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Journal articles on the topic 'CAMP induced conformational changes'

Author: Grafiati

Published: 9 March 2023

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1

Introini, Bianca, Andrea Saponaro, Alessio Bonucci, Oliver Rauh, Francesca Cantini, Lucia Banci, Gerhard Thiel, and Anna Moroni. "Camp-Induced Conformational Changes in the C-Linker of HCN4." Biophysical Journal 118, no. 3 (February 2020): 419a. http://dx.doi.org/10.1016/j.bpj.2019.11.2365.

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2

Baichoo, Noel, and Tomasz Heyduk. "Mapping Conformational Changes in a Protein: Application of a Protein Footprinting Technique to cAMP-Induced Conformational Changes in cAMP Receptor Protein†." Biochemistry 36, no. 36 (September 1997): 10830–36. http://dx.doi.org/10.1021/bi970714v.

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3

Hinds, M. G., R. W. King, and J. Feeney. "19F n.m.r. studies of conformational changes accompanying cyclic AMP binding to 3-fluorophenylalanine-containing cyclic AMP receptor protein from Escherichia coli." Biochemical Journal 287, no. 2 (October 15, 1992): 627–32. http://dx.doi.org/10.1042/bj2870627.

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A fluorine-containing analogue of the cyclic AMP (cAMP) receptor protein (CRP) from Escherichia coli was prepared by biosynthetic incorporation of 3-fluorophenylalanine (3-F-Phe). 19F n.m.r. studies on this protein have provided direct evidence for cAMP-induced conformational changes not only within the cAMP-binding domain but also within the hinge region connecting the cAMP-binding domain to the DNA-binding headpiece. At 313 K, the 19F n.m.r. spectrum of [3-F-Phe]CRP showed five signals corresponding to the five phenylalanine residues as expected for a symmetrical dimer. Proteolysis of [3-F-Phe]CRP with subtilisin produced a fragment (the alpha-fragment) containing the cAMP-binding domain. The alpha-fragment contains all the phenylalanines except for Phe-136, a residue located in the hinge region. By comparing the 19F spectra of [3-F-Phe]CRP and its alpha-fragment, the signal for Phe-136 was assigned. The chemical shifts of the corresponding signals in the two spectra are similar, indicating that the alpha-fragment retains the structure it has in the intact protein. The largest cAMP-induced shift was observed for the signal from Phe-136 providing direct evidence for a conformational change in the hinge region. However, whereas binding of a single cAMP molecule to a CRP dimer is known to be sufficient to activate the DNA binding, the n.m.r. data indicate that the hinge region does not have the same conformation in both subunits when only one cAMP molecule is bound.

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4

Cheng, Xiaodong, Shmuel Shaltiel, and Susan S. Taylor. "Mapping Substrate-Induced Conformational Changes in cAMP-Dependent Protein Kinase by Protein Footprinting†." Biochemistry 37, no. 40 (October 1998): 14005–13. http://dx.doi.org/10.1021/bi981057p.

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5

Introini, Bianca, Andrea Saponaro, Alessio Bonucci, Oliver Rauh, Francesca Cantini, Lucia Banci, Gerhard Thiel, and Anna Moroni. "Chimeric HCN Channels for Studying Camp-Induced Conformational Changes in the C-Linker." Biophysical Journal 116, no. 3 (February 2019): 301a. http://dx.doi.org/10.1016/j.bpj.2018.11.1631.

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6

Prade, Lars, Richard A. Engh, Andreas Girod, Volker Kinzel, Robert Huber, and Dirk Bossemeyer. "Staurosporine-induced conformational changes of cAMP-dependent protein kinase catalytic subunit explain inhibitory potential." Structure 5, no. 12 (December 1997): 1627–37. http://dx.doi.org/10.1016/s0969-2126(97)00310-9.

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7

Tworzydło, Magdalena, Agnieszka Polit, Jan Mikołajczak, and Zygmunt Wasylewski. "Fluorescence quenching and kinetic studies of conformational changes induced by DNA and cAMP binding to cAMP receptor protein from Escherichia coli." FEBS Journal 272, no. 5 (February 17, 2005): 1103–16. http://dx.doi.org/10.1111/j.1742-4658.2005.04540.x.

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8

Fic, Ewelina, Agnieszka Polit, and Zygmunt Wasylewski. "Kinetic and Structural Studies of the Allosteric Conformational Changes Induced by Binding of cAMP to the cAMP Receptor Protein fromEscherichia coli†." Biochemistry 45, no. 2 (January 2006): 373–80. http://dx.doi.org/10.1021/bi051586a.

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9

López, Ximena, Rosalba Escamilla, Paola Fernández, Yorley Duarte, Fernando González-Nilo, Nicolás Palacios-Prado, Agustín D. Martinez, and Juan C. Sáez. "Stretch-Induced Activation of Pannexin 1 Channels Can Be Prevented by PKA-Dependent Phosphorylation." International Journal of Molecular Sciences 21, no. 23 (December 2, 2020): 9180. http://dx.doi.org/10.3390/ijms21239180.

