ライフサイエンスコーパス: myosin phosphatase

1 phatase, indicating that it does not inhibit myosin phosphatase.

2 eased phosphatase activity of phosphorylated myosin phosphatase.

3 ated and converted to a potent inhibitor for myosin phosphatase.

4 eloped two reagents with opposing effects on myosin phosphatase.

5 mutant of MBS that constitutively activates myosin phosphatase.

6 ion with the myosin-binding subunit (MBS) of myosin phosphatase.

7 ified a novel interaction between Nkx2.5 and myosin phosphatase.

8 cell cluster through localized inhibition of myosin phosphatase.

9 t dependent on myosin light chain kinase and myosin phosphatase.

10 osphorylation and subsequent inactivation of myosin phosphatase.

11 major substrates are myosin light chain and myosin phosphatase.

12 th siRNA prevented ATP-induced activation of myosin phosphatase.

13 We demonstrate that Myosin phosphatase, a complex of Protein phosphatase 1 a

14 7) and Ser(854)-Thr(855) phosphorylations on myosin phosphatase activity and contraction are unknown.

15 After 20 min of nitroprusside, myosin phosphatase activity had declined to basal levels

16 rial contractility is governed by regulating myosin phosphatase activity in response to agonist stimu

17 ation of nitroprusside at the same time that myosin phosphatase activity increased, suggesting that t

18 Myosin phosphatase activity is critical to the regulatio

19 atase in cell division, the possibility that myosin phosphatase activity may be altered during cell d

20 In vitro SMTNL1 suppresses myosin phosphatase activity through a substrate-directed

21 30-kDa subunit and resulted in inhibition of myosin phosphatase activity was not identified.

22 oprusside, when force declined, increases in myosin phosphatase activity, concurrent with cGMP-mediat

23 hat regulate actin cytoskeleton dynamics and myosin phosphatase activity, including focal adhesion ki

24 Myosin phosphatase activity, myosin light chain phosphor

25 e-dependent protein kinases had no effect on myosin phosphatase activity, whereas phosphorylation at

26 explain Ca2+ sensitization is inhibition of myosin phosphatase activity.

27 on of cGMP and a large transient increase in myosin phosphatase activity.

28 hospho-CPI-17 contributed to the increase in myosin phosphatase activity.

29 af-1 in the regulation of pathways involving myosin phosphatase activity.

30 antibody against MBS that is able to inhibit myosin phosphatase activity.

31 We have previously reported that myosin phosphatase also controls mitosis, apparently by

32 dressed how CPI-17 could selectively inhibit myosin phosphatase among other protein phosphatase-1 (PP

33 etion of the myosin binding subunit (Mbs) of myosin phosphatase, an antagonist of myosin II activatio

34 rotein-coupled receptor agonists can inhibit myosin phosphatase and cause smooth muscle cell contract

35 hoA/Rho kinase, whereas NO/cGMP can activate myosin phosphatase and cause smooth muscle cell relaxati

36 in situ, thereby regulating the activity of myosin phosphatase and contraction.

37 ectly bound to the Myosin-binding subunit of Myosin phosphatase and decreased Myosin dephosphorylatio

38 ooth muscle cells (VSMCs) via stimulation of myosin phosphatase and inhibition of Rho kinase activity

39 orylates the myosin binding subunit (MBS) of myosin phosphatase and inhibits the phosphatase activity

40 Par-1 binds to myosin phosphatase and phosphorylates it at a known inac

41 e, we describe the association of Raf-1 with myosin phosphatase and phosphorylation of the regulatory

42 tly binds both the myosin binding subunit of myosin phosphatase and RhoA and is localized to actin-my

43 6-kDa human protein that interacts with both myosin phosphatase and RhoA.

44 is a phosphorylation-dependent inhibitor of myosin phosphatase and, in response to agonists, Thr-38

45 ation was associated with high expression of myosin phosphatase and/or reduced myosin light-chain kin

46 targeting subunit (MYPT1) by the endogenous myosin phosphatase-associated kinase, MYPT1 kinase.

