BioModelsapplication/xmlhttps://www.ebi.ac.uk/biomodels/model/download/BIOMD0000000441?filename=BIOMD0000000441.pdfhttps://www.ebi.ac.uk/biomodels/model/download/BIOMD0000000441?filename=BIOMD0000000441-biopax3.owlhttps://www.ebi.ac.uk/biomodels/model/download/BIOMD0000000441?filename=BIOMD0000000441-biopax2.owlhttps://www.ebi.ac.uk/biomodels/model/download/BIOMD0000000441?filename=BIOMD0000000441_urn.xmlhttps://www.ebi.ac.uk/biomodels/model/download/BIOMD0000000441?filename=BIOMD0000000441_url.xmlhttps://www.ebi.ac.uk/biomodels/model/download/BIOMD0000000441?filename=BIOMD0000000441.mhttps://www.ebi.ac.uk/biomodels/model/download/BIOMD0000000441?filename=BIOMD0000000441.pnghttps://www.ebi.ac.uk/biomodels/model/download/BIOMD0000000441?filename=BIOMD0000000441.scihttps://www.ebi.ac.uk/biomodels/model/download/BIOMD0000000441?filename=BIOMD0000000441.xpphttps://www.ebi.ac.uk/biomodels/model/download/BIOMD0000000441?filename=BIOMD0000000441.vcmlprimaryOK200Uddipan SarmaManually curatedL2V4https://www.ebi.ac.uk/biomodels/BIOMD000000044122694947falseBioModelsBIOMD0000000010 biomodels.db BIOMD0000000009 biomodels.db BIOMD0000000146 biomodels.dbSBMLModelsSarma2012 Oscillations in MAPK cascade (S2)2012MODEL1112190004Sarma U, Ghosh ISarma U22694947,
BACKGROUND: Feedback loops, both positive and negative are embedded in the Mitogen Activated Protein Kinase (MAPK) cascade. In the three layer MAPK cascade, both feedback loops originate from the terminal layer and their sites of action are either of the two upstream layers. Recent studies have shown that the cascade uses coupled positive and negative feedback loops in generating oscillations. Two plausible designs of coupled positive and negative feedback loops can be elucidated from the literature; in one design the positive feedback precedes the negative feedback in the direction of signal flow and vice-versa in another. But it remains unexplored how the two designs contribute towards triggering oscillations in MAPK cascade. Thus it is also not known how amplitude, frequency, robustness or nature (analogous/digital) of the oscillations would be shaped by these two designs. RESULTS: We built two models of MAPK cascade that exhibited oscillations as function of two underlying designs of coupled positive and negative feedback loops. Frequency, amplitude and nature (digital/analogous) of oscillations were found to be differentially determined by each design. It was observed that the positive feedback emerging from an oscillating MAPK cascade and functional in an external signal processing module can trigger oscillations in the target module, provided that the target module satisfy certain parametric requirements. The augmentation of the two models was done to incorporate the nuclear-cytoplasmic shuttling of cascade components followed by induction of a nuclear phosphatase. It revealed that the fate of oscillations in the MAPK cascade is governed by the feedback designs. Oscillations were unaffected due to nuclear compartmentalization owing to one design but were completely abolished in the other case. CONCLUSION: The MAPK cascade can utilize two distinct designs of coupled positive and negative feedback loops to trigger oscillations. The amplitude, frequency and robustness of the oscillations in presence or absence of nuclear compartmentalization were differentially determined by two designs of coupled positive and negative feedback loops. A positive feedback from an oscillating MAPK cascade was shown to induce oscillations in an external signal processing module, uncovering a novel regulatory aspect of MAPK signal processing.. null, 5.