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Pannexin 1 channels located in the cell membrane are permeable to ions, metabolites, and signaling molecules. While the activity of these channels is known to be modulated by phosphorylation on T198, T308, and S206, the possible involvement of other putative phosphorylation sites remains unknown. Here, we describe that the activity of Panx1 channels induced by mechanical stretch is reduced by adenosine via a PKA-dependent pathway. The mechanical stretch-induced activity—measured by changes in DAPI uptake—of Panx1 channels expressed in HeLa cell transfectants was inhibited by adenosine or cAMP analogs that permeate the cell membrane. Moreover, inhibition of PKA but not PKC, p38 MAPK, Akt, or PKG prevented the effects of cAMP analogs, suggesting the involvement of Panx1 phosphorylation by PKA. Accordingly, alanine substitution of T302 or S328, two putative PKA phosphorylation sites, prevented the inhibitory effect of cAMP analogs. Moreover, phosphomimetic mutation of either T302 or S328 to aspartate prevented the mechanical stretch-induced activation of Panx1 channels. A molecular dynamics simulation revealed that T302 and S328 are located in the water–lipid interphase near the lateral tunnel of the intracellular region, suggesting that their phosphorylation could promote conformational changes in lateral tunnels. Thus, Panx1 phosphorylation via PKA could be modulated by G protein-coupled receptors associated with the Gs subunit.

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10

Buechler, Joseph A., Thomas A. Vedvick, and Susan S. Taylor. "Differential labeling of the catalytic subunit of cAMP-dependent protein kinase with acetic anhydride: substrate-induced conformational changes." Biochemistry 28, no. 7 (April 4, 1989): 3018–24. http://dx.doi.org/10.1021/bi00433a042.

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11

Fic, Ewelina, Andrzej Górecki, and Zygmunt Wasylewski. "Fluorescence Quenching Studies of Conformational Changes Induced by cAMP and DNA Binding to Heterodimer of Cyclic AMP Receptor Protein from Escherichia coli." Protein Journal 26, no. 7 (May 16, 2007): 457–66. http://dx.doi.org/10.1007/s10930-007-9085-0.

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12

KRAAKMAN, Leon S., Joris WINDERICKX, Johan M. THEVELEIN, and Johannes H. DE WINDE. "Structure–function analysis of yeast hexokinase: structural requirements for triggering cAMP signalling and catabolite repression." Biochemical Journal 343, no. 1 (September 24, 1999): 159–68. http://dx.doi.org/10.1042/bj3430159.

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In baker's yeast (Saccharomyces cerevisiae) the hexokinases PI (Hxk1) and PII (Hxk2) are required for triggering of the activation of the Ras-cAMP pathway and catabolite repression. Specifically, Hxk2 is essential for the establishment of glucose repression, whereas either Hxk1 or Hxk2 can sustain fructose repression. Previous studies have suggested that the extent of glucose repression is inversely correlated with hexokinase catalytic activity and hence with an adequate elevation of intracellular sugar phosphate levels. However, several lines of evidence indicate that glucose 6-phosphate is not the trigger of catabolite repression in yeast. In the present study we employed site-directed mutagenesis of amino acids important for the binding of sugar and ATP, for efficient phosphoryl transfer and for the closure of the substrate-binding cleft, to obtain an insight into the structural requirements of Hxk2 for sugar-induced signalling. We show that the ATP-binding Lys-111 is not essential for catalysis in vivo or for signal triggering. Substitution of the catalytic-centre Asp-211 caused loss of catalytic activity, but high-affinity sugar binding was retained. However, this was not sufficient to cause cAMP activation nor catabolite repression. Mutation of Ser-158 abrogated glucose-induced, but not fructose-induced, repression. Moreover, 2-deoxyglucose sustained repression despite an extremely low catalytic activity. We conclude that the establishment of catabolite repression is dependent on the onset of the phosphoryl transfer reaction on hexokinase and is probably related to the stable formation of a transition intermediate and concomitant conformational changes within the enzyme. In contrast, the role of Hxk2 in Ras-cAMP activation seems to be directly connected to its catalytic function. The implications of this model are discussed.

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13

Lisenbee, Cayle S., Kaleeckal G. Harikumar, and Laurence J. Miller. "Mapping the Architecture of Secretin Receptors with Intramolecular Fluorescence Resonance Energy Transfer Using Acousto-Optic Tunable Filter-Based Spectral Imaging." Molecular Endocrinology 21, no. 8 (August 1, 2007): 1997–2008. http://dx.doi.org/10.1210/me.2007-0063.

