ライフサイエンスコーパス: CaM

1 CaM (calmodulin) mutations are associated with congenita

2 CaM adopts a highly compact conformation in which its op

3 CaM binds to and stimulates PI3Kalpha/Akt signaling, pro

4 CaM binds to the rib helix of TRPC4, which results in th

5 CaM is a Ca(2+)-sensitive regulatory protein that intera

6 CaM is shown to be absolutely necessary for efficient ac

7 CaM mutations were identified in 4 independent cases by

8 CaM oxidation alters regulation of a host of CaM's prote

9 CaM triggered an increase in hydrodynamic volume in both

10 M368 on KCa3.1 and M72 on CaM at the KCa3.1-CaM-BD/CaM interface.

11 uggest that in response to increased Ca(2+), CaM undergoes lobe switching that imposes a dramatic mut

12 Apo-CaM and Ca(2+)-CaM bind to distinct but overlapping sites in an elongat

13 Here we present the NMR structure of Ca(2+)-CaM bound to two molecules of ER-alpha (residues 287-305

14 as a result of rapid pacing triggers Ca(2+)-CaM dependent inactivation of RyR2.

15 terminant of Ca(2+) alternans, making Ca(2+)-CaM dependent regulation of RyR2 an important therapeuti

16 Ca(2+)-CaM induces rotations and intradomain shifts of individu

17 onstrate that inactivation of RyR2 by Ca(2+)-CaM is a major determinant of Ca(2+) alternans, making C

18 ce of Ca(2+)-CaM, which suggests that Ca(2+)-CaM is one of the many competing modulators of RyR2 gati

19 annel remains open in the presence of Ca(2+)-CaM, which suggests that Ca(2+)-CaM is one of the many c

20 K293 cells, supporting the model that Ca(2+)-CaM-dependent regulation of CNGC channel activity provid

21 of Ca(2+) alternans that incorporates Ca(2+)-CaM-dependent regulation of RyR2 and the L-type Ca(2+) c

22 Ca(2+).CaM binds primarily to the small lobe of the kinase doma

23 e to show that the C-terminal lobe of Ca(2+).CaM regulates membrane binding while the N-terminal lobe

24 To define the role of each lobe of Ca(2+).CaM, we utilized the natural product malbrancheamide as

25 roduct and its derivatives in probing Ca(2+).CaM-dependent hypertrophy.

26 in, we report the architecture of the Ca(2+).CaM-GRK5 complex determined by small-angle X-ray scatter

27 It was shown experimentally that Ca(2+)/CaM (holoCaM) binds to the CaMKII peptide with overwhelm

28 revealed that KN-93 binds directly to Ca(2+)/CaM and not to CaMKII.

29 The Ca(2+)/CaM binding triggers transphosphorylation of critical th

30 We present a crystal structure of Ca(2+)/CaM bound to the Na(V)1.4 IQ domain, which shows a bindi

31 l titration calorimetry revealed that Ca(2+)/CaM has higher affinity for the B domain than for the A

32 the peptides are disordered, whereas Ca(2+)/CaM imposed helical structure on both KCNQ A and B domai

33 We demonstrated that Ca(2+)/CaM interaction with the 2(nd) helix of the GTL1 N-termi

34 The effect of the variable linker on Ca(2+)/CaM sensitivity depended on the kinase and hub domains.

35 Together, these data suggest that Ca(2+)/CaM sensitivity in CaMKII is homolog dependent and inclu

36 We characterized the Ca(2+)/CaM sensitivity of hippocampal CaMKII variants spanning

37 Here we report a novel Ca(2+)/CaM signal transduction mechanism that allosterically re

38 The molecular mechanisms of Ca(2+)/CaM signal transduction processes and their functional s

39 of LAVP-mediated autoinhibiton during Ca(2+)/CaM stimulation.

