scholarly journals The myosin superfamily at a glance

2012 ◽  
Vol 125 (7) ◽  
pp. 1627-1632 ◽  
Author(s):  
M. A. Hartman ◽  
J. A. Spudich
Keyword(s):  
Myosin Superfamily

scholarly journals A Millennial Myosin Census

2001 ◽  
Vol 12 (4) ◽  
pp. 780-794 ◽  
Author(s):  
Jonathan S. Berg ◽  
Bradford C. Powell ◽  
Richard E. Cheney
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Phylogenetic Analysis ◽  
Molecular Basis ◽  
General Interest ◽  
Class Iii ◽  
New Class ◽  
The Past ◽  
Human Genes ◽  
Complete Set ◽  
Myosin Superfamily

The past decade has seen a remarkable explosion in our knowledge of the size and diversity of the myosin superfamily. Since these actin-based motors are candidates to provide the molecular basis for many cellular movements, it is essential that motility researchers be aware of the complete set of myosins in a given organism. The availability of cDNA and/or draft genomic sequences from humans,Drosophila melanogaster, Caenorhabditis elegans, Arabidopsis thaliana,Saccharomyces cerevisiae, Schizosaccharomyces pombe, andDictyostelium discoideum has allowed us to tentatively define and compare the sets of myosin genes in these organisms. This analysis has also led to the identification of several putative myosin genes that may be of general interest. In humans, for example, we find a total of 40 known or predicted myosin genes including two new myosins-I, three new class II (conventional) myosins, a second member of the class III/ninaC myosins, a gene similar to the class XV deafness myosin, and a novel myosin sharing at most 33% identity with other members of the superfamily. These myosins are in addition to the recently discovered class XVI myosin with N-terminal ankyrin repeats and two human genes with similarity to the class XVIII PDZ-myosin from mouse. We briefly describe these newly recognized myosins and extend our previous phylogenetic analysis of the myosin superfamily to include a comparison of the complete or nearly complete inventories of myosin genes from several experimentally important organisms.

Regulation of myosin 5a and myosin 7a

2011 ◽  
Vol 39 (5) ◽  
pp. 1136-1141 ◽  
Author(s):  
Verl B. Siththanandan ◽  
James R. Sellers
Keyword(s):  
Cellular Function ◽  
Enzymatic Activities ◽  
Motor Domain ◽  
Present Review ◽  
Structural Basis ◽  
Ion Binding ◽  
Inactive State ◽  
Kinetic Mechanisms ◽  
Myosin Superfamily

The myosin superfamily is diverse in its structure, kinetic mechanisms and cellular function. The enzymatic activities of most myosins are regulated by some means such as Ca2+ ion binding, phosphorylation or binding of other proteins. In the present review, we discuss the structural basis for the regulation of mammalian myosin 5a and Drosophila myosin 7a. We show that, although both myosins have a folded inactive state in which domains in the myosin tail interact with the motor domain, the details of the regulation of these two myosins differ greatly.

scholarly journals The Formin Inhibitor, SMIFH2, Inhibits Members of the Myosin Superfamily

2020 ◽  
Vol 118 (3) ◽  
pp. 125a ◽  
Author(s):  
James R. Sellers ◽  
Shidong Shi ◽  
Yukako Nishimura ◽  
Fang Zhang ◽  
Rong Liu ◽  
...  
Keyword(s):  
Myosin Superfamily

scholarly journals Cryo-EM structures reveal specialization at the myosin VI-actin interface and a mechanism of force sensitivity

eLife ◽  
2017 ◽  
Vol 6 ◽  
Author(s):  
Pinar S Gurel ◽  
Laura Y Kim ◽  
Paul V Ruijgrok ◽  
Tosan Omabegho ◽  
Zev Bryant ◽  
...  
Keyword(s):  
Bound States ◽  
Motor Domain ◽  
Myosin Vi ◽  
Primary Sequence ◽  
Evolutionary Path ◽  
Force Sensitivity ◽  
Mechanochemical Cycle ◽  
Structural Diversification ◽  
Insight Into ◽  
Myosin Superfamily

Despite extensive scrutiny of the myosin superfamily, the lack of high-resolution structures of actin-bound states has prevented a complete description of its mechanochemical cycle and limited insight into how sequence and structural diversification of the motor domain gives rise to specialized functional properties. Here we present cryo-EM structures of the unique minus-end directed myosin VI motor domain in rigor (4.6 Å) and Mg-ADP (5.5 Å) states bound to F-actin. Comparison to the myosin IIC-F-actin rigor complex reveals an almost complete lack of conservation of residues at the actin-myosin interface despite preservation of the primary sequence regions composing it, suggesting an evolutionary path for motor specialization. Additionally, analysis of the transition from ADP to rigor provides a structural rationale for force sensitivity in this step of the mechanochemical cycle. Finally, we observe reciprocal rearrangements in actin and myosin accompanying the transition between these states, supporting a role for actin structural plasticity during force generation by myosin VI.

The Myosin Superfamily: An Overview

2004 ◽  
pp. 1-44 ◽  
Author(s):  
Michele C. Kieke ◽  
Margaret A. Titus
Keyword(s):  
Myosin Superfamily

The myosin superfamily inDrosophila melanogaster

1995 ◽  
Vol 273 (2) ◽  
pp. 104-117 ◽  
Author(s):  
Nancy Strom Morgan
Keyword(s):  
Myosin Superfamily
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