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Abstract The molecular structure and agonist-induced conformational changes of class II G protein-coupled receptors are poorly understood. In this work, we developed and characterized a series of dual cyan fluorescent protein (CFP)-tagged and yellow fluorescent protein (YFP)-tagged secretin receptor constructs for use in various functional and fluorescence analyses of receptor structural variants. CFP insertions within the first or second intracellular loop domains of this receptor were tolerated poorly or partially, respectively, in receptors tagged with a carboxyl-terminal yellow fluorescent protein that itself had no effect on secretin binding or cAMP production. A similar CFP insertion into the third intracellular loop resulted in a plasma membrane-localized receptor that bound secretin and signaled normally. This fully active third-loop variant exhibited a significant decrease in fluorescence resonance energy transfer signals that were recorded with an acousto-optic tunable filter microscope after exposure to secretin agonist but not to a receptor antagonist. These data demonstrate changes in the relative positions of intracellular structures that support a model for secretin receptor activation.

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14

Persat, Alexandre, Yuki F. Inclan, Joanne N. Engel, Howard A. Stone, and Zemer Gitai. "Type IV pili mechanochemically regulate virulence factors inPseudomonas aeruginosa." Proceedings of the National Academy of Sciences 112, no. 24 (June 3, 2015): 7563–68. http://dx.doi.org/10.1073/pnas.1502025112.

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Bacteria have evolved a wide range of sensing systems to appropriately respond to environmental signals. Here we demonstrate that the opportunistic pathogenPseudomonas aeruginosadetects contact with surfaces on short timescales using the mechanical activity of its type IV pili, a major surface adhesin. This signal transduction mechanism requires attachment of type IV pili to a solid surface, followed by pilus retraction and signal transduction through the Chp chemosensory system, a chemotaxis-like sensory system that regulates cAMP production and transcription of hundreds of genes, including key virulence factors. Like other chemotaxis pathways, pili-mediated surface sensing results in a transient response amplified by a positive feedback that increases type IV pili activity, thereby promoting long-term surface attachment that can stimulate additional virulence and biofilm-inducing pathways. The methyl-accepting chemotaxis protein-like chemosensor PilJ directly interacts with the major pilin subunit PilA. Our results thus support a mechanochemical model where a chemosensory system measures the mechanically induced conformational changes in stretched type IV pili. These findings demonstrate thatP. aeruginosanot only uses type IV pili for surface-specific twitching motility, but also as a sensor regulating surface-induced gene expression and pathogenicity.

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15

BOTTOMLEY, Joanna R., Alastair R. HAWKINS, and Colin KLEANTHOUS. "Conformational changes and the role of metals in the mechanism of type II dehydroquinase from Aspergillus nidulans." Biochemical Journal 319, no. 1 (October 1, 1996): 269–78. http://dx.doi.org/10.1042/bj3190269.

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We have investigated the involvement of metal ions and conformational changes in the elimination reaction catalysed by type II dehydroquinase from Aspergillus nidulans. Mechanistic comparisons between dehydroquinases and aldolases raised the possibility that, by analogy with type II aldolases, type II dehydroquinases may require bivalent metal ions for activity. This hypothesis was tested by a combination of metal analysis, effects of metal chelators and denaturation/renaturation experiments, all of which failed to show any evidence that type II dehydroquinases are metal-dependent dehydratases. Analysis of native and refolded enzyme by electron microscopy showed that the dodecameric type II enzyme from A. nidulans adopts a ring-like structure similar to that of glutamine synthase, suggesting an arrangement of two hexameric rings stacked on top of one another. Evidence for a ligand-induced conformational change came from both chemical modification and proteolysis experiments. Inactivation data with the arginine-specific reagent phenylglyoxal indicated that, at pH 7.5, two arginine residues are modified: one modification displays affinity-labelling kinetics and has a 1:1 stoichiometry, while the other displays simple bimolecular kinetics and a stoichiometry of 2:1. The labelling at the affinity site is markedly enhanced by the addition of ligand, implying that this active-site residue is further exposed to modification by phenylglyoxal as a result of a ligand-induced conformational change. A combination of proteolysis and electrospray MS experiments identified the site of affinity labelling as Arg-19. The highly conserved N-terminal region encompassing Arg-19 of type II dehydroquinase was found to be particularly susceptible to proteolytic cleavage. Limited digestion with proteinase K inactivates the enzyme, although the type II oligomeric structure is retained, and ligand binding partially protects against this inactivation.

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16

Pedicord, Donna, Ira Dicker, Karyn O’Neil, Leah Breth, Richard Wynn, Greogory Hollis, Jeffrey Billheimer, Andrew Stern, and Dietmar Seiffert. "CD32-dependent platelet activation by a drug-dependent antibody to glycoprotein IIb/IIIa antagonists." Thrombosis and Haemostasis 89, no. 03 (2003): 513–21. http://dx.doi.org/10.1055/s-0037-1613382.