40 binding would disrupt the ability of Ca(2+)/CaM to interact with CaMKII, effectively inhibiting CaMK

41 Accordingly, increased binding of Ca(2+)/CaM to PSD-95 induced by a chronic increase in Ca(2+) in

42 ctivated by calcium-bound calmodulin (Ca(2+)/CaM) through a direct binding mechanism involving a regu

43 of BdALMT12 activation by malate, and Ca(2+)/CaM, emphasizing that a complex regulatory network modul

44 des spontaneously form a complex with Ca(2+)/CaM, similar to previous reports of CaM binding KCNQ-AB

45 d found that CPK28 is a high affinity Ca(2+)/CaM-binding protein.

46 almodulin (CaM) and are transduced to Ca(2+)/CaM-binding transcription factors to directly regulate g

47 er, leading to osmotic stress-induced Ca(2+)/CaM-dependent activation (de-repression) of SDD1 express

48 ecause Nav1.6 and the multifunctional Ca(2+)/CaM-dependent protein kinase II (CaMKII) are independent

49 rve Myo1c Ser(701) phosphorylation by Ca(2+)/CaM-dependent protein kinase II (CaMKII), although CaMKI

50 They further suggest that other Ca(2+)/CaM-dependent, non-CaMKII activities should be considere

51 ructural plasticity is largely due to Ca(2+)/CaM-independent, autonomous activity.

52 ether, our results demonstrate that a Ca(2+)/CaM-regulated transcriptional switch on a trihelix trans

53 least two KN-93 molecules can bind to Ca(2+)/CaM.

54 Idelta-derived peptide for binding to Ca(2+)/CaM.

55 g kinase activation by competing with Ca(2+)/CaM.

56 aining detailed structural information for a CaM-K-Ras complex is still challenging.

57 amed NAD kinase-CaM dependent (NADKc), has a CaM-binding peptide located in its N-terminal region and

58 molecules to a specific residue of SdeA in a CaM-dependent manner.

59 computational, and biochemical analysis of a CaM complex with GRK5, revealing how CaM shapes GRK5 res

60 o be inhibited by exogenous application of a CaM inhibitor.

61 a(2+) transients, nuclear translocation of a CaM shuttle, and nuclear CaMKIV activation.

62 tem such that the concentration of an active CaM-binding TF is insensitive to the concentration of an

63 Additional CaMs that colocalize with the channel complex are unable

64 , the N53I substitution dramatically affects CaM's ability to reduce the open probability of the card

65 cells, we demonstrate that inhibition of Akt-CaM binding attenuated Akt activation.

66 n vivo local gene delivery approach to alter CaM function by directly injecting adenoviruses expressi

67 Altered CaM function also affected the recovery from inactivatio

68 es the impact on Ca(2+) alternans of altered CaM and RyR2 functions under 9 different experimental co

69 Although CaM binds over 100 proteins, practical limitations cause

70 on of Ser-500 is found to require Ca(2+) and CaM and is inhibited by mutations that compromise bindin

71 the physical interaction between the CBD and CaM.

72 he proximal C terminus of KCNQ4 channels and CaM, likely underlying Ca(2+)-dependent regulation of KC

73 suggest that the competition between CTM and CaM is influenced by calcium, allowing further fine-tuni

74 with three pyridazinone-based inhibitors and CaM.

75 he interaction between prenylated KRAS4b and CaM is enthalpically driven, and electrostatic interacti

76 etails of the interplay between membrane and CaM binding to Akt may help in the development of potent

77 We found that CaM-wild type and CaM-M37Q promoted Ca(2+) alternans and prolonged Ca(2+)

78 by this work can be used to explain how any CaM-binding TF decodes calcium signals to generate speci

79 Apo-CaM and Ca(2+)-CaM bind to distinct but overlapping site

80 ular Dynamics (MD) simulations show that apo-CaM exists in dynamic equilibrium with holo-like conform

81 as the mechanistic effects of arrhythmogenic CaM mutations.

82 nd that all structures of the arrhythmogenic CaM-N53I variant are highly similar to those of WT CaM.

83 Resolving this ambiguity is critical as CaM is enriched in subcellular domains where Ca(V) chann

84 rimetry and CBD-mimetic peptides, as well as CaM-agarose affinity pulldown of full-length recombinant

85 Similarly, when the amount of the available CaM in the cell was reduced, the short Ca(V)1.3(42A) iso

86 n KCa3.1 and M72 on CaM at the KCa3.1-CaM-BD/CaM interface.