National Centre for Cell Science, Ganeshkhind, Pune, India. uddipans@gmail.comuddipan@nccs.res.inNational Centre for Cell ScienceBIOMD0000000441A hallmark of protein kinase/phosphatase cascades, including mitogen-activated protein kinase (MAPK) pathways, is the spatial separation of their components within cells. The top-level kinase, MAP3K, is phosphorylated at the cell membrane, and cytoplasmic kinases at sequential downstream levels (MAP2K and MAPK) spread the signal to distant targets. Given measured protein diffusivity and phosphatase activities, signal propagation by diffusion would result in a steep decline of MAP2K activity and low bisphosphorylated MAPK (ppMAPK) levels near the nucleus, especially in large cells, such as oocytes. Here, we show that bistability in a two-site MAPK (de)phosphorylation cycle generates a novel type of phosphoprotein wave that propagates from the surface deep into the cell interior. Positive feedback from ppMAPK to cytoplasmic MAP2K enhances the propagation span of the ppMAPK wave, making it possible to convey phosphorylation signals over exceedingly long distances. The finding of phosphorylation waves traveling with constant amplitude and high velocity may solve a long-standing enigma of survival signaling in developing neurons.<h4>Background</h4>Feedback loops, both positive and negative are embedded in the Mitogen Activated Protein Kinase (MAPK) cascade. In the three layer MAPK cascade, both feedback loops originate from the terminal layer and their sites of action are either of the two upstream layers. Recent studies have shown that the cascade uses coupled positive and negative feedback loops in generating oscillations. Two plausible designs of coupled positive and negative feedback loops can be elucidated from the literature; in one design the positive feedback precedes the negative feedback in the direction of signal flow and vice-versa in another. But it remains unexplored how the two designs contribute towards triggering oscillations in MAPK cascade. Thus it is also not known how amplitude, frequency, robustness or nature (analogous/digital) of the oscillations would be shaped by these two designs.<h4>Results</h4>We built two models of MAPK cascade that exhibited oscillations as function of two underlying designs of coupled positive and negative feedback loops. Frequency, amplitude and nature (digital/analogous) of oscillations were found to be differentially determined by each design. It was observed that the positive feedback emerging from an oscillating MAPK cascade and functional in an external signal processing module can trigger oscillations in the target module, provided that the target module satisfy certain parametric requirements. The augmentation of the two models was done to incorporate the nuclear-cytoplasmic shuttling of cascade components followed by induction of a nuclear phosphatase. It revealed that the fate of oscillations in the MAPK cascade is governed by the feedback designs. Oscillations were unaffected due to nuclear compartmentalization owing to one design but were completely abolished in the other case.<h4>Conclusion</h4>The MAPK cascade can utilize two distinct designs of coupled positive and negative feedback loops to trigger oscillations. The amplitude, frequency and robustness of the oscillations in presence or absence of nuclear compartmentalization were differentially determined by two designs of coupled positive and negative feedback loops. A positive feedback from an oscillating MAPK cascade was shown to induce oscillations in an external signal processing module, uncovering a novel regulatory aspect of MAPK signal processing.Long-range signaling by phosphoprotein waves arising from bistability in protein kinase cascades.Oscillations in MAPK cascade triggered by two distinct designs of coupled positive and negative feedback loops.Sarma Uddipan U, Ghosh Indira IMarkevich Nick I NI, Tsyganov Mikhail A MA, Hoek Jan B JB, Kholodenko Boris N BNMAPKKK cascade, MAPK