Visual transduction. Sensing calcium in rod cells.
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Animals↗
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Development of the signal in sensory rhodopsin and its transfer to the cognate transducer.
The microbial phototaxis receptor sensory rhodopsin II (NpSRII, also named phoborhodopsin) mediates the photophobic response of the haloarchaeon Natronomonas pharaonis by modulating the swimming behaviour of the bacterium. After excitation by blue-green light NpSRII triggers, by means of a tightly bound transducer protein (NpHtrII), a signal transduction chain homologous with the two-component system of eubacterial chemotaxis. Two molecules of NpSRII and two molecules of NpHtrII form a 2:2 complex in membranes as shown by electron paramagnetic resonance and X-ray structure analysis. Here we present X-ray structures of the photocycle intermediates K and late M (M2) explaining the evolution of the signal in the receptor after retinal isomerization and the transfer of the signal to the transducer in the complex. The formation of late M has been correlated with the formation of the signalling state. The observed structural rearrangements allow us to propose the following mechanism for the light-induced activation of the signalling complex. On excitation by light, retinal isomerization leads in the K state to a rearrangement of a water cluster that partly disconnects two helices of the receptor. In the transition to late M the changes in the hydrogen bond network proceed further. Thus, in late M state an altered tertiary structure establishes the signalling state of the receptor. The transducer responds to the activation of the receptor by a clockwise rotation of about 15 degrees of helix TM2 and a displacement of this helix by 0.9 A at the cytoplasmic surface.
Biological Evolution↗
Crystal structure of a photoactive yellow protein from a sensor histidine kinase: conformational variability and signal transduction.
Photoactive yellow protein (E-PYP) is a blue light photoreceptor, implicated in a negative phototactic response in Ectothiorhodospira halophila, that also serves as a model for the Per-Arnt-Sim superfamily of signaling molecules. Because no biological signaling partner for E-PYP has been identified, it has not been possible to correlate any of its photocycle intermediates with a relevant signaling state. However, the PYP domain (Ppr-PYP) from the sensor histidine kinase Ppr in Rhodospirillum centenum, which regulates the catalytic activity of Ppr by blue light absorption, may allow such issues to be addressed. Here we report the crystal structure of Ppr-PYP at 2 A resolution. This domain has the same absorption spectrum and similar photocycle kinetics as full length Ppr, but a blue-shifted absorbance and considerably slower photocycle than E-PYP. Although the overall fold of Ppr-PYP resembles that of E-PYP, a novel conformation of the beta 4-beta 5 loop results in inaccessibility of Met-100, thought to catalyze chromophore reisomerization, to the chromophore. This conformation also exposes a highly conserved molecular surface that could interact with downstream signaling partners. Other structural differences in the alpha 3-alpha 4 and beta 4-beta 5 loops are consistent with these regions playing significant roles in the control of photocycle dynamics and, by comparison to other sensory Per-Arnt-Sim domains, in signal transduction. Because of its direct linkage to a measurable biological output, Ppr-PYP serves as an excellent system for understanding how changes in photocycle dynamics affect signaling by PYPs.
Bacterial Proteins↗
The mobile receptor hypothesis revisited: a mechanistic role for hormone receptor lateral mobility in signal transduction.
Recent application of the technique of fluorescence photobleaching recovery to direct measurement of the lateral mobility of plasma membrane-localized hormone receptors has shed new light on the role of receptor lateral mobility in signal transduction. Receptors for insulin and EGF have been known for some time to be largely immobile at physiological temperatures. This presumably relates to their signal transduction mechanism, which appears to require intermolecular autophosphorylation (receptor aggregation) for activation. In contrast, G-protein coupled receptors must interact with other membrane components to bring about signal transduction, and it is interesting in this regard that the adenylate cyclase (AC) activating vasopressin V2-receptor is highly laterally mobile at 37 degrees C. It has recently been possible to reversibly modulate the V2-receptor mobile fraction (f) to largely varying extents, and to demonstrate thereby a direct effect on the maximal rate of in vivo cAMP production at 37 degrees C in response to vasopressin. A direct correlation between f and maximal cAMP production indicates that f may be a key parameter in hormone signal transduction in vivo, especially at sub-KD (physiological) hormone concentrations, with mobile receptors being required to effect G-protein activation.