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SummaryThrombocytopenia is observed with a frequency of up to 2% in patients treated with glycoprotein (GP) IIb/IIIa antagonists. We recently provided evidence that thrombocytopenia is caused by antibody binding to drug-induced conformational changes in GP IIb/IIIa. Here, we report that a murine monoclonal antibody binds to GP IIb/IIIa in an antagonist-dependent manner and activates platelets. Platelet stimulation is associated with a disruption of the phospholipid asymmetry, resulting in the assembly of catalytic active intrinsic Xase and prothrombinase complexes. Further mechanistic studies revealed that this response is (I) mediated in cis, (II) not associated with the formation of pro-thrombotic microparticles, and (III) requires intact platelet signaling and (IV) is blocked by increases in cAMP. The prothrombotic response is not observed using F(ab’)2 fragments and is blocked by incubation of platelets with neutralizing antibodies to the platelet FcγRIIa receptor (CD 32). Taken together, these observations suggest that GPIIb/IIIa antagonist-dependent antibody binding to the platelet fibrinogen receptor has the propensity to lead to CD32-mediated platelet activation and accelerated platelet clearance, leading to thrombocytopenia.

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17

Tao, Fei, Ya-Wen He, Dong-Hui Wu, Sanjay Swarup, and Lian-Hui Zhang. "The Cyclic Nucleotide Monophosphate Domain of Xanthomonas campestris Global Regulator Clp Defines a New Class of Cyclic Di-GMP Effectors." Journal of Bacteriology 192, no. 4 (December 11, 2009): 1020–29. http://dx.doi.org/10.1128/jb.01253-09.

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ABSTRACT The widely conserved second messenger cyclic diguanosine monophosphate (c-di-GMP) plays a key role in quorum-sensing (QS)-dependent production of virulence factors in Xanthomonas campestris pv. campestris. The detection of QS diffusible signal factor (DSF) by the sensor RpfC leads to the activation of response regulator RpfG, which activates virulence gene expression by degrading c-di-GMP. Here, we show that a global regulator in the X. campestris pv. campestris QS regulatory pathway, Clp, is a c-di-GMP effector. c-di-GMP specifically binds to Clp with high affinity and induces allosteric conformational changes that abolish the interaction between Clp and its target gene promoter. Clp is similar to the cyclic AMP (cAMP) binding proteins Crp and Vfr and contains a conserved cyclic nucleotide monophosphate (cNMP) binding domain. Using site-directed mutagenesis, we found that the cNMP binding domain of Clp contains a glutamic acid residue (E99) that is essential for c-di-GMP binding. Substituting the residue with serine (E99S) resulted in decreased sensitivity to changes in the intracellular c-di-GMP level and attenuated bacterial virulence. These data establish the direct role of Clp in the response to fluctuating c-di-GMP levels and depict a novel mechanism by which QS links the second messenger with the X. campestris pv. campestris virulence regulon.

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18

Paschke, R., M. Parmentier, and G. Vassart. "Importance of the extracellular domain of the human thyrotrophin receptor for activation of cyclic AMP production." Journal of Molecular Endocrinology 13, no. 2 (October 1994): 199–207. http://dx.doi.org/10.1677/jme.0.0130199.

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ABSTRACT The mechanism by which the TSH receptor is activated is unknown. Current knowledge leads us to consider that G protein-coupled receptors are activated by positioning of their ligand in the pocket formed by the hydrophobic transmembrane segments. Furthermore, activation of an N-terminally truncated LH receptor lacking most of the extracellular domain has been described, suggesting the existence of a mechanism involving a direct interaction between LH and the transmembrane segments. The high conservation of the transmembrane segments among G protein-coupled receptors is a strong indication for a common mechanism of receptor activation. To test this hypothesis for the TSH receptor we have constructed four N-terminally truncated TSH receptor mutants with 5 or 69 amino acids of the extracellular domain joined to signal peptide regions consisting of the first 23 or 33 amino acids. The four fragments were amplified by PCR and subcloned into pBSK+. Sequences were confirmed after subcloning in M13. After joining the four fragments in pBSK+, the four TSH receptor constructs were subcloned in pSVL and transiently or stably expressed in COS and Chinese hamster ovary (CHO) cells respectively. In contrast to results obtained for the LH receptor, stimulation of the transfectants with 10 μm human chorionic gonadotrophin or 350 mU TSH/ml did not increase cyclic AMP (cAMP) concentrations in cultures of transiently transfected COS cells or stably transfected CHO cells. However, mRNA for the TSH receptor could be detected by RNase protection assay in all stable transfectants used for stimulation of cAMP. These results suggest that activation of the receptor does not implicate direct interaction of TSH with the transmembrane domains. However, our experiments could not investigate whether binding of TSH to the extracellular part of the TSH receptor can induce conformational changes of the transmembrane part, which might trigger activation of the receptor or any other role of the extracellular receptor domain as a cofactor for TSH receptor activation.

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19

Zennadi, Rahima, and Marilyn J. Telen. "Atypical Activation of Plasma Membrane-Bound ERK1/2 Is Associated with Regulation of Sickle Red Cell Adhesion to Endothelium." Blood 116, no. 21 (November 19, 2010): 266. http://dx.doi.org/10.1182/blood.v116.21.266.266.