signaling., mitogen-activated protein kinase cascade, MAPKKK cascade during sporulation, MAP kinase kinase kinase cascade, ERK/MAPK cascade, MAPK signalling, MAP kinase cascade, MAPK signal transductionextracellular signal-regulated kinase activity, GrpL, DmErk, Plasma Membranes, pp44mapk, GRPL, CRKII, fond, A4, CycEI, p38-alpha, phosphorylation, p38MAPK, p38a, Prp4 protein kinase activity, Hog, p38ALPHA, dmTAF[[II]]230, protein polypeptide chains, LeMPK3, ATP-protein transphosphorylase activity, p44mpk, hnRNP A2/B1, ATP:protein phosphotransferase (non-specific) activity, Dp38, Kinase, SAPK2, myd, Mpk34C, SEM, Sem, p38B, integumentum commune, p38A, MAP-k, mapk14a, mitogen-activated protein kinase kinase kinase activity, TFIID TAF250, pp42, cel, hrp40, MAP kinase kinase 4 activity, hnRNP36, Dsor2, Mbp-1, proteins, Dm p38b, Hrb87Fa, sem, Diffusions, D17Mit170, Hrb85CD, inner endospore membrane, plasma membrane lipid bilayer, hrp36, l(2)k03107, Grf40, dMKK3, MLTK, ATP Phosphotransferases, phosphatase, GRBLG, ESTS:186F5S, DmMPK2, single organism signaling, p82 kinase activity, ERK-A, dTAF[[II]]230, dpERK, dpErk, external covering of organism, 6.3.2.-, csbp, ERK-2, betaIIPKC, TAF200, DmMAPK, PMK-2, PMK-1, dp-ERK, cRaf, Tl3, Cyc E, DmSCAR, Tl2, CG4636, PMK-3, Hrb87f, CSBP, Wee-kinase activity, cellular membrane, BG:DS07108.3, Double ring-finger protein, mKIAA0609, WAVE1, pMAPK, pMapK, D-MPK2, GRAP-2, bacterial inner membrane, l(2)05206, D-SCAR, fg, DmelCG5475, deep, Mek3, MEK3, DMEK3, DmERKA, cell membrane, Nerve Cells, rl/MAPK, MAP2K, expanded, non-specific serine/threonine protein kinase activity, l(2)41Ac, c-Crk, ERK activator kinase activity, MEKK, CSBP2, MDC1D, CSBP1, CT34260, dpERk, enr, Taf250, MITOGEN-ACTIVATED PROTEIN KINASE, serine-specific protein kinase activity, Cells, HIPK2, SAPK, MAP3K, cytidine 3', Csbp2, dWAVE, Csbp1, Feedbacks, mitogen-activated protein kinase 1, Wee 1-like kinase activity, MEK1, MEK2, TAF230, big, D-p38 MAPK, cycline, glycogen synthase A kinase activity, region or site annotation, DmcyclinE, glycogen synthase kinase 3 activity, Nerve, 12559, F14N23.9, Kern, protein-containing complex, Exip, phosphorylase b kinase kinase activity, EK2-1, cdi7, PRKM15, large, surface, ATP:protein phosphotransferase (MAPKKKK-activated) activity, cyclinE, dMPK2, p38 MAPK, PRKM14, sapk2a, Cdi7, CDI7, nucleo atomico, MAM, ribosomal protein S6 kinase II activity, EXIP, ERK, Erk, PRKM1, p38beta, PRKM2, protein-serine kinase activity, positional, Hrp36, JTV1, dTAF[[II]]250, p38Ka, cell, MDDGB6, p38Kb, STK32, AI848995, DmcycE, BC023857, GRB2L, erk, SCAR1, dTAF250, CG12749, protein-cysteine kinase activity, STK28, Cytoplasmic Membranes, Hpr kinase activity, rll, Neuron, HRP36, STK26, STK27, p38-2, myelin basic protein kinase activity, Dp38b, ATP:protein phosphotransferase (MAPKKK-activated) activity, mitogen-activated protein kinase kinase activity, Dp38a, RING finger protein 19A, SAPK2A, constant, cou, AI838537, stress-activated kinase activity, Phosphorylations, MAP-2 kinase activity, BG:DS00004.13, protein serine kinase activity, Cell, protein phosphokinase activity, dTAF230, DmMKK3, Lr, PKA, l(2)k02514, native protein, DmCycE, PKC, p38MAPKK, stress-activated protein kinase activity, mapk2, mapk1, TAF[[II]]250/230, Cell Membranes, p38 beta, protein kinase p58 activity, serine/threonine protein kinase activity, Taf[[II]]250, CG12559, l(2)k02602, DMDA1, P42MAPK, dpERK1, Crk1, nucleus of neuraxis, Crk3, CSPB1, dsk1, neuraxis nucleus, 5'-cyclic monophosphate-responsive protein kinase activity, atypical PKC activity, signalling, D-CycE, 38 kDa DNA polymerase delta interaction protein, D-MKK3, binding_or_interaction_site, signalling process, dpMAPK, CRK1, Mil/Raf, Bra, protein serine-threonine kinase activity, General activity, SAP kinase activity, glycogen synthase kinase activity, protein kinase A activity, Activity, sapk2, Mpk2, Mpk3, MAPK/ERK kinase kinase activity, Mbp1, Crko, p42mapk, MEK kinase