87 and R335A/K342A, within a predicted BdALMT12 CaM-binding domain (CBD), also decreased the channels' a

88 However, the correlation between CaM structure and functional regulation of RyR in physio

89 yses to investigate the interactions between CaM and synthetic peptides corresponding to the A and B

90 molecular mechanism of the interplay between CaM and membrane binding is not established.

91 Both CaM and K-Ras4B HVR are highly flexible molecules, sugge

92 p to the hydrophobic pockets located at both CaM lobes further enhanced CaM-HVR complex stability.

93 stoichiometry; one TRPV6 tetramer binds both CaM lobes, which adopt a distinct head-to-tail arrangeme

94 Molecular details of both CaM and drug binding have remained elusive so far.

95 gating, and that (2) TRPV1 and Ca(2+)-bound CaM but not Ca(2+)-free CaM were preassociated in restin

96 s and dynamics of both apo- and Ca(2+)-bound CaM-N53I in solution.

97 a(2+)-dependent structural dynamics of bound CaM.

98 dependent on the conformation of RyR1-bound CaM.

99 Ca(2+)-dependent inactivation is effected by CaM's N-lobe binding outside the Na(V) C-terminal while

100 Using an explicit model of Ca2+, CaM, and seven highly-expressed hippocampal CaM binding

101 tection of autophosphorylated CaMKII by Ca2+/CaM may be an important mechanism for regulation of syna

102 Specifically, we explore how Ca2+/CaM-binding may both stabilize CaMKII subunit activation

103 Noting that Ca2+/CaM and protein phosphatases bind CaMKII at nearby or ov

104 In this work, we view Ca2+/CaM as a limiting resource in the signal transduction pa

105 lled "CaM trapping" phenomenon, wherein Ca2+/CaM may structurally exclude phosphatase binding and the

106 es, we compare model scenarios in which Ca2+/CaM and protein phosphatase do or do not structurally ex

107 st a functional mechanism for the so-called "CaM trapping" phenomenon, wherein Ca2+/CaM may structura

108 Calmodulin (CaM) conveys intracellular Ca(2+) signals to KCNQ (Kv7,

109 Calmodulin (CaM) has been suggested to selectively bind KRAS4b to ac

110 Calmodulin (CaM) is proposed to modulate activity of the skeletal mu

111 Calmodulin (CaM) mediates a wide range of biological responses to ch

112 Calmodulin (CaM) regulation of voltage-gated calcium (Ca(V)1-2) chan

113 The Ca(2+)/calmodulin (CaM)-dependent protein kinase II (CaMKII) was touted as

114 e current density of BdALMT12, a calmodulin (CaM) inhibitor reduced the Ca(2+)-dependent channel acti

115 ulates lysosome fusion through a calmodulin (CaM)-dependent mechanism.

116 has long been known to involve a calmodulin (CaM)/Ca(2+)-dependent NAD(+) kinase, the nature of the e

117 eceptor (DHPR), FKBP12/12.6, and calmodulin (CaM), as well as ions and small molecules including Ca(2

118 equires intracellular Ca(2+) and calmodulin (CaM).

119 Ca(2+)-binding proteins such as calmodulin (CaM) and recoverin, the molecular mechanisms are poorly

120 imal Kv7.1 C terminus (CT) binds calmodulin (CaM) and phosphatidylinositol-4,5-bisphosphate (PIP2), b

121 rane potentials and modulated by calmodulin (CaM) in a calcium-dependent manner.

122 s, the channels are regulated by calmodulin (CaM).

123 hannels (Ca(V)) form targets for calmodulin (CaM), which affects channel inactivation properties.

124 limits the availability of free calmodulin (CaM), the protein which activates CaMKII in the presence

125 How calmodulin (CaM) acts in KRAS-driven cancers is a vastly important q

126 In calmodulin (CaM)-rich environments, oncogenic KRAS plays a critical

127 Among various modulators, calmodulin (CaM) regulates RyR2 in a Ca(2+)-dependent manner.

128 associated with dissociation of calmodulin (CaM) from the IQ motif in Myo1c.

