Signal Transduction Mechanisms

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Signal transduction mechanisms of cryptochrome

Signal transduction mechanisms of cryptochrome

In order for a candidate receptor to participate in the radical-pair mechanism, several important criteria must be met. First, the receptor must be expressed in the retina, specifically in neurons that signal geomagnetic information to the brain. Secondly, the receptor should be localized in an ordered lattice with fixed orientation. The receptor must create a radical-pair as a result of photon absorption, and have a long enough lifetime (~100 nanoseconds) to allow the ambient magnetic field to alter the spin correlation, but not slow enough to allow stochastic fluctuations in spin states to dominate the signaling species. Based on evidence presented to date, cryptochromes satisfy several of these criteria, suggesting that they may act as magnetoreceptors for directional sense in animals. Cryptochrome expression in magnetically orienting garden warblers was identified in the subset of retinal ganglion cells that project to the nucleus of the basal optic root (Mouritsen et al., 2004), where magnetically sensitive neurons have been reported (Semm and Demaine, 1986) and the visual flow-fields arising from self motion are processed (Wylie et al., 1998). Moreover, CRY1-expressing ganglion cells in these birds show high levels of neuronal activity at night during magnetic orientation (Mouritsen et al., 2004). Retinal CRY1 expression is predominantly cytoplasmic and is therefore more likely to be maintained in a specific orientation via structural proteins than nuclear protein. Striking differences in the expression of CRY in migratory and nonmigratory birds also supports a unique role for cryptochromes in magnetoreception (Mouritsen et al., 2004). This model depends on the formation of a cryptochrome radical state in vivo; although the physiological relevance of such a state is not known, a plant cryptochrome has been shown to generate a radical pair upon photon absorption in vitro (Giovani et al., 2003). These studies therefore provide a correlative link between cryptochromes and magnetoreception in animals.
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Signal Transduction Mechanisms in Commissural Axon Guidance: The Role of Intracellular Tyrosine Kinases in Netrin-Dcc/Frazzled Axon Attraction

Signal Transduction Mechanisms in Commissural Axon Guidance: The Role of Intracellular Tyrosine Kinases in Netrin-Dcc/Frazzled Axon Attraction

Each pathway uses a Rac GAