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PubMed2000

PAS domain residues involved in signal transduction by the Aer redox sensor of Escherichia coli.

PAS domains sense oxygen, redox potential and light, and are implicated in behaviour, circadian rhythmicity, development and metabolic regulation. Although PAS domains are widespread in archaea, bacteria and eukaryota, the mechanism of signal transduction has been elucidated only for the bacterial photo sensor PYP and oxygen sensor FixL. We investigated the signalling mechanism in the PAS domain of Aer, the redox potential sensor and aerotaxis transducer in Escherichia coli. Forty-two residues in Aer were substituted using cysteine-replacement mutagenesis. Eight mutations resulted in a null phenotype for aerotaxis, the behavioural response to oxygen. Four of them also led to the loss of the non-covalently bound FAD cofactor. Three mutant Aer proteins, N34C, F66C and N85C, transmitted a constant signal-on bias. One mutation, Y111C, inverted signalling by the transducer so that positive stimuli produced negative signals and vice versa. Residues critical for signalling were mapped onto a three-dimensional model of the Aer PAS domain, and an FAD-binding site and 'active site' for signal transduction are proposed.

Amino Acid Sequence↗
PubMed1997

Immunodeficiencies and haematological disorders--direct connections to cellular signalling pathways.

Extracellular signals, such as cytokines and foreign antigens, regulate the development and activation of haematopoietic cells through receptor-mediated transcriptional responses. Investigation of the biochemical events that transduce receptor activation to intracellular signal transduction have revealed a general mechanism for both the antigen receptor and the cytokine receptor nuclear signalling. Receptor stimulation is coupled to down-stream signalling cascades through activation of cytoplasmic tyrosine kinases but both receptor types utilize distinct signalling proteins. Antigen receptors employ protein tyrosine kinases of the Src, Syk, and Tec families which phosphorylate and activate cytoplasmic signalling proteins leading to activation of NF-AT, AP-1 and NF-kappaB transcription factors, while the principal signal transducers for cytokine receptors are the Jak tyrosine kinases and Stat transcription factors. The molecular basis for several immune and haematological disorders has been characterized during the last few years and they have been found to be caused by defects in various signalling proteins. In this review the aetiology of immune and haematological disorders is discussed in the light of the recent developments in signal transduction.

Antigens↗
PubMed1993

Neuronal inositol 1,4,5-trisphosphate receptor localized to the plasma membrane of olfactory cilia.

Both the cyclic adenosine 3',5'-monophosphate and the phosphoinositide second messenger systems are involved in olfactory signal transduction. The inositol 1,4,5-trisphosphate receptor is one of the principal intracellular calcium channels responsible for mobilizing stored calcium. The precise location of the 1,4,5-trisphosphate receptor (endoplasmic reticulum vs surface) and its role in the events of olfactory signal transduction need to be defined. By light microscopic and confocal immunohistochemistry we show expression of the olfactory-enriched G-protein, G(olf), associated with cyclic AMP responses, and of the inositol 1,4,5-trisphosphate receptor in the dendritic projections and cilia of essentially all olfactory receptor neurons, indicating that individual neurons express components of both second messenger systems. By immunoelectron microscopy, we demonstrate that the inositol 1,4,5-trisphosphate receptor is localized to the surface membrane of rat olfactory cilia. This is the first morphological demonstration of the surface membrane localization of inositol 1,4,5-trisphosphate receptor in olfactory cilia. Our findings, taken in conjunction with electrophysiological data from other workers, are supportive of the inositol 1,4,5-trisphosphate receptor playing a novel role in regulating calcium flux at the ciliary surface membrane.

Animals↗
PubMedDate not supplied

Ciliary neurotrophic factor protects rat retina cells in vitro and in vivo via PI3 kinase.

PURPOSE: Neurotrophic factors and neurotrophins are well-known to have neuroprotective efficacy against retinal injury. The aim of this experiment is to investigate the signal transduction pathway of ciliary neurotrophic factor (CNTF) on the upregulation of viability of retinal primary culture and retinal protection against constant light damage in vivo. CNTF is known to enhance the viability of retinal culture and provide protection under constant light exposure conditions, but little is known about how the signal transduction pathways of CNTF affect retina function. METHODS: Primary retinal cultures were prepared from 7-day-old Wistar rats. Brain-derived neurotrophic factor (BDNF) (0.1, 1, 10 ng/ml), CNTF (0.1, 1, 10 ng/ml), PD98059 (10, 100, 1000 nM), or LY294002 (10, 100, 1000 nM) was added to these cultures at the time of cell preparation. After 3 days, the percentage of cells surviving was assessed using alamarBlue. For the in vivo experiment, inhibitors for the MAPKK (PD98059, 10 microg/eye) or PI3K (LY294002, 10 microg/eye) pathways were injected into the vitreous together with CNTF (1 microg/eye) 2 days before constant light exposure. Electroretinogram (ERG) analysis was performed to investigate which pathway was used by CNTF. RESULTS: CNTF at 1, 10, or 100 ng/ml enhanced cell viability in retinal cultures. The cell-survival activity of CNTF was blocked by 10 ng/ml LY294002 (Dunnet's test, p < 0.05). In vivo, the neuroprotective activity of CNTF in constant-light conditions was attenuated by 10 microg/eye LY294002 (Dunnet's test, p < 0.05). CONCLUSIONS: These data suggest that CNTF promotes cell survival via the PI3K signaling pathway in vitro and in vivo.