Adenylyl Cyclases↗
Redox regulation of signal transduction in mammalian cells.
This mini-review addresses the mechanism of ultraviolet-light-induced activation of receptor tyrosine kinases. The experimental approach into this mechanism revealed the existence of redox regulation of signal transduction in mammalian cells. It is postulated that, in addition to responsiveness to oxidative attacks from outside, redox regulation of specific redox-sensitive proteins likely represents an important physiological mechanism.
Animals↗
Light-induced exposure of the cytoplasmic end of transmembrane helix seven in rhodopsin.
A key step in signal transduction in the visual cell is the light-induced conformational change of rhodopsin that triggers the binding and activation of the guanine nucleotide-binding protein. Site-directed mAbs against bovine rhodopsin were produced and used to detect and characterize these conformational changes upon light activation. Among several antibodies that bound exclusively to the light-activated state, an antibody (IgG subclass) with the highest affinity (Ka approximately 6 x 10(-9) M) was further purified and characterized. The epitope of this antibody was mapped to the amino acid sequence 304-311. This epitope extends from the central region to the cytoplasmic end of the seventh transmembrane helix and incorporates a part of a highly conserved NPXXY motif, a critical region for signaling and agonist-induced internalization of several biogenic amine and peptide receptors. In the dark state, no binding of the antibody to rhodopsin was detected. Accessibility of the epitope to the antibody correlated with formation of the metarhodopsin II photointermediate and was reduced significantly at the metarhodopsin III intermediate. Further, incubation of the antigen-antibody complex with 11-cis-retinal failed to regenerate the native rhodopsin chromophore. These results suggest significant and reversible conformational changes in close proximity to the cytoplasmic end of the seventh transmembrane helix of rhodopsin that might be important for folding and signaling.
Amino Acid Sequence↗
Phase change and the regulation of developmental timing in plants.
Plants produce different types of organs at different times in shoot development. Along with the major changes in organ morphology that take place during developmental transitions, more gradual patterns of variation occur. The identity of organs produced at a particular position on the shoot is determined by interactions between several independently regulated, temporally coordinated processes. Two of these processes are organ production and the specification of organ identity. Coordination of these processes is accomplished in part by a thermal clock and by signal transduction pathways that mediate the response of plants to light.
Biological Clocks↗
Calcium oscillations in a subpopulation of S-antigen-immunoreactive pinealocytes of the rainbow trout (Oncorhynchus mykiss).
By means of the fura-2 technique and image analysis the intracellular concentration of free calcium ions [Ca2+]i was examined in isolated rainbow trout pinealocytes identified by S-antigen immunocytochemistry. Approximately 30% of the pinealocytes exhibited spontaneous [Ca2+]i oscillations whose frequency differed from cell to cell. Neither illumination with bright light nor dark adaptation of the cells had an apparent effect on the oscillations. Removal of extracellular Ca2+ or application of 10 microM nifedipine caused a reversible breakdown of the [Ca2+]i oscillations. Application of 60 mM KCl elevated [Ca2+]i in 90% of the oscillating and 50% of the non-oscillating pinealocytes. The effect of KCl was blocked by 50 microM nifedipine. These results suggest that voltage-gated L-type calcium channels play a major role in the regulation of [Ca2+]i in trout pinealocytes. Experiments with thapsigargin (2 microM) revealed the presence of intracellular calcium stores in 80% of the trout pinealocytes, but their role for regulation of [Ca2+]i remains elusive. Treatment with norepinephrine (100 pM-50 microM), previously shown to induce calcium release from intracellular calcium stores in rat pinealocytes, had no apparent effect on [Ca2+]i in any trout pinealocyte. This finding conforms to the concept that noradrenergic mechanisms are not involved in signal transduction in the directly light-sensitive pineal organ of anamniotic vertebrates.