47 tase, suggesting that ROCK not only inhibits myosin phosphatase but also phosphorylates MLC directly

48 ed phosphorylation of myosin light chain and myosin phosphatase, but not LIM kinase, suggesting that

49 e regulatory myosin-binding subunit (MBS) of myosin phosphatase by Raf-1.

50 at PP1 phosphatase, the catalytic subunit of myosin phosphatase, can regulate PDE5 dephosphorylation.

51 ify PPP1R12A and PPP1CB, two subunits of the myosin phosphatase complex that antagonizes actomyosin c

52 e-Rho interacting protein as a member of the myosin phosphatase complex that directly binds both the

53 ing subunit 1 (MYPT1), two components of the myosin phosphatase complex, as HDAC7-associated proteins

54 n, and efficient operation of multimolecular myosin phosphatase complexes that include myosin IIA, pr

55 ctly dephosphorylating SA2, and the other is myosin phosphatase counteracting PLK1.

56 Myosin phosphatase dephosphorylates HDAC7 and promotes i

57 phila melanogaster myosin binding subunit of myosin phosphatase (DMYPT) in both processes.

58 The activation of myosin phosphatase during mitosis would enhance dephosph

59 Histamine stimulus triggers inhibition of myosin phosphatase-enhanced phosphorylation of myosin an

60 The inhibition of myosin phosphatase evokes smooth muscle contraction in t

61 Myosin phosphatase from smooth muscle consists of a cata

62 phosphatase catalytic subunit (PP1c) and the myosin phosphatase holoenzyme (MBP) were compared using

63 ase) and MEL-11 (a myosin-binding subunit of myosin phosphatase), impairs ovulation.

64 To explore the function of myosin phosphatase in cell division, the possibility tha

65 f a unique positive regulatory mechanism for myosin phosphatase in cell division.

66 induced by agents that inhibit smooth muscle myosin phosphatase in the absence of Ca2+ may be mediate

67 ds directly to the myosin binding subunit of myosin phosphatase in vivo in vascular smooth muscle cel

68 On the other hand, inhibition of myosin phosphatase increased MLC phosphorylation and blo

69 Consistent with this model, depletion of myosin phosphatase increased the velocity of ring moveme

70 phosphorylate the myosin binding subunit of myosin phosphatase, indicating that it does not inhibit

71 light chain phosphorylation or depletion of myosin phosphatase inhibit Myo-II contractile pulses, di

72 ROCK) Ca(2+)-sensitizing pathways leading to myosin phosphatase inhibition are critically involved in

73 on and inhibition of myosin phosphatase, the myosin phosphatase inhibitor CPI17, or direct phosphoryl

74 CPI-17, a myosin phosphatase inhibitor phosphoprotein, is phosphor

75 subunit 1, and protein kinase C-potentiated myosin phosphatase inhibitor) and integrins were reduced

76 rough which phorbol esters and smooth muscle myosin phosphatase inhibitors can induce contraction of

77 We propose that Myosin phosphatase is a crucial and tightly controlled r

78 Myosin phosphatase is a heterotrimeric holoenzyme consis

79 Inhibition of myosin phosphatase is critical for agonist-induced contr

80 Myosin phosphatase is localized not only at actin-myosin

81 The mechanisms by which myosin phosphatase is targeted to these loci are incompl

82 Myosin phosphatase is the primary effector of smooth mus

83 Myosin light chains are dephosphorylated by myosin phosphatase, leading to vascular smooth muscle re

84 KG I and its subsequent dephosphorylation by myosin phosphatase may be key steps in the regulation of

85 n response to vasoconstrictors by inhibiting myosin phosphatase (MLCP) activity and increasing myosin

86 Myosin phosphatase (MLCP) plays a critical regulatory ro

87 y is through inhibition of the smooth muscle myosin phosphatase (MLCP) that dephosphorylates the RLC

88 kinase I (PKG-Ialpha)-mediated activation of myosin phosphatase (MLCP).

89 This study identifies myosin phosphatase (MP) holoenzyme consisting of protein

90 Myosin phosphatase (MP) is a key regulator of myosin lig

91 The phosphatase activity of myosin phosphatase (MP) that dephosphorylates MLC is ina

92 Dephosphorylation is mediated by myosin phosphatase (MP), a complex that consists of a ca

93 This reaction is catalyzed by the holoenzyme myosin phosphatase (MP), which includes the catalytic su

94 activation involves PIP(2) hydrolysis and/or myosin phosphatase (MP).

95 Neither cellular myosin phosphatase, myosin light chain kinase, nor RhoA

96 myosin (pMLC), and the regulatory subunit of myosin phosphatase (MYPT1) were determined by Western bl

97 proteins, PP-1bp55, was homologous to human myosin phosphatase, MYPT2.

98 kinase C-potentiated inhibitory protein for myosin phosphatase of 17 kDa (CPI-17), prostate apoptosi

99 Furthermore, both overexpression of myosin phosphatase or inhibition of the myosin light-cha

100 with measurements of myosin light chain and myosin phosphatase phosphorylation.

101 ignificantly enhanced the phosphorylation of myosin phosphatase, promoted assembly of stress fibers,

102 BS, suggesting that M-RIP may play a role in myosin phosphatase regulation by RhoA.

103 A mutation in the myosin phosphatase regulator mypt1 results in a small ve

104 xpress the phosphatase inhibitor CPI-17, the myosin phosphatase regulatory (MYPT-1) and catalytic (PP

105 nd vasodilator pathways inhibit and activate myosin phosphatase, respectively.

106 This reduction in stress fiber myosin phosphatase-Rho interacting protein and myosin bi

107 We recently identified myosin phosphatase-Rho interacting protein as a member o

108 NA interference to silence the expression of myosin phosphatase-Rho interacting protein in human vasc

109 Myosin phosphatase-Rho interacting protein silencing red

110 Furthermore, myosin phosphatase-Rho interacting protein silencing res

111 kinase, nor RhoA activities were changed by myosin phosphatase-Rho interacting protein silencing.

112 We hypothesized that myosin phosphatase-Rho interacting protein targets myosi

113 These data support the importance of myosin phosphatase-Rho interacting protein-dependent tar

114 This myosin phosphatase-RhoA interacting protein, or M-RIP, i

115 translocation via a previously unrecognized myosin phosphatase-RhoA-interacting protein-dependent pa

116 Regulation of smooth muscle myosin phosphatase (SMPP-1M) is thought to be a primary

117 nd catalytic, 37-kDa, PP1c) of smooth muscle myosin phosphatase (SMPP-1M), we determined, in Triton-X

118 5-HT increased phosphorylation of myosin phosphatase subunit 1 (Mypt-1), a known ROCK targ

119 .5 from differentiating cells identified the myosin phosphatase subunits protein phosphatase 1beta an

120 CK activity in addition to the inhibition of myosin phosphatase, suggesting that ROCK not only inhibi

121 inhibited the consequent phosphorylation of myosin phosphatase target subunit (MYPT1) and the expres

122 iation between NF2 and its activator MYPT-1 (myosin phosphatase target subunit 1) in cardiomyocytes,

123 ractile response (myosin light chain kinase, myosin phosphatase target subunit 1, and protein kinase

124 is balance is achieved by interaction of the myosin phosphatase target subunit of myosin phosphatase

125 f myosin binding subunit 85 (MBS85), another myosin phosphatase targeting subunit (MYPT) family membe

126 We have found that the myosin phosphatase targeting subunit (MYPT) undergoes mi

127 We are using the tissue-specific splicing of myosin phosphatase targeting subunit (MYPT1) as a model

128 ho-associated kinase, that phosphorylate the myosin phosphatase targeting subunit (MYPT1) at Thr(697)

129 Alternative splicing of the smooth muscle myosin phosphatase targeting subunit (Mypt1) exon 23 (E2

130 on of MLCP induced by the phosphorylation of myosin phosphatase targeting subunit (MYPT1), a regulato

131 ooth muscle express distinct isoforms of the myosin phosphatase targeting subunit (MYPT1), and the is

132 phosphorylation and dephosphorylation of the myosin phosphatase targeting subunit (MYPT1).