activity, Ovocytes, protein, D-p38, Atomkern, Ovocyte, Crk-II, p38 alpha, binding site, SR2-1, Ccne, DmelCG4636, horsetail nucleus, kinase-related transforming protein, mitogen-activated protein kinase activity, Q14, Q16, protein aggregate, RK, mpk2, MLK-like mitogen-activated protein triple kinase activity, mpk1, neuronal nucleus, nucleus atomi, me75, Erk/Map kinase, DMKK3, MEK3/MKK3, long, DERK-A, E(sina)7, Rl, Phosphoprotein, T1, Raf kinase activity, MP kinase activity, serine kinase activity, MEKK1, DERK, MEKK3, MEKK2, Dmp38a, AHA1, atypical protein kinase C activity, Dmp38b, plasmalemma, MKK, MAPK activator activity, WAVE-1, signaling process, MBP kinase II activity, DmelCG12749, Plasma Membrane, P11, mitogen-activated S6 kinase activity, protein-aspartyl kinase activity, dERK, l(2)k13811, CG5475, Nerve Cell, ATP, Oocyte, MAP kinase 2 activity, Scar, SCAR/WAVE, Mapk, gyltl1b-b, Erk1, ERK1, ERK2, mapk1a, Erk2, A230093K24Rik, organism surface, Hrb2, TAFII-250, br37, TAF250/230, D-P38a, GrbX, D-p38b, M phase-specific cdc2 kinase activity, D-p38a, TAFII250, p41mapk, juxtamembrane, Syn, MapK, mapk1b, MLTKa, BEST:SD02991, MAPK, MLTKb, MDDGA6, cell nucleus, P38, scar, C14orf3, serine protein kinase activity, DWave, erk2, mapk, region, CG12244, HRB87F/hrp36, Transphosphorylases, phosphorylase B kinase kinase activity, ERKa, gyltl1b, GADS, BcDNA:RE08694, positional polypeptide feature, protein glutamyl kinase activity, JTV-1, AI195380, l(2R)EMS45-39, wave, HRB87F, Mona, mdc1d, WAVE, DmelCG12559, p38alpha, p38, Prkm15, MAP kinase kinase 7 activity, CG17603, Nerve., Prkm14, TAF[[II]], Proto-oncogene c-Crk, DpErk, DpERK, ErkA, ERKA, hydroxyalkyl-protein kinase activity, WEE1Hu, DMDA, l35Dd, enlarged, integumentary system, SR3-5, p41, epsilon PKC, p40, DmelCG12304, 186F5S, dermal system, pERK, REKS, F14N23_9, ribosomal S6 protein kinase activity, calcium/phospholipid-dependent protein kinase activity, d230, biological signaling, l(1)G0252, noyau atomique, GroupII, MAPKK1, CG7393, Cytoplasmic Membrane, dTAFII250, cycE, EfW1, l(2)br37, TYPE, froggy, Gyltl1a, CYCLE, CrkIII, DAGA4, p38Hog, dp38a, dp38b, Gads, polypeptide chain, dmTAF1, Taf230, Wave, Dscar, serine(threonine) protein kinase activity, Low, p42-MAPK, SCG3, Phosphotransferase, T-antigen kinase activity, TAF250, nuclei, galactosyltransferase-associated kinase activity, MKK2, Mkk3, MKK3, MKK4, Taf200, CYCE, MAPKKK activity, DmelCG12244, MKK6, DmelCG3938, xp42, MKK7, nucleus of CNS, noyau, nucleo, CyclE, uniform, 3938, Taf1p, Transphosphorylase, p42 mitogen-activated protein kinase activity, Crk-III, CG18732, ATP:protein phosphotransferase (MAPKK-activated) activity, Cytoplasmic, l(2)k05007, BPFD#36, protein kinase (phosphorylating) activity, dm-cycE, GRID, nucleus, Raf-1, time of survival, great, ATMPK1, site, DmERK-A, TAF, casein kinase (phosphorylating) activity, integral to plasma membrane, cMos, ert1, TAF[[II]]250, protein complex, DMPK2, integral component of plasma membrane, prkm2, anon-sts23, prkm1, CT39192, l(3)84Ab, P11/Hrb87F, MAP kinase or ERK kinase activity, Phosphotransferases, Crk-I, DMKK3/lic, DmelCG7393, MEKK activity, LGMD2C, p38delta, twitchin kinase activity, survival, natural protein, nervous system nucleus, group 2, MEK activity, p230, Protein, AP50 kinase activity, MBP kinase I activity, TFIID, CyeE, Xp42, threonine-specific protein kinase activity, Plasma, Membranes, MAPKK, TAF[[II]]230, Kinases, mitogen activated kinase activity, body surface, INSDC_feature:misc_binding, Su(Raf)2B, MAPKK activity, Mxi2, l(2)35Dd, phosphoric monoester hydrolase activity, Sapk2A, EY2-2, TAF[II]250, MAPK2, Membrane, dp38, Dorfin, phosphorylated protein, D-ERK, DmelCG17603, mxi2, ERT1, velocity, SCARMD2, BG:DS00797.3, Prot/PhosRes+, cytoplasmic membrane, CG3938, MAP kinase 1 activity, A-kinase activity, TAF1glycogen synthase kinase activity, extent, DmErk, extracellular signal-regulated kinase activity, D-jun/Jra, pp44mapk, Public Sectors, protein kinase A activity, ERK/MAPK cascade, AP-1, d-jun, Mpk2, p42mapk, protein, jra, Prp4 