Animals↗
Signal transduction pathways involved in phosphorylation and activation of p70S6K following exposure to UVA irradiation.
Ultraviolet light A (UVA) plays an important role in the etiology of human skin cancer, and UVA-induced signal transduction has a critical role in UVA-induced skin carcinogenesis. The upstream signaling pathways leading to p70(S6K) phosphorylation and activation are not well understood. Here, we observed that UVA induces phosphorylation and activation of p70(S6K). Further, UVA-stimulated p70(S6K) activity and phosphorylation at Thr(389) were blocked by wortmannin, rapamycin, PD98059, SB202190, and dominant negative mutants of phosphatidylinositol (PI) 3-kinase p85 subunit (DNM-Deltap85), ERK2 (DNM-ERK2), p38 kinase (DNM-p38), and JNK1 (DNM-JNK1) and were absent in Jnk1-/- or Jnk2-/- knockout cells. The p70(S6K) phosphorylation at Ser(411) and Thr(421)/Ser(424) was inhibited by rapamycin, PD98059, or DNM-ERK2 but not by wortmannin, SB202190, DNM-Deltap85, or DNM-p38. However, Ser(411), but not Thr(421)/Ser(424) phosphorylation, was suppressed in DNM-JNK1 and abrogated in Jnk1-/- or Jnk2-/- cells. In vitro assays indicated that Ser(411) on immunoprecipitated p70(S6K) proteins is phosphorylated by active JNKs and ERKs, but not p38 kinase, and Thr(421)/Ser(424) is phosphorylated by ERK1, but not ERK2, JNKs, or p38 kinase. Moreover, p70(S6K) co-immunoprecipitated with PI 3-kinase and possibly PDK1. The complex possibly possessed a partial basal level of phosphorylation, but not at MAPK sites, which was available for its activation by MAPKs in vitro. Thus, these results suggest that activation of MAPKs, like PI 3-kinase/mTOR, may be involved in UVA-induced phosphorylation and activation of p70(S6K).
Androstadienes↗
Elicitors triggering the simultaneous gene expression of antibacterial proteins of the silkworm, Bombyx mori.
Various elicitors were examined by Northern blot analysis to investigate the simultaneous induction of gene expression of antibacterial proteins such as cecropin B, attacin and lebocin from the silkworm, Bombyx mori. Lipopolysaccharide (LPS), lipid A, 2-keto-3-deoxyoctonate (KDO) and peptidoglycan (PG) triggered efficiently and simultaneously the gene expression of antibacterial proteins. Effects of inhibitors for signal transduction on the gene expression of Bombyx mori (Bm) cecropin B triggered by lipid A were observed using isolated adherent hemocytes consisting of granular cells and plasma cells. H-7, H-89 but not W-7 inhibited gene expression, suggesting that protein kinase C and A but not myosine light chain kinase may participate in signal transduction.
1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine↗
The distribution of calcium buffering proteins in the turtle cochlea.
Hair cells of the inner ear contain high concentrations of calcium-binding proteins that limit calcium signals and prevent cross talk between different signaling pathways during auditory transduction. Using light microscope immunofluorescence and post-embedding immunogold labeling in the electron microscope, we characterized the distribution of three calcium-buffering proteins in the turtle cochlea. Both calbindin-D28k and parvalbumin-beta were confined to hair cells in which they showed a similar distribution, whereas calretinin was present mainly in hair-cell nuclei but also occurred in supporting cells and nerve fibers. The hair-cell concentration of calbindin-D28k but not of parvalbumin-beta increased from the low- to high-frequency end of the cochlea. Calibration against standards containing known amounts of calcium-buffering protein processed in the same fluid drop as the cochlear sections gave cytoplasmic concentrations of calbindin-D28k as 0.13-0.63 mm and parvalbumin-beta as approximately 0.25 mm, but calretinin was an order of magnitude less. Total amount of Ca 2+-binding sites on the proteins is at least 1.0 mm in low-frequency hair cells and 3.0 mm in high-frequency cells. Reverse transcription-PCR showed that mRNA for all three proteins was expressed in turtle hair cells. We suggest that calbindin-D28k and parvalbumin-beta may serve as endogenous mobile calcium buffers, but the predominantly nuclear location of calretinin argues for another role in calcium signaling. The results support conclusions from electrophysiological measurements that millimolar concentrations of endogenous calcium buffers are present in turtle hair cells. Parvalbumin-beta was also found in both inner and outer hair cells of the guinea pig cochlea.
