Name: Myosins
Price: $98.70
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Author: Sellers, James R.
ISBN: 9780198505099

The term myosin refers to a diverse superfamily of molecular motors that are capable of either translocating actin filaments or of translocating vesicles or other cargo on fixed actin filaments. There are currently 15 distinct classes in the superfamily, and this book provides complete and up-to-date information on all of them. Since the publication of the first edition in 1995, a large amount of information has been printed about myosin, including the link of mutations in myosin to three human diseases. Myosin examines this new information in conjunction with helpful data provided by new techniques such as molecular imaging. This thoroughly revised edition is ideal for post-graduates and researchers in biochemistry, cell biology, molecular biology, and medicine who are seeking the latest information on the myosin superfamily of proteins.

Acknowledgements

xii

Abbreviations

xiii

Introduction

1

(36)

Definition of myosin

1

(1)

Classification of myosins

1

(8)

Domain structure of myosins

9

(5)

Myosin II

14

(6)

Subclassification of myosin II

14

(4)

Proteolytic fragmentation of myosin II

18

(2)

Myosin I

20

(3)

Myosin III

23

(1)

Myosin V

23

(4)

Myosin VI

27

(1)

Myosin VII

28

(1)

Myosin IX

29

(1)

Myosin XV

29

(1)

Other myosin classes

29

(2)

Myosin sequence analysis

31

(4)

Gene localization

31

(1)

Alternative splicing of myosin heavy chain genes

32

(3)

Purification of myosins

35

(2)

Myosin structure

37

(20)

The crystal structure of subfragment 1

37

(3)

Structure of the neck region of chicken skeletal muscle S-1

40

(1)

Scallop regulatory domain

41

(1)

Comparisons to other MgATPases

42

(1)

Structure of Dictyostelium motor domains with bound nucleotides

42

(6)

Low resolution structure of brush border myosin I from two-dimensional crystals

48

(1)

Model for the binding of myosin to actin

48

(4)

Model for the powerstroke

52

(1)

Sequence analysis of the myosin rod

52

(2)

Myosin II filament structure

54

(3)

Functional properties of myosin

57

(13)

MgATPase activity

57

(6)

Actin-activated MgATPase activity

58

(2)

Mechanical experiments on muscle fibres

60

(1)

Structural model of contraction

61

(1)

The nonphysiological high salt ATPase activity of myosin

62

(1)

Hydrolysis of other nucleotide triphosphates

62

(1)

Actin binding properties

63

(1)

Effect of nucleotide on actin binding

63

(1)

In vitro motility assays

63

(4)

In vitro mechanical studies

64

(3)

Functional studies of myosin in cells

67

(1)

Divalent cation binding

68

(2)

Covalent derivatization of myosin

70

(5)

Modification of Cys-707 and Cys-697

70

(1)

Cross-linking experiments

70

(3)

Photoaffinity nucleotide analogs

73

(1)

Modification of light chains

74

(1)

Regulation

75

(12)

Phosphorylation of vertebrate smooth and nonmuscle myosins

75

(6)

Structural basis for phosphorylation-dependent regulation

81

(1)

Phosphorylation-dependent regulation in some invertebrate myosins

82

(1)

Phosphorylation does not regulate vertebrate skeletal muscle myosin

82

(1)

Phosphorylation-dependent regulation in lower eukaryotic myosin II

83

(1)

Regulation of lower eukaryotic myosin I

84

(1)

Regulation of brush border myosin I

84

(1)

Regulation of myosin V

85

(1)

Regulation of molluscan myosin II by calcium binding

85

(2)

Myosin binding proteins

87

(4)

Mutations in myosin

91

(24)

Mutations in human β-cardiac myosin heavy chain

91

(6)

Mutations in the human myosin VA heavy chain gene are linked to Griscelli disease

97

(2)

Mutations in the human myosin heavy chains are linked to congenital deafness

99

(1)

Mouse mutant models

99

(1)

Mutations in the myosins of Dictyostelium discoideum

100

(5)

Mutations in yeast

105

(1)

Mutations in Drosophila

105

(1)

Mutations in C. elegans

105

(7)

Expression of myosins

112

(1)

Expression of mutant light chains in bacteria and exchange into myosin

112

(1)

Expression of active recombinant myosins in heterologous systems

112

(1)

Concluding remarks

113

(2)

Bibliography

115

(113)

Books on myosin

115

(1)

Reviews (references 1-136)

115

(4)

Structure of myosin (references 137-476)

119

(13)

Sequence analysis of myosin (references 477-603)

132

(5)

Interaction with actin (references 604-765)

137

(6)

ATPase activity of myosin (references 766-908)

143

(5)

Kinetics of actomyosin interaction (references 909-1045)

148

(5)

Nucleotide binding (references 1046-1137)

153

(4)

Mechanical studies of myosin in muscles and cells (references 1138-1287)

157

(6)

In vitro motility of myosin (references 1288-1403)

163

(4)

Myosin filament assembly and structure (references 1404-1547)

167

(5)

Phosphorylation of myosin (references 1548-1706)

172

(6)

Cation binding to myosin (references 1707-1736)

178

(1)

Myosin light chains (references 1737-1931)

179

(8)

Regulation of myosin (references 1932-2018)

187

(3)

Myosin expression, localization, and isoform diversity (references 2019-2193)

190

(7)

Covalent derivatization of myosin (references 2194-2284)

197

(3)

Proteolysis of myosin (references 2285-2358)

200

(3)

Myosin binding proteins (references 2359-2494)

203

(5)

Myosin mutations (references 2495-2646)

208

(7)

Unconventional myosins (references 2647-2836)

215

(7)

Methods for analysis of myosin (references 2837-2931)

222

(3)

Other references (references 2932-2942)

225

(1)

References added in proof (references 2943-2959)

226

(2)

Sequence alignment

228

Alignment of myosin motor domains

228

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Myosins

9780198505099

0198505094

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