Animals↗
PubMed1990

Subsecond deactivation of transducin by endogenous GTP hydrolysis.

The response of a retinal rod cell to a weak flash of light is mediated by a receptor/GTP-binding protein (rhodopsin/transducin) signal transduction system and terminates within a second. The T alpha subunit of transducin (composed of subunits T alpha, T beta and T gamma) is triggered by photoexcited rhodopsin (R*) to release GDP and bind GTP. The binding of GTP causes release of the T alpha unit from T beta gamma and allows it to modulate the activity of an enzyme that generates a second messenger. Termination of the response requires the hydrolysis of the GTP by intrinsic GTPase. As with other G proteins, the GTPase activity of transducin seems to be slow. Reported in vitro turnover rates of a few molecules of GTP hydrolysed per molecule of transducin per minute imply a T alpha-GTP deactivation time of many seconds. But this time might be only a small fraction of that of the GTPase cycle. We have now used time-resolved microcalorimetry in bovine rod outer segments (ROS) to monitor the heat release due to the hydrolysis of GTP by a transducin population that had been quickly activated by flash illumination of rhodopsin. The enthalpy of GTP hydrolysis is released within 1 s at 23 degrees C. This deactivation time seems to be independent of any diffusible factor in the preparation and concurs with the termination kinetics of the rod's response. Thereafter, transducin seems unable to reload GTP for many seconds. This refractory 'resetting' time may account for the low steady-state GTPase rates in vitro.

Animals↗
PubMed1994

Analysis of the parsley chalcone-synthase promoter in response to different light qualities.

We examined the chalcone synthase (chs) promoter from parsley [Petroselinum crispum Miller (A.W. Hill)] for the existence of separate promoter elements responsible for transcriptional activation of the chs gene by UV-B and by blue light. A combination of in-vivo foot-printing in parsley cells and light-induced transient expression assays with different chs promoter constructs in parsley protoplasts was used. Dark controls and blue-light-irradiated cells gave identical in-vivo footprints on the chs promoter. Pre-irradiation with blue light prior to a UV-B-light pulse is known to cause a shift in the timing of UV-B-light-induced increase in chs transcription rates. This shift was also manifested on the DNA template, since UV-B-light-induced in-vivo footprints in cells pretreated with blue light were detected earlier than in cells which had been irradiated with a UV-B-light pulse only. Although there was a clear shift in the timing of footprint appearance, the patterns of footprinting did not change. Light-induced transient-expression assays revealed that the shortest tested chs promoter which retained any light responsiveness, was sufficient for mediating both induction by UV light and the blue-light-mediated kinetic shift. These findings argue against a spatial separation of UV-B- and blue-light-responsive elements on the chs promoter. We interpret these data by postulating that the signal transduction pathways originating from the excitation of UV-B- and blue-light receptors merge at the chs promoter, or somewhere between light perception and protein-DNA interaction.

Acyltransferases↗
PubMed2005

Host-based antipoxvirus therapeutic strategies: turning the tables.

The potential threat of the smallpox virus as a bioterror weapon has long been recognized, and the need for developing suitable countermeasures has become especially acute following the events of September 2001. Traditional antiviral agents interfere with viral proteins or functions. In a new study, Yang et al. focus instead on host cellular pathways used by the virus. A drug that interferes with the cellular ErbB-1 signal transduction pathway, activated by smallpox growth factor, sheds new light on how the virus replicates in the cell. Drugs that target the ErbB-signaling pathways represent a promising new class of antiviral agents.

Biological Warfare↗
PubMed2002

Expression of the grape dihydroflavonol reductase gene and analysis of its promoter region.