protein kinase activity, SR2-1, protein polypeptide chains, LeMPK3, ATP-protein transphosphorylase activity, p44mpk, ATP:protein phosphotransferase (non-specific) activity, kinase-related transforming protein, Dp38, mitogen-activated protein kinase activity, Kinase, Public Enterprise, protein aggregate, SAPK2, mpk1, SEM, Sem, MAP-k, Junc, Erk/Map kinase, pp42, FATE, l(2)IA109, Public Domains, DERK-A, MAP kinase kinase 4 activity, Dsor2, cell sheath, V, proteins, E(sina)7, sem, Rl, Raf kinase activity, Jun, JUN, serine kinase activity, MP kinase activity, DERK, atypical protein kinase C activity, MAPKKK cascade during sporulation, MAPK activator activity, MKK, MBP kinase II activity, c-Jun, mitogen-activated S6 kinase activity, protein-aspartyl kinase activity, dERK, ATP Phosphotransferases, phosphatase, ATP, p82 kinase activity, ERK-A, jun, notes, MAP kinase 2 activity, d-JRA, dpERK, dpErk, Papers, D-Jun, Mapk, completeness, lamina, betaIIPKC, Erk1, incomplete, ERK1, mapk1a, ERK2, DmMAPK, PMK-2, dp-ERK, PMK-1, MAPK signal transduction, results, PMK-3, M phase-specific cdc2 kinase activity, Wee-kinase activity, Literatures, abolished, MapK, mapk1b, Public Domain, MAPK, D-jun, CT43, Domains, pMAPK, pMapK, serine protein kinase activity, erk2, mapk, Domain, Transphosphorylases, phosphorylase B kinase kinase activity, ERKa, DmERKA, absence, rl/MAPK, BcDNA:RE08694, protein glutamyl kinase activity, l(2R)EMS45-39, MAP2K, DmelCG12559, non-specific serine/threonine protein kinase activity, MAP kinase kinase 7 activity, p38, l(2)41Ac, ERK activator kinase activity, DpErk, DpERK, ErkA, ERKA, hydroxyalkyl-protein kinase activity, WEE1Hu, CT34260, Sector, dpERk, serine-specific protein kinase activity, MAPK signalling, d-Jun, epsilon PKC, HIPK2, SAPK, cytidine 3', Feedbacks, Wee 1-like kinase activity, MEK1, MEK2, footnotes, pERK, ribosomal S6 protein kinase activity, calcium/phospholipid-dependent protein kinase activity, Sectors, glycogen synthase A kinase activity, GroupII, MAPKK1, cJun, glycogen synthase kinase 3 activity, number, l(2)46Ef, 12559, Copyrights, protein-containing complex, presence, phosphorylase b kinase kinase activity, EK2-1, polypeptide chain, serine(threonine) protein kinase activity, ribosomal protein S6 kinase II activity, Enterprises, dJRA, dJra, Phosphotransferase, MAP kinase cascade, T-antigen kinase activity, Erk, ERK, MKK2, galactosyltransferase-associated kinase activity, MKK4, protein-serine kinase activity, MKK6, Direction, MKK7, layer, xp42, MAPK signaling, absent from organism, dJun, dJUN, STK32, Transphosphorylase, Public Enterprises, p42 mitogen-activated protein kinase activity, CG18732, ATP:protein phosphotransferase (MAPKK-activated) activity, erk, DmelCG2275, protein kinase (phosphorylating) activity, Abstract, protein-cysteine kinase activity, Raf-1, MAP kinase kinase kinase cascade, Hpr kinase activity, rll, DmERK-A, l(2R)IA109, STK26, STK27, p38-2, Enterprise, casein kinase (phosphorylating) activity, myelin basic protein kinase activity, ATP:protein phosphotransferase (MAPKKK-activated) activity, mitogen-activated protein kinase kinase activity, MAPKKK cascade, ert1, protein complex, c-jun, prkm2, stress-activated kinase activity, prkm1, CT39192, MAP-2 kinase activity, function, protein serine kinase activity, mitogen-activated protein kinase cascade, MAP kinase or ERK kinase activity, Phosphotransferases, Djun, protein phosphokinase activity, p38delta, count in organism, dm-Jun, twitchin kinase activity, PKA, native protein, natural protein, PKC, Public, MEK activity, stress-activated protein kinase activity, Protein, mapk2, AP50 kinase activity, mapk1, djun, MBP kinase I activity, background, protein kinase p58 activity, Data Base, DJUN, DJun, Xp42, serine/threonine protein kinase activity, threonine-specific protein kinase activity, MAPKK, CG12559, distinct, Kinases, mitogen activated kinase activity, Su(Raf)2B, MAPKK activity, dpERK1, phosphoric monoester hydrolase