129 e found that the large number of calmodulin (CaM)-binding TFs or proteins in plant cells form a buffe

130 dynamic effects of oxidation on calmodulin (CaM), using peroxide and the Met to Gln oximimetic mutat

131 ded by the Ca(2+)-sensor protein calmodulin (CaM) and are transduced to Ca(2+)/CaM-binding transcript

132 acellular Ca(2+)-sensing protein calmodulin (CaM) are arrhythmogenic, yet their underlying mechanisms

133 conserved Ca(2+)-sensing protein calmodulin (CaM) cause severe cardiac arrhythmias, including catecho

134 The Ca(2+) -sensing protein calmodulin (CaM) has a central role in tuning Na(V) function to [Ca(

135 gulatory calcium-binding protein calmodulin (CaM) to the proximal C-terminus leads to the boosting of

136 d by the calcium-sensing protein calmodulin (CaM), which leads to nuclear translocation of GRK5 and p

137 s the eukaryote-specific protein calmodulin (CaM).

138 ryotic Ca(2+)-binding regulator, calmodulin (CaM).

139 Na(V)1.4) activity is subject to calmodulin (CaM) mediated Ca(2+)-dependent inactivation; no such ina

140 +) inhibits TRPV6 via binding to calmodulin (CaM), which mediates Ca(2+) -dependent inactivation.

141 alpha is modulated by Ca(2+) via calmodulin (CaM).

142 C termini, which associate with calmodulin (CaM), a universal calcium sensor.

143 Here, we imaged CaMKIIalpha-CaM association in single dendritic spines using a new F

144 ces spine structural plasticity, CaMKIIalpha-CaM association did not show further increase but sustai

145 e to a glutamate uncaging pulse, CaMKIIalpha-CaM association increases in ~0.1 s and decays over ~3 s

146 Due to its high methionine content, CaM is highly susceptible to oxidation by reactive oxyge

147 A Ca(2+)-dependent CaM N-lobe binding site previously identified in Na(V)1.

148 a or fetal demise combined with a documented CaM mutation.

149 Furthermore, CaM-F142L enhanced CaM-dependent RyR2 inhibition at the single channel leve

150 s located at both CaM lobes further enhanced CaM-HVR complex stability.

151 y directly injecting adenoviruses expressing CaM-wild type, a loss-of-function CaM mutation, CaM (1-4

152 ns, we observe that nSH2 prefers an extended CaM conformation, whereas cSH2 prefers a collapsed confo

153 erpinnings of lowered affinity of Ca(2+) for CaM in the presence of Ng13-49 by showing that the N-ter

154 in return increases the Ca(2+) affinity for CaM.

155 nding proteins, we find that competition for CaM binding serves as a tuning mechanism: the presence o

156 herefore screened a subset of plant CPKs for CaM binding and found that CPK28 is a high affinity Ca(2

157 A major interaction site for CaM resides in the C-terminal (CT) region, consisting of

158 show that this allosteric loop is vital for CaM regulation of the channels, facilitating cooperativi

159 rwhelmingly higher affinity than Ca(2+)-free CaM (apoCaM); the binding of CaMKII peptide to CaM in re

160 troscopy indicated the C-lobe of Ca(2+)-free CaM to interact with the KCNQ4 B domain (K(d) ~10-20 mum

161 PV1 and Ca(2+)-bound CaM but not Ca(2+)-free CaM were preassociated in resting live cells, while caps

162 expressing CaM-wild type, a loss-of-function CaM mutation, CaM (1-4), and a gain-of-function mutation

163 Furthermore, CaM-F142L enhanced CaM-dependent RyR2 inhibition at the

164 CaM, and seven highly-expressed hippocampal CaM binding proteins, we find that competition for CaM b

165 Cav2) and sodium channels possess homologous CaM-binding motifs, known as IQ motifs in their C termin

166 is of a CaM complex with GRK5, revealing how CaM shapes GRK5 response to calcium.

167 by which porcine RyR2 is modulated by human CaM through the structural determination of RyR2 under e

168 fer (TR-FRET) to study structural changes in CaM that may play a role in the regulation of RyR1.