Dihydroflavonol reductase (DFR) is a key enzyme involved in anthocyanin biosynthesis and proanthocyanidin synthesis in grape. DFR catalyses the reduction of dihydroflavonols to leucoanthocyanidins in the anthocyanin pathway. The DFR products, the leucoanthocyanidins, are substrates for the next step in the anthocyanin pathway and are also the substrates for the proanthocyanidin pathway. In the present study the promoter of the grape dfr gene was cloned. Analysis of the dfr promoter sequence revealed the existence of several putative DNA binding motifs. The dfr promoter was fused to the uidA gene and the control of this fusion and the endogenous dfr gene expression, was studied in transformed plants and in red cell suspension originated from fruits. The dfr promoter-uidA gene fusion was expressed in leaves, roots and stems. Deletions of the dfr promoter influenced the specificity of the expression of the GUS gene fusion in plantlet roots and the level of expression in plants and in the red cell suspension originated from fruits. The deletion analysis of the dfr promoter suggests that a specific sequence located between -725 to -233 might be involved in expression of the dfr gene in fruits. Light, calcium and sucrose induced the dfr gene expression. In the transformed suspension cultures, expression of both the endogenous dfr gene and the dfr promoter-uidA gene fusions was induced by white light. The induction by both light and calcium suggests the possible involvement of a UV receptors signal transduction pathway in the induction of the dfr gene. The induction of the dfr gene and the dfr promoter-uidA gene fusions by light and sucrose indicates a close interaction between sucrose and light signalling pathways.

Alcohol Oxidoreductases↗
PubMed2000

Time-resolved detection of transient movement of helix F in spin-labelled pharaonis sensory rhodopsin II.

Sensory rhodopsin II (also called phoborhodopsin) from the archaeal Natronobacterium pharaonis (pSRII) functions as a repellent phototaxis receptor. The excitation of the receptor by light triggers the activation of a transducer molecule (pHtrII) which has close resemblance to the cytoplasmic domain of bacterial chemotaxis receptors. In order to elucidate the first step of the signal transduction chain, the accessibility as well as static and transient mobility of cytoplasmic residues in helices F and G were analysed by electron paramagnetic resonance spectroscopy. The results indicate an outward tilting of helix F during the early steps of the photocycle which is sustained until the reformation of the initial ground state. Co-expression of pSRII with a truncated fragment of pHtrII affects the accessibility and/or the mobility of certain spin-labelled residues on helices F and G. The results suggest that these sites are located within the binding surface of the photoreceptor with its transducer.

Amino Acid Sequence↗
PubMed1998

Involvement of plasma membrane redox activity and calcium homeostasis in the UV-B and UV-A/blue light induction of gene expression in Arabidopsis.

UV and blue light are important regulators of plant gene expression and development. We investigated the signal transduction processes involved in the induction of chalcone synthase (CHS) and phenylalanine ammonia-lyase (PAL) gene expression by UV-B and UV-A/blue light in an Arabidopsis cell suspension culture. Experiments with electron transport inhibitors indicated that plasma membrane redox activity is involved in both signal transduction pathways. Calcium ionophore treatment stimulated expression of the TOUCH3 gene, and this induction was strongly antagonized by UV-A/blue and UV-B light, suggesting that both light qualities may promote calcium efflux from the cytosol. Consistent with this hypothesis, experiments with specific inhibitors indicated that UV-B and UV-A/blue light regulate calcium levels in a cytosolic pool in part via the action of specific Ca2+-ATPases. On the basis of these and previous findings, we propose that plasma membrane redox activity, initiated by photoreception, is coupled to the regulation of calcium release from an intracellular store, generating a calcium signal that is required to induce CHS expression.

Acyltransferases↗
PubMed1996

Flowers into shoots: photo and hormonal control of a meristem identity switch in Arabidopsis.

Little is known about the signals that govern the network of meristem and organ identity genes that control flower development. In Arabidopsis, we can induce a heterochronic switch from flower to shoot development, a process known as floral meristem reversion, by manipulating photo-period in the floral homeotic mutant agamous and in plants heterozygous for the meristem identity gene leafy. The transformation from flower to shoot meristem is suppressed by hy1, a mutation blocking phytochrome activity, by spindly, a mutation that activates basal gibberellin signal transduction in a hormone independent manner, or by the exogenous application of gibberellins. We propose that LFY and AG play an important role in the maintenance of flower meristem identity and that floral meristem reversion in heterozygous lfy and in ag flowers is regulated by a phytochrome and gibberellin signal transduction cascade.

Arabidopsis↗
PubMed1998

Light and circadian rhythmicity regulate MAP kinase activation in the suprachiasmatic nuclei.

Although the circadian time-keeping properties of the suprachiasmatic nuclei (SCN) require gene expression, little is known about the signal transduction pathways that initiate transcription. Here we report that a brief exposure to light during the subjective night, but not during the subjective day, activates the p44/42 mitogen-activated protein kinase (MAPK) signaling cascade in the SCN. In addition, MAPK stimulation activates CREB (cAMP response element binding protein), indicating that potential downstream transcription factors are stimulated by the MAPK pathway in the SCN. We also observed striking circadian variations in MAPK activity within the SCN, suggesting that the MAPK cascade is involved in clock rhythmicity.