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Abstract 266 Abnormal adhesion of erythrocytes homozygous for hemoglobin S (SS RBCs) and vaso-occlusion are hallmarks of sickle cell disease (SCD). SS RBC adhesion can be activated via stimulation of the cAMP/PKA pathway by the stress hormone epinephrine. We have found that the extracellular signal-regulated kinase-1 and 2 (ERK1/2) is abundantly expressed in mature RBCs and is bound to the isolated plasma membrane. Because aberrations in ERK1/2 signaling are associated with various pathologies, we predicted that this prototypical molecular regulator of cell division and differentiation remained functional in terminally differentiated SS RBCs and plays a role in regulating RBC adherence. Western blot analysis of RBC ghosts showed that ERK1/2 was phosphorylated to some degree in SS but not normal RBCs. Although this basal ERK1/2 phosphorylation was not detected in all SS RBC samples tested, ERK1/2 underwent increased phosphorylation (p<0.01) in all samples tested (n=8) in response to epinephrine stimulation. Incubation of SS RBCs with the MEK inhibitor (MEKI) U0126, which specifically inhibits MEK1/2, the upstream kinase of ERK activation, completely abolished epinephrine-induced ERK1/2 phosphorylation. In contrast, epinephrine completely failed to activate ERK1/2 in normal RBCs. We further confirmed that ERK1/2 preserved its activity in SS RBCs by determining that ERK1/2 immunoprecipitated from sham-treated SS RBCs was able to phosphorylate to some extent myelin basic protein (MBP), the ERK specific substrate. However, MBP phosphorylation by ERK1/2 isolated from epinephrine-treated SS RBCs increased by 62% compared to MPB phosphorylation by ERK1/2 isolated from sham-treated cells (n=4, p<0.03). This indicates that ERK1/2 is active in SS RBCs and that epinephrine amplifies its activity. Active ERK1/2 was also found to act downstream of cAMP/PKA, since treatment of SS RBCs with forskolin, which directly activates adenylyl cyclase to produce cAMP, increased ERK1/2 phosphorylation, and the PKA-specific inhibitor 14–22 amide completely blocked the effect of epinephrine on ERK phosphorylation (n=3, p<0.001). Importantly, we found that activation of ERK1/2 signaling was implicated in adhesion of SS RBC to endothelial cells (ECs). Epinephrine significantly up-regulated SS RBC adhesion at a shear stress of 2 dynes/cm2 (p < 0.001). However, SS RBC adhesion induced by epinephrine was completely inhibited by pre-treatment of SS RBCs with MEKI U0126 (p < 0.001). PhosphorImager analysis of immunoprecipitated 32P-radiolabeled ICAM-4, which mediates SS RBC adhesion to ECs, showed that the previously described phosphorylation of ICAM-4 in response to epinephrine was dependent on PKA and MEK1/2/ERK1/2. Furthermore, addition of recombinant ERK2 to RBC ghosts, followed by mass spectrometric analysis, showed that ERK phosphorylated its consensus motif on adducins α and β and dematin; band 4.1 also underwent phosphorylation but not at an ERK consensus motif. This suggests that phosphorylation of cytoskeletal proteins may induce membrane protein conformational changes that render ICAM-4 accessible to phosphorylation by an as yet unidentified kinase. Finally, SS RBC adhesion was closely related to the onset of ERK1/2 activation. Within 1 minute of stimulation, epinephrine induced a significant increase in both SS RBC adhesion to ECs and phosphorylation of ERK1/2 (p < 0.001). Both SS RBC adhesion and ERK phosphorylation decreased after longer exposure to epinephrine (30 min vs 1 min, p < 0.001 for each). Addition of recombinant ERK2 to SS RBC ghosts, followed by mass spectrometry, also showed that phosphorylation of the ERK consensus motif on adenylyl cyclase-associated protein 1 increased 5-fold (p < 0.0003). These data suggest that activation of adenylyl cyclase-associated protein 1, which is known to inhibit adenylyl cyclase activity, may negatively regulate activation of ERK in SS RBCs. In summary, our data indicate that ERK1/2 activity is atypically preserved in SS RBCs. These data also suggest that ICAM-4 adhesive function is regulated by ERK activation, and that ERK activity could probably be turned off by ERK-induced inactivation of adenylyl cyclase. Activation of ERK1/2 in SS RBCs is an extremely interesting phenomenon in SCD physiopathology, since its mode of action could become a potential therapeutic target, and MEK inhibitors are currently in development as therapeutic agents in cancer. Disclosures: Telen: GlycoMimetics: Consultancy.

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20

Hoppe, Jürgen. "cAMP-dependent protein kinases: conformational changes during activation." Trends in Biochemical Sciences 10, no. 1 (January 1985): 29–31. http://dx.doi.org/10.1016/0968-0004(85)90013-1.