169 Exposed glutamate residues in CaM (Glu-11, Glu-14, Glu-84, and Glu-87) form salt bridg

170 The shift in CaM-binding sites on RyR2 is controlled by Ca(2+) bindin

171 on or overexpression of a Ca(2+)-insensitive CaM mutant, reduced coupling, which is consistent with C

172 of a large family of diverse and interesting CaM kinases.

173 odulin and sheds new light on the intriguing CaM-binding properties of hundreds of plastid proteins,

174 In isolated CaM, at low Ca(2+), the two conformations of CaM are res

175 w that the beta-AR downstream protein kinase CaM kinase II (CaMKII) directly binds and phosphorylates

176 a(2+) This enzyme, which we named NAD kinase-CaM dependent (NADKc), has a CaM-binding peptide located

177 ur data provide new insights into the KRAS4b-CaM interaction and suggest a possible mechanism whereby

178 Transfection of cells with full-length CaM slightly increased the ability of estrogen to enhanc

179 It has been shown that the M125Q CaM mutant can mimic the functional effects of methionin

180 fficient for binding and defines the minimal CaM-binding motif.

181 and structural studies showed that multiple CaM molecules interact with distinct interfaces within c

182 We here localized multiple CaMs to the Ca(V) nanodomain by tethering either WT or m

183 However, when multiple CaMs are localized concurrently, Ca(V) channels preferen

184 nanodomain by tethering either WT or mutant CaM that lack Ca(2+)-binding capacity to the pore-formin

185 -wild type, a loss-of-function CaM mutation, CaM (1-4), and a gain-of-function mutation, CaM-M37Q, in

186 CaM (1-4), and a gain-of-function mutation, CaM-M37Q, into the anterior wall of the left ventricle o

187 solved the crystal structures of WT and N53I CaM in complex with the primary calmodulin-binding domai

188 finely tuned through the interactions of Ng, CaM, CaMKII, and PP1, providing a mechanism to precisely

189 f plastid proteins, despite the fact that no CaM or CaM-like proteins were identified in plastids.

190 ulation of L-type Ca(2+) channels by 2 novel CaM mutations affecting the same residue.

191 Genetic studies identified 2 novel CaM variants (CALM3-E141K in 2 cases; CALM1-E141V) and o

192 ion of KRAS4b, which might represent a novel CaM-binding motif.

193 This represents a novel CaM-induced regulatory mechanism of canonical TRP channe

194 ng sites for Ca(2+)-free and Ca(2+)-occupied CaM contain targets for mutations linked to long-QT synd

195 a crystal structure of fully Ca(2+)-occupied CaM, bound to the CT of Na(V)1.5.

196 We found that in the absence of CaM, the peptides are disordered, whereas Ca(2+)/CaM imp

197 hat results from the different affinities of CaM for CaMKII depending on the number of calcium ions b

198 d Ca(2+) is shown to enhance the affinity of CaM toward eEF-2K.

199 NMR analysis of CaM oxidation by peroxide offers further insights into t

200 which perhaps reflects occasional binding of CaM despite the presence of CTM.

201 CaM, at low Ca(2+), the two conformations of CaM are resolved, centered at 5 nm (closed) and 7 nm (op

202 istinct structural states (conformations) of CaM, each characterized by an interlobe distance and Gau

203 localization, can cooperate under control of CaM for selective substrate targeting by GRK5.

204 nd sharpens the Ca2+ frequency-dependence of CaM binding proteins.

205 Ca(2+)-dependent structural distribution of CaM bound to RyR1 is distinct from that of CaM bound to

206 mutations reside in the C-terminal domain of CaM and mostly affect Ca(2+)-coordinating residues.

207 ncreases Ca(2+) affinity for the C-domain of CaM by stabilizing the two Ca(2+) binding loops.

208 elops contacts with the C-terminal domain of CaM in about 2 ms.

209 elops contacts with the N-terminal domain of CaM more slowly, in about 8 ms.

210 +) binding loops particularly at C-domain of CaM, enabling Ca(2+) release.