Animals↗
PubMed1999

SPA1, a WD-repeat protein specific to phytochrome A signal transduction.

The five members of the phytochrome photoreceptor family of Arabidopsis thaliana control morphogenesis differentially in response to light. Genetic analysis has identified a signaling pathway that is specifically activated by phytochrome A. A component in this pathway, SPA1 (for "suppressor of phyA-105"), functions in repression of photomorphogenesis and is required for normal photosensory specificity of phytochrome A. Molecular cloning of the SPA1 gene indicates that SPA1 is a WD (tryptophan-aspartic acid)-repeat protein that also shares sequence similarity with protein kinases. SPA1 can localize to the nucleus, suggesting a possible function in phytochrome A-specific regulation of gene expression.

Amino Acid Sequence↗
PubMed2002

Incomplete block of B cell development and immunoglobulin production in mice carrying the muMT mutation on the BALB/c background.

The expression of the preB cell receptor (preBCR), composed of the mu chain, surrogate light chains and the Igalpha /Igbeta signal transduction unit, permits further differentiation of Bcell precursors. C57BL/6 mice homozygous for an inactivating mutation of the membrane exon of the mu chain gene (C57BL/6muMT/muMT)) cannot form a preBCR and are, consequently, devoid of mature B lymphocytes. Here we present evidence that the block of B cell development by the muMT mutation is incomplete in BALB/c mice. Unlike C57BL/6muMT/muMT), BALB/cmuMT/muMT) mice generate small numbers of mature B cells, accumulate plasma cells and produce high levels of all immunoglobulin isotypes, except IgM. The observed phenomenon seems to be controlled by a single genetic locus that is not linked to IgH.

Animals↗
PubMed1996

Inhibition of agonist-induced Ca2+ entry in endothelial cells by myosin light-chain kinase inhibitor.

Identification of the signal which links the depletion of Ca2+ stores to a Ca2+ entry pathway in the plasma membrane remains to be determined. In the present study, effects of ML-9 and wortmannin, inhibitors of myosin light-chain kinase (MLCK), on agonist-stimulated Ca2+ response were investigated in porcine aortic endothelial cells loaded with the Ca(2+)-sensitive dye fura-2. Bradykinin (BK) caused a rapid increase in [Ca2+]i, followed by a sustained increase due to the influx of Ca2+ from the extracellular space. ML-9 almost completely abolished the sustained increase in [Ca2+]i in BK-stimulated cells, while it did not affect the mobilization of Ca2+ from intracellular stores. ML-9 also abolished the sustained increase in [Ca2+]i caused by thapsigargin. Wortmannin mimicked the effect of ML-9 on the thapsigargin-stimulated Ca2+ response. These findings document for the first time the involvement of MLCK inhibitor in Ca2+ signaling in endothelial cells.

Androstadienes↗
PubMed1994

Complementary chromatic adaptation: photoperception to gene regulation.

Many photosynthetic organisms can acclimate to the quantity and quality of light present in their environment. In certain cyanobacteria the wavelengths of light in the environment control the synthesis of specific polypeptides of the light harvesting antenna complex or phycobilisome. This phenomenon, called complementary chromatic adaptation, is most dramatically observed in a comparison of cyanobacteria after growth in green light and red light. In red light-grown cells the phycobilisome is largely composed of phycocyanin and its associated linker polypeptides (the latter are important for the assembly of the phycocyanin subunits and their placement within the light harvesting structure); the organisms appear blue-green in color. In green light-grown cells the phycobilisome is largely composed of phycoerythrin and its associated linker polypeptides; the organisms appear red in color. The ways in which these cyanobacteria sense their changing light environment and the regulatory elements involved in controlling the process of complementary chromatic adaptation are discussed in this review.

Adaptation, Physiological↗
PubMed1992

The "ON"-bipolar agonist, L-2-amino-4-phosphonobutyrate, blocks light-evoked cone contraction in xenopus eye cups.

Rhythmic photoreceptor metabolism in relationship to light-dark cycles is now thought to be regulated through a retinal feed-back mechanism with dopamine serving as a principal signal initiating light-evoked events. In order to test the hypothesis that depolarizing "ON"-bipolar neurons participate in the retinal signalling pathway, we determined the effects of L-2-amino-4-phosphonobutyrate (L-APB) on light-evoked cone contraction in eye cups from Xenopus laevis. L-APB blocked the response stereospecifically when applied over a broad concentration range. The high specificity of L-APB in retina suggests that sign-inverting bipolar neurons which depolarize in light are in the signalling pathway. One possibility is that this pathway conveys signals that regulate dopamine release.

Aminobutyrates↗