133 Isoforms of the smooth muscle myosin phosphatase targeting subunit 1 (MYPT1) are gener

134 atase subunits protein phosphatase 1beta and myosin phosphatase targeting subunit 1 (Mypt1) as novel

135 ase inhibitor protein of 17 kDa (CPI-17) and myosin phosphatase targeting subunit 1 (MYPT1) phosphory

136 otein phosphatase 1 (PP1) regulatory subunit myosin phosphatase targeting subunit 1 (MYPT1) to activa

137 s I and II, and the total and phosphorylated myosin phosphatase targeting subunit 1 (MYPT1) were asse

138 One Cyclin A/Cdk1 substrate is myosin phosphatase targeting subunit 1 (MYPT1), and we s

139 tify protein phosphatase 1beta (PP1beta) and myosin phosphatase targeting subunit 1 (MYPT1), two comp

140 l adhesion kinase, myosin light chain 2, and myosin phosphatase targeting subunit 1 in primary human

141 MYPT1 (myosin phosphatase targeting subunit 1) is responsible f

142 en PP1 and a 34-kDa N-terminal domain of the myosin phosphatase targeting subunit MYPT1.

143 tion is due to the binding of p116Rip to the myosin phosphatase targeting subunit MYPT1.

144 tein phosphatase 1c, PP1c), a large subunit (myosin phosphatase targeting subunit, MYPT), and a small

145 Myosin phosphatase-targeting subunit 1 (MYPT1) binds to

146 is a heterotrimeric holoenzyme consisting of myosin phosphatase-targeting subunit 1 (MYPT1), a cataly

147 (CPI-17), prostate apoptosis response-4, or myosin phosphatase-targeting subunit 1 (MYPT1), all of w

148 rmation of a signaling complex of RhoA/ROCK2/myosin phosphatase-targeting subunit 1 (MYPT1).

149 ry target gene of SMTNL1 in these muscles is myosin phosphatase-targeting subunit 1 (MYPT1).

150 myosin IIA, protein phosphatase 1delta, and myosin phosphatase-targeting subunit 1, BIG1 and BIG2 se

151 been impaired, the levels of phosphorylated myosin phosphatase-targeting subunit 1, the regulatory s

152 rgeting subunit 1, the regulatory subunit of myosin phosphatase that is inhibited by Rho-kinase, were

153 Myosin phosphatase, the key enzyme controlling myosin li

154 ugh either phosphorylation and inhibition of myosin phosphatase, the myosin phosphatase inhibitor CPI

155 e regulated by myosin light-chain kinase and myosin phosphatase through phosphorylation and dephospho

156 o interacting protein-dependent targeting of myosin phosphatase to stress fibers for regulating myosi

157 Targeting of myosin phosphatase to the cell membrane precedes the dis

158 phosphatase-Rho interacting protein targets myosin phosphatase to the contractile apparatus to depho

159 the epithelium must ;relax', via activity of myosin phosphatase, to allow for normal hindbrain morpho

160 ntracellular Ca2+, but involve activation of myosin phosphatase via a novel G-protein-coupled mechani

161 y and microtubule acetylation is mediated by myosin phosphatase via controlled activation and deactiv

162 ro experiments showing the activation of the myosin phosphatase via heterophilic leucine zipper inter

163 The MYPT1 regulatory subunit of myosin phosphatase was concentrated only in the fraction

164 Furthermore, the activity of myosin phosphatase was increased more than twice and it

165 The regulatory subunit (MYPT1) of the myosin phosphatase was phosphorylated in PC3 cells and H

166 of the myosin phosphatase target subunit of myosin phosphatase with either myosin light chain or HDA