211 d Ca(2+) binding affinity to the C-domain of CaM.

212 each of the two four-helix-bundle domains of CaM results in major conformational changes that create

213 CaM oxidation alters regulation of a host of CaM's protein targets, emphasizing the importance of und

214 a combination of selective (13)C labeling of CaM and M13, rapid mixing of CaM solutions with M13/Ca(2

215 We covalently labeled each lobe of CaM (N and C) with fluorescent probes and used intramole

216 st, expression of either the N- or C-lobe of CaM abrogated estrogen-stimulated transcription of the e

217 to Akt(PHD) displaces the C-terminal lobe of CaM but not the weakly binding N-terminal lobe.

218 ocalized unfolding of the C-terminal lobe of CaM, preventing the formation of a hydrophobic cluster o

219 low binding of the Ca(2+)-occupied C-lobe of CaM.

220 The two lobes of CaM bind to the same site on two separate ER-alpha molec

221 importance of understanding the mechanism of CaM oxidation in muscle degeneration and overall physiol

222 Despite progress in resolving mechanisms of CaM-Ca(V) feedback, the stoichiometry of CaM interaction

223 3)C labeling of CaM and M13, rapid mixing of CaM solutions with M13/Ca(2+) solutions, rapid freeze-qu

224 and domain in modulating the binding mode of CaM.

225 Such results support a paradigm of CaM-facilitated recovery from inactivation (CFRI).

226 oxidation-driven structural perturbation of CaM, with implications for RyR regulation and the decay

227 g to CaM and that the hydrophobic pockets of CaM can accommodate the prenylated region of KRAS4b, whi

228 +) production exclusively in the presence of CaM/Ca(2+) This enzyme, which we named NAD kinase-CaM de

229 h Ca(2+)/CaM, similar to previous reports of CaM binding KCNQ-AB domains that are linked together.

230 tol-4,5-bisphosphate (PIP2), but the role of CaM in channel function is still unclear, and its possib

231 Here, we studied the role of CaM kinase II-delta (CaMKIIdelta), which is known to be

232 ation and reveal a flexible stoichiometry of CaM binding to TRPV5.

233 of CaM-Ca(V) feedback, the stoichiometry of CaM interaction with Ca(V) channels remains ambiguous.

234 We determined a crystal structure of CaM bound to a peptide encompassing its binding site in

235 further insights into the susceptibility of CaM's Met residues to oxidation and the resulting struct

236 f CaM bound to RyR1 is distinct from that of CaM bound to RyRp.

237 y, these results add to our understanding of CaM-dependent regulation of RyR2 as well as the mechanis

238 ity to CNbeta1, decreasing its dependence on CaM, but also limited maximal enzyme activity through pe

239 a non-intuitive dependence of this effect on CaM concentration that results from the different affini

240 ions with S372 and M368 on KCa3.1 and M72 on CaM at the KCa3.1-CaM-BD/CaM interface.

241 unctional effects of methionine oxidation on CaM's regulation of the calcium release channel, ryanodi

242 id proteins, despite the fact that no CaM or CaM-like proteins were identified in plastids.

243 ibited by intracellular Ca(2+)i chelation or CaM inhibition.

244 (such as fibroblast growth factors (FGF) or CaM-dependent kinase II (CaMKII)) that can also modify c

245 nsensitive to the concentration of any other CaM-binding protein, thus maintaining specificity.

246 m is to place CaMKII in context of the other CaM kinases and then review certain aspects of this kina

247 Recently CaM was found to engage part of Na(V) 1.5 that is requir

248 es; CALM1-E141V) and one previously reported CaM pathogenic variant (CALM3-D130G) among 4 probands wi

249 We solved a structure of SidJ-CaM in complex with AMP and found that the ATP used in t

250 (V) channels depends exquisitely on a single CaM preassociated with the alpha-subunit carboxyl tail.

251 ered CaM to Ca(V)1.2 suggested that a single CaM sufficed for Ca(2+) feedback, yet biochemical, FRET,

252 We observed that a single CaM tethered to either the alpha or beta(2A) subunit tun

253 to signaling from the alpha-subunit-tethered CaM.