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21

Oakley, Robert H., J. Alberto Olivares-Reyes, Christine C. Hudson, Fabiola Flores-Vega, Frank M. Dautzenberg, and Richard L. Hauger. "Carboxyl-terminal and intracellular loop sites for CRF1 receptor phosphorylation and β-arrestin-2 recruitment: a mechanism regulating stress and anxiety responses." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 293, no. 1 (July 2007): R209—R222. http://dx.doi.org/10.1152/ajpregu.00099.2006.

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The primary goal was to test the hypothesis that agonist-induced corticotropin-releasing factor type 1 (CRF1) receptor phosphorylation is required for β-arrestins to translocate from cytosol to the cell membrane. We also sought to determine the relative importance to β-arrestin recruitment of motifs in the CRF1 receptor carboxyl terminus and third intracellular loop. β-Arrestin-2 translocated significantly more rapidly than β-arrestin-1 to agonist-activated membrane CRF1 receptors in multiple cell lines. Although CRF1 receptors internalized with agonist treatment, neither arrestin isoform trafficked with the receptor inside the cell, indicating that CRF1 receptor-arrestin complexes dissociate at or near the cell membrane. Both arrestin and clathrin-dependent mechanisms were involved in CRF1 receptor internalization. To investigate molecular determinants mediating the robust β-arrestin-2-CRF1 receptor interaction, mutagenesis was performed to remove potential G protein-coupled receptor kinase phosphorylation sites. Truncating the CRF1 receptor carboxyl terminus at serine-386 greatly reduced agonist-dependent phosphorylation but only partially impaired β-arrestin-2 recruitment. Removal of a serine/threonine cluster in the third intracellular loop also significantly reduced CRF1 receptor phosphorylation but did not alter β-arrestin-2 recruitment. Phosphorylation was abolished in a CRF1 receptor possessing both mutations. Surprisingly, this mutant still recruited β-arrestin-2. These mutations did not alter membrane expression or cAMP signaling of CRF1 receptors. Our data reveal the involvement of at least the following two distinct receptor regions in β-arrestin-2 recruitment: 1) a carboxyl-terminal motif in which serine/threonine residues must be phosphorylated and 2) an intracellular loop motif configured by agonist-induced changes in CRF1 receptor conformation. Deficient β-arrestin-2-CRF1 receptor interactions could contribute to the pathophysiology of affective disorders by inducing excessive CRF1 receptor signaling.

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22

Johnson, Dennis R., and Shan S. Wong. "Conformational changes of type II regulatory subunit of cAMP- dependent protein kinase on cAMP binding." FEBS Letters 247, no. 2 (April 24, 1989): 480–82. http://dx.doi.org/10.1016/0014-5793(89)81395-x.

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23

Edreira, Martin M., Sheng Li, Daniel Hochbaum, Sergio Wong, Alemayehu A. Gorfe, Fernando Ribeiro-Neto, Virgil L. Woods, and Daniel L. Altschuler. "Phosphorylation-induced Conformational Changes in Rap1b." Journal of Biological Chemistry 284, no. 40 (August 3, 2009): 27480–86. http://dx.doi.org/10.1074/jbc.m109.011312.

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24

Miller, Thomas F., David C. Clary, and Anthony J. H. M. Meijer. "Collision-induced conformational changes in glycine." Journal of Chemical Physics 122, no. 24 (June 22, 2005): 244323. http://dx.doi.org/10.1063/1.1927527.

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25

Lin, Yi-Chih, Yusong R. Guo, Atsushi Miyagi, Jesper Levring, Roderick MacKinnon, and Simon Scheuring. "Force-induced conformational changes in PIEZO1." Nature 573, no. 7773 (August 21, 2019): 230–34. http://dx.doi.org/10.1038/s41586-019-1499-2.

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26

Qasba, Pradman K., Boopathy Ramakrishnan, and Elizabeth Boeggeman. "Substrate-induced conformational changes in glycosyltransferases." Trends in Biochemical Sciences 30, no. 1 (January 2005): 53–62. http://dx.doi.org/10.1016/j.tibs.2004.11.005.

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27

Wilkinson, Keith D., and Alan N. Mayer. "Alcohol-induced conformational changes of ubiquitin." Archives of Biochemistry and Biophysics 250, no. 2 (November 1986): 390–99. http://dx.doi.org/10.1016/0003-9861(86)90741-1.

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28

Blaak, Ronald, Swen Lehmann, and Christos N. Likos. "Charge-Induced Conformational Changes of Dendrimers." Macromolecules 41, no. 12 (June 2008): 4452–58. http://dx.doi.org/10.1021/ma800283z.

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29

Grossmann, J. Günter, Margarete Neu, Robert W. Evans, Peter F. Lindley, Helmut Appel, and S. Samar Hasnain. "Metal-induced Conformational Changes in Transferrins." Journal of Molecular Biology 229, no. 3 (February 1993): 585–90. http://dx.doi.org/10.1006/jmbi.1993.1063.

