Mol. Biol.

Biochem. Biophys. Res. Commun.

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Binding of myosin I to membrane lipids

Nature

Propulsion of organelles isolated from Acanthamoeba along actin filaments by myosin-1

Nature

Phosphorylation of platelet myosin increases actin-activated myosin ATPase activity

Nature

Molecular Biology of the Cell

The Src homology domain 3 (SH3) of a yeast type I myosin, Myo5p, binds to verprolin and is required for targeting to sites of actin polarization

J. Cell Biol.

Characterization of unconventional MYO6, the human homologue of the gene responsible for deafness in Snell's waltzer mice

Human Mol. Genet.

The mouse Snell's waltzer deafness gene encodes an unconventional myosin required for structural integrity of inner-ear hair cells

Nature Genet.

Rat myr4 defines a novel subclass of myosin I: Identification, distribution, localization, and mapping of calmodulin-binding sites with differential calcium sensitivity

J. Cell Biol.

Quantification and localization of phosphorylated myosin I isoforms in Acanthamoeba castellanii

J. Cell Biol.

Differential localization of Acanthamoeba myosin I isoforms

J. Cell Biol.

Localization of myosin IC and myosin II in Acanthamoeba castellanii by indirect immunofluorescence and immunogold electron microscopy

J. Cell Biol.

Interaction of f-actin with synthetic peptides spanning the loop region of human cardiac β-myosin heavy chain containing Arg403

Eur. J. Biochem.

Purification and characterization of a mammalian myosin I

A myosin III from Limulus eyes is a clock-regulated phosphoprotein

J. Neurosci.

Localization and anchoring of mRNA in budding yeast

Curr. Biol.