254 Functional studies that tethered CaM to Ca(V)1.2 suggested that a single CaM sufficed for

255 We found that CaM regulation of Ca(V)1.3 channels is dynamic on a minu

256 We found that CaM-wild type and CaM-M37Q promoted Ca(2+) alternans and

257 The CaM C-terminal lobe plugs the channel through a unique c

258 The CaM N and C domains bind independently to two helical re

259 The CaM N domain strongly activates GRK5 via ordering of the

260 antly altered such that they destabilize the CaM N-domain.

261 that create a potential binding site for the CaM binding domain of a target protein, which also under

262 The level of structural order in the CaM/M13/Ca(2+) complexes, indicated by (13)C ssNMR line

263 induced changes alter the interaction of the CaM N-domain with RyR2 and thereby likely cause the arrh

264 estigated the physiological relevance of the CaM-based regulation in planta, where stomatal closure,

265 strably affects the internal dynamics of the CaM-peptide complex.

266 angement or only slight perturbations of the CaM/KCNQ complex is as yet unclear.

267 g the CaM-B domain interactions via only the CaM C-lobe to also include the N-lobe.

268 26-residue peptide M13, which represents the CaM binding domain of skeletal muscle myosin light chain

269 increasing Ca(2+) molar ratios shifting the CaM-B domain interactions via only the CaM C-lobe to als

270 is and enzymatic assays, we propose that the CaM/Ca(2+)-dependent NAD(+) kinase activity found in pho

271 Thus, the CaM-peptide interface is an important determinant of the

272 fied RyR1, or a peptide corresponding to the CaM-binding domain of RyR (RyRp).

273 critical threonine residues proximal to the CaM-binding site leading to the autoactivated state of C

274 of Ca(V)1.3 channels can interfere with the CaM binding, thereby inhibiting channel activity and CDI

275 The interaction involved all three CaM domains including the central linker and both lobes.

276 RAS4b prenylation is required for binding to CaM and that the hydrophobic pockets of CaM can accommod

277 s on RyR2 is controlled by Ca(2+) binding to CaM, rather than to RyR2.

278 M (apoCaM); the binding of CaMKII peptide to CaM in return increases the Ca(2+) affinity for CaM.

279 ion induced both the formation of more TRPV1/CaM complexes and conformational changes.

280 The TRPV6-CaM complex exhibits 1:1 stoichiometry; one TRPV6 tetram

281 cause many models to include only one or two CaM-activated proteins.

282 ent functional stoichiometry, permitting two CaMs to mediate functional regulation.

283 omyocytes overexpressing mutant or wild-type CaM showed that both mutants impaired Ca(2+)-dependent i

284 How Na(V) -CaM, CaMKII and FGF/fibroblast growth factor homologous

285 When CaM is bound to full-length RyR1, either purified or in

286 r TR-FRET to assess interlobe distances when CaM is bound to RyR1 in SR membranes, purified RyR1, or

287 ct RyR2 wild type and mutant hearts, whereas CaM (1-4) exerted opposite effects.

288 ion and suggest a possible mechanism whereby CaM can regulate KRAS4b membrane localization.

289 Our findings support a model by which CaM binds to Akt to facilitate its translocation to the

290 ide a structure-based docking model by which CaM binds to prenylated KRAS4b.

291 However, the mechanism by which CaM can recognize and displace KRAS4b from the membrane

292 e binding outside the Na(V) C-terminal while CaM's C-lobe remains bound to the Na(V) C-terminal.

293 296, 299, 302, and 303), which explains why CaM binds two molecules of ER-alpha in a 1:2 complex and

294 ction changes in response to activation with CaM in the dimeric mutant, WT-holoenzyme, and a monomeri

295 on at the single channel level compared with CaM-WT.

296 AS4b forms a 2:1 stoichiometric complex with CaM in a nucleotide-independent manner.

297 sin light chain kinase, forms a complex with CaM in the presence of excess Ca(2+) on the millisecond

298 TRPV5 W583A mutant and TRPV5 in complex with CaM.

299 formational changes to form the complex with CaM.

300 3I variant are highly similar to those of WT CaM.