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30

Suhayda, Charles G., and Alfred Haug. "Metal-induced conformational changes in calmodulin." Bulletin of Environmental Contamination and Toxicology 38, no. 2 (February 1987): 289–94. http://dx.doi.org/10.1007/bf01606676.

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31

Lund, Camilla, Christian B. Borg, Timothy Lynagh, and Stephan A. Pless. "Inhibitor-Induced Conformational Changes in ASIC1A." Biophysical Journal 114, no. 3 (February 2018): 130a. http://dx.doi.org/10.1016/j.bpj.2017.11.735.

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32

Dostmann, Wolfgang R. G. "(R P )-cAMPS inhibits the cAMP-dependent protein kinase by blocking the cAMP-induced conformational transition." FEBS Letters 375, no. 3 (November 20, 1995): 231–34. http://dx.doi.org/10.1016/0014-5793(95)01201-o.

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33

Pina, David G., Anna V. Shnyrova, Francisco Gavilanes, Anabel Rodríguez, Fernando Leal, Manuel G. Roig, Ivan Y. Sakharov, Galina G. Zhadan, Enrique Villar, and Valery L. Shnyrov. "Thermally induced conformational changes in horseradish peroxidase." European Journal of Biochemistry 268, no. 1 (January 2001): 120–26. http://dx.doi.org/10.1046/j.1432-1033.2001.01855.x.

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34

Menger, F. M., Paige A. Chicklo, and Michael J. Sherrod. "Ion-induced conformational changes in Kemp's triacid." Tetrahedron Letters 30, no. 50 (1989): 6943–46. http://dx.doi.org/10.1016/s0040-4039(01)93393-3.

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35

da Silva, J. E. Pereira, S. I. Córdoba de Torresi, D. L. A. de Faria, and M. L. A. Temperini. "Raman characterization of polyaniline induced conformational changes." Synthetic Metals 101, no. 1-3 (May 1999): 834–35. http://dx.doi.org/10.1016/s0379-6779(98)01300-9.

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Noda, Seiichiro, Masaya Ito, Satoshi Watanabe, Katsuhito Takahashi, and Koscak Maruyama. "Conformational changes of actin induced by calponin." Biochemical and Biophysical Research Communications 185, no. 1 (May 1992): 481–87. http://dx.doi.org/10.1016/s0006-291x(05)81010-1.

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37

Nakatani, Alan I., and John D. Ferry. "Thermally induced conformational changes in fibrin film." Thrombosis Research 52, no. 5 (December 1988): 361–67. http://dx.doi.org/10.1016/0049-3848(88)90020-5.

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38

Moulin, A. M., S. J. O'Shea, R. A. Badley, P. Doyle, and M. E. Welland. "Measuring Surface-Induced Conformational Changes in Proteins." Langmuir 15, no. 26 (December 1999): 8776–79. http://dx.doi.org/10.1021/la990416u.

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39

Lemke, Christopher T., and P. Lynne Howell. "Substrate Induced Conformational Changes in Argininosuccinate Synthetase." Journal of Biological Chemistry 277, no. 15 (January 23, 2002): 13074–81. http://dx.doi.org/10.1074/jbc.m112436200.

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40

Outeiro, Tiago F., Jochen Klucken, Kathryn Bercury, Julie Tetzlaff, Preeti Putcha, Luis M. A. Oliveira, Alexandre Quintas, Pamela J. McLean, and Bradley T. Hyman. "Dopamine-Induced Conformational Changes in Alpha-Synuclein." PLoS ONE 4, no. 9 (September 4, 2009): e6906. http://dx.doi.org/10.1371/journal.pone.0006906.

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41

Baffa, O., M. Tabak, O. R. Nascimento, S. Condo, and M. Brunori. "Temperature-induced conformational changes in turtle myoglobin." Il Nuovo Cimento D 7, no. 2 (February 1986): 139–50. http://dx.doi.org/10.1007/bf02451237.

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42

Saunders, Aleister J., Paula R. Davis-Searles, Devon L. Allen, Gary J. Pielak, and Dorothy A. Erie. "Osmolyte-induced changes in protein conformational equilibria." Biopolymers 53, no. 4 (April 5, 2000): 293–307. http://dx.doi.org/10.1002/(sici)1097-0282(20000405)53:4<293::aid-bip2>3.0.co;2-t.

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Puljung, Michael C., Hannah A. DeBerg, William N. Zagotta, and Stefan Stoll. "Double electron–electron resonance reveals cAMP-induced conformational change in HCN channels." Proceedings of the National Academy of Sciences 111, no. 27 (June 23, 2014): 9816–21. http://dx.doi.org/10.1073/pnas.1405371111.

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44

Ponsioen, Bas, Martijn Gloerich, Laila Ritsma, Holger Rehmann, Johannes L. Bos, and Kees Jalink. "Direct Spatial Control of Epac1 by Cyclic AMP." Molecular and Cellular Biology 29, no. 10 (March 9, 2009): 2521–31. http://dx.doi.org/10.1128/mcb.01630-08.