activity, CG2275, EY2-2, dsk1, 5'-cyclic monophosphate-responsive protein kinase activity, atypical PKC activity, introduction, AP1, requirements, D-ERK, dAP-1, dpMAPK, sheath of cells, layer of cells, Public., quantitative, JRA, protein serine-threonine kinase activity, SAP kinase activity, A-kinase activity, MAP kinase 1 activity, presence or absence in organismTransphosphorylases, biological signaling, protein complex, Kinases, long, ATP., proteins, protein, Transphosphorylase, Phosphoprotein, protein-containing complex, Phosphotransferases, signalling, phosphorylated protein, protein polypeptide chains, signalling process, native protein, natural protein, polypeptide chain, signaling process, Protein, Prot/PhosRes+, Kinase, protein aggregate, ATP Phosphotransferases, Phosphotransferase, single organism signalingfalseSarma2012 - Oscillations in MAPK cascade (S2)
Sarma2012 - Oscillations in MAPK cascade (S2)
Two plausible designs (S1 and S2) of coupled positive and negative feedback loops of MAPK cascade has been described in this paper. This model corresponds to model S2 that comprises negative feedback from MK-PP to MKK_PP layer coupled to positive feedback from MK-PP to MKKK-P layer.
This model is described in the article:
Oscillations in MAPK cascade triggered by two distinct designs of coupled positive and negative feedback loops.
Sarma U, Ghosh I.
BMC Res Notes. 2012 Jun 13;5:287.
Abstract:
BACKGROUND:
Feedback loops, both positive and negative are embedded in the Mitogen Activated Protein Kinase (MAPK) cascade. In the three layer MAPK cascade, both feedback loops originate from the terminal layer and their sites of action are either of the two upstream layers. Recent studies have shown that the cascade uses coupled positive and negative feedback loops in generating oscillations. Two plausible designs of coupled positive and negative feedback loops can be elucidated from the literature; in one design the positive feedback precedes the negative feedback in the direction of signal flow and vice-versa in another. But it remains unexplored how the two designs contribute towards triggering oscillations in MAPK cascade. Thus it is also not known how amplitude, frequency, robustness or nature (analogous/digital) of the oscillations would be shaped by these two designs.
RESULTS:
We built two models of MAPK cascade that exhibited oscillations as function of two underlying designs of coupled positive and negative feedback loops. Frequency, amplitude and nature (digital/analogous) of oscillations were found to be differentially determined by each design. It was observed that the positive feedback emerging from an oscillating MAPK cascade and functional in an external signal processing module can trigger oscillations in the target module, provided that the target module satisfy certain parametric requirements. The augmentation of the two models was done to incorporate the nuclear-cytoplasmic shuttling of cascade components followed by induction of a nuclear phosphatase. It revealed that the fate of oscillations in the MAPK cascade is governed by the feedback designs. Oscillations were unaffected due to nuclear compartmentalization owing to one design but were completely abolished in the other case.
CONCLUSION:
The MAPK cascade can utilize two distinct designs of coupled positive and negative feedback loops to trigger oscillations. The amplitude, frequency and robustness of the oscillations in presence or absence of nuclear compartmentalization were differentially determined by two designs of coupled positive and negative feedback loops. A positive feedback from an oscillating MAPK cascade was shown to induce oscillations in an external signal processing module, uncovering a novel regulatory aspect of MAPK signal processing.
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2016-04-082013-03-182011-12-19BIOMD00000004412269494717102806MODEL1112190004BIOMD0000000441GO:0000165GO:0005623GO:0016310GO:0016311C00562131567P04049Q02750P28482P51452