Animals↗
Olfactory G proteins: simple and complex signal transduction.
In both vertebrates and invertebrates, olfactory perception is mediated by G-protein-coupled receptors. Recent work, in both mouse and Caenorhabditis elegans, sheds light on the role of specific G proteins in olfactory signal transduction, neuronal morphology and axon guidance.
Animals↗
Light, immediate-early genes, and circadian rhythms.
Many diverse behaviors exhibit clear circadian rhythms in their expression. In mammals, these rhythms originate from a neural circadian clock located in the suprachiasmatic nuclei (SCN). Recently, signaling pathways activated by light in the SCN have begun to be identified. A specific set of immediate-early genes is induced by light in the SCN, and their expression is correlated with the resetting of circadian behavioral rhythms. These light-regulated immediate-early genes offer multiple inroads into the biology of the SCN: first, they are functional markers for the activation of SCN neurons by light; second, they can direct us to the upstream light-activated (and clock-regulated) signal transduction pathways which mediate their induction; and finally, they encode transcription factor proteins which may play a role in the molecular mechanism of resetting the circadian clock.
Animals↗
The phytochromes: photosensory perception and signal transduction.
Phytochromes are regulatory photoreceptors which primarily absorb red (R) and far-red (FR) light. A great deal is known about the spectroscopic properties, primary structure, gene regulation and gross structure of phytochromes, and about the set of developmental changes which they control, but the early steps in signal transduction from phytochrome which result in these changes are still mysterious. In angiosperms, phytochromes are encoded by a small gene family, and as a result of recent work with mutants and transgenic overexpressors it is possible to assign distinct functions to some of the individual types of phytochrome. For two of these, phytochrome A and phytochrome B, overexpression of chimeras has revealed that the determinants for their photosensory specificity and the light-promoted degradation of phytochrome A reside on the amino-terminal halves of the molecules. The interchangeability of the C-terminal halves suggests that they may share a common signal transduction mechanism. These results also invite a reappraisal of the various models that have been proposed over the years to explain the complexity of phytochrome sensitivity to various light regimes.
Light↗
Independent photoreceptive circadian clocks throughout Drosophila.
Transgenic Drosophila that expressed either luciferase or green fluorescent protein driven from the promoter of the clock gene period were used to monitor the circadian clock in explanted head, thorax, and abdominal tissues. The tissues (including sensory bristles in the leg and wing) showed rhythmic bioluminescence, and the rhythms could be reset by light. The photoreceptive properties of the explanted tissues indicate that unidentified photoreceptors are likely to contribute to photic signal transduction to the clock. These results show that autonomous circadian oscillators are present throughout the body, and they suggest that individual cells in Drosophila are capable of supporting their own independent clocks.
Animals↗
Involvement of E-cadherin and beta-catenin in germ cell tumours and in normal male fetal germ cell development.
Intercellular contacts, mediated by E-cadherin, are essential for germ cell migration and maturation. Furthermore, it has been suggested that decrease or loss of E-cadherin correlates with tumour progression and invasive behaviour. beta-catenin is involved in a number of different processes, including cell--cell interaction when bound to cadherins, and determination of cell fate in pluripotent cells when activated via the Wnt signal-transduction pathway. To shed more light on the role of these factors in normal fetal germ cell development and the pathogenesis of germ cell tumours (GCTs), the present study investigated the presence and localization of E-cadherin and beta-catenin by immunohistochemistry. E-cadherin was only weakly expressed in or absent from fetal germ cells of the second and third trimesters, and was not expressed in carcinoma in situ/intratubular germ cell neoplasia unclassified (CIS/ITGCNU) and gonadoblastoma, the precursor of an invasive GCT in dysgenetic gonads. In GCTs, it was generally not expressed in seminoma and dysgerminoma, but was found in the vast majority of non-seminoma cells. beta-catenin was found in the cytoplasm of fetal germ cells at all gestational ages and in spermatogenesis in post-pubertal testes. It was also present in CIS/ITGCNU and gonadoblastoma. Whereas seminomas and dysgerminoma were negative, non-seminoma cells were frequently found to express beta-catenin. Expression of both factors therefore reflects the degree of differentiation of these tumours. No differences for either E-cadherin or beta-catenin were observed between samples of tumours resistant or sensitive to chemotherapy, and E-cadherin expression did not correlate with vascular invasion. E-cadherin and beta-catenin therefore play a role in both normal and malignant germ cell development and differentiation that warrants further investigation, but they seem to be of limited value as predictive or prognostic factors in GCTs.
Adolescent↗
Fibroblast growth factors and their receptors: an information network controlling tissue growth, morphogenesis and repair.
The stimulation of cellular metabolism by the nine fibroblast growth factors (FGFs) is mediated by a dual-receptor system. This comprises a family of four receptor tyrosine kinases (FGFR) and heparan sulphate proteoglycans (HSPG). The stimulation of cell division by FGFs has an obligate requirement for both partners of the dual-receptor system. The binding of the nine FGFs to the FGFRs is marked by a pattern of overlapping specificity despite alternative splicing events generating a large number of FGFR proteins. Thus many of the FGFR isoforms bind several FGFs. It is likely that each FGF requires a different pattern of sulphation within the heparan sulphate chains for binding. Therefore, the HSPG receptors may provide additional specificity, allowing a cell to fine tune its response to the FGFs present in the extracellular milieu. The HSPG receptors also control the availability of FGFs and hence regulate the transport of FGFs within a tissue. FGF-stimulated cell division would appear to have a mandatory requirement for the FGFs to be translocated to the nucleus via the cytosol after interacting with the dual-receptor system. The consequences of the potential direct action of FGFs in stimulating cell division are examined in the light of current models of signal transduction.
Animals↗
Mechanism of altered TNF-alpha expression by macrophage and the modulatory effect of Panax notoginseng saponins in scald mice.
AIM: To explore the mechanism of altered tumor necrosis factor-alpha (TNF-alpha) expression by peritoneal macrophages (PMPhi) and Panax notoginseng saponins (PNS) modulation in light of NF-kappaB signal transduction in severely scalded mice. METHODS: Eighteen percent total body surface area (TBSA) full-thickness scalded mice were used. PMPhi was collected at different time intervals (0, 2, 6, 12, 24 and 48 post-burn hour (PBH)) separately. The following parameters were measured: TNF-alpha mRNA and IL-10 mRNA expression (reverse transcription-polymerase chain reaction, RT-PCR), protein kinase C (PKC) activity (isotope incorporation analysis), NF-kappaB activity (electrophoretic mobility shift assay, EMSA), IkappaB-alpha expression (Western blot). RESULTS: After scald, increased expression of TNF-alpha mRNA of PMPhi peaked at 12 PBH. Meanwhile, expression of IL-10 mRNA dropped to the lowest level at 12 PBH. NF-kappaB activity was markedly activated and reached its peak at 2 PBH. Membrane PKC activity was up-regulated after scald and showed a positive correlation with the change of TNF-alpha mRNA. Expression of IkappaB-alpha first decreased at 2 PBH and then increased to high level at 24 PBH. When 12 PBH was chosen as the time point for in vitro intervention with the application of specific NF-kappaB inhibitor pyrrolidine dithiocarbamate (PDTC), PKC inhibitor H-7 and PNS, both TNF-alpha mRNA expression and NF-kappaB activity decreased significantly. CONCLUSIONS: These results indicate that abnormal expression of TNF-alpha mRNA of macrophages might be regulated by PKC-NF-kappaB signaling following severe burn. PNS might play an anti-inflammatory effect by inhibiting NF-kappaB activity and TNF-alpha mRNA expression.
Animals↗