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ABSTRACT Epac1 is a guanine nucleotide exchange factor (GEF) for the small G protein Rap and is directly activated by cyclic AMP (cAMP). Upon cAMP binding, Epac1 undergoes a conformational change that allows the interaction of its GEF domain with Rap, resulting in Rap activation and subsequent downstream effects, including integrin-mediated cell adhesion and cell-cell junction formation. Here, we report that cAMP also induces the translocation of Epac1 toward the plasma membrane. Combining high-resolution confocal fluorescence microscopy with total internal reflection fluorescence and fluorescent resonance energy transfer assays, we observed that Epac1 translocation is a rapid and reversible process. This dynamic redistribution of Epac1 requires both the cAMP-induced conformational change as well as the DEP domain. In line with its translocation, Epac1 activation induces Rap activation predominantly at the plasma membrane. We further show that the translocation of Epac1 enhances its ability to induce Rap-mediated cell adhesion. Thus, the regulation of Epac1-Rap signaling by cAMP includes both the release of Epac1 from autoinhibition and its recruitment to the plasma membrane.

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Sugimoto, Naotoshi, Shinji Miwa, Hiroyuki Nakamura, Hiroyuki Tsuchiya, and Akihiro Yachie. "Protein kinase A and Epac activation by cAMP regulates the expression of glial fibrillary acidic protein in glial cells." Archives of Biological Sciences 68, no. 4 (2016): 795–801. http://dx.doi.org/10.2298/abs160112067s.

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Cyclic adenosine monophosphate (cAMP) controls differentiation in several types of cells during brain development. However, the molecular mechanism of cAMP-controlled differentiation is not fully understood. We investigated the role of protein kinase A (PKA) and exchange protein directly activated by cAMP (Epac) on cAMP-induced glial fibrillary acidic protein (GFAP), an astrocyte marker, in cultured glial cells. B92 glial cells were treated with cAMP-elevating drugs, an activator of adenylate cyclase, phosphodiesterase inhibitor and a ? adrenal receptor agonist. These cAMP-elevating agents induced dramatic morphological changes and expression of GFAP. A cAMP analog, 8-Br-cAMP, which activates Epac as well as PKA, induced GFAP expression and morphological changes, while another cAMP analog, 8-CPT-cAMP, which activates Epac with greater efficacy when compared to PKA, induced GFAP expression but very weak morphological changes. Most importantly, the treatment with a PKA inhibitor partially reduced cAMP-induced GFAP expression. Taken together, these results indicate that cAMP-elevating drugs lead to the induction of GFAP via PKA and/or Epac activation in B92 glial cells.

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Norström, Anders, and Ingrid Wiqvist. "Relaxin-induced changes in adenosine 3',5'-monophosphate levels in the human cervix." Acta Endocrinologica 109, no. 1 (May 1985): 122–25. http://dx.doi.org/10.1530/acta.0.1090122.

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Abstract. The effects of porcine relaxin on the levels of cAMP in human cervical tissue were studied in vitro. The specimens were obtained by needle biopsy from women undergoing hysterectomy, legal abortion in the first trimester or elective Casearean section at term, and were incubated in Krebs-Ringer buffer for 15 min in the presence of porcine relaxin (5 μg/ml, 3000 GPU/mg). cAMP was determined using a modified protein binding assay. The concentration of cAMP was higher in pregnant than in non-pregnant women. Relaxin stimulated the production of cAMP in the 7th–8th week of gestation and at term but did not significantly alter the cervical cAMP levels in neither non-pregnant women nor in women in the 10th–12th week of pregnancy. Previous studies have shown that porcine relaxin reduces collagen synthesis in tissue from the human cervix and lower uterine segment. The present observations indicate that these effects can be mediated by cAMP.

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Yang, Shumei, Kestrel M. Rogers, and David A. Johnson. "MgATP-induced conformational change of the catalytic subunit of cAMP-dependent protein kinase." Biophysical Chemistry 113, no. 2 (February 2005): 193–99. http://dx.doi.org/10.1016/j.bpc.2004.08.008.

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Lensink, M., and R. Mendez. "Recognition-induced Conformational Changes in Protein-Protein Docking." Current Pharmaceutical Biotechnology 9, no. 2 (April 1, 2008): 77–86. http://dx.doi.org/10.2174/138920108783955173.

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Gerasimova, Tatjana, A. F. Santos Seica, Thorsten Friedrich, and Petra Hellwig. "Substrate-induced conformational changes in respiratory complex I." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1863 (September 2022): 148651. http://dx.doi.org/10.1016/j.bbabio.2022.148651.

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Ghosh, S. K., D. Chattopadhyay, A. C. Sen, and B. Chakrabarti. "Melittin-induced conformational changes in human lens protein." Current Eye Research 10, no. 11 (January 1991): 1065–68. http://dx.doi.org/10.3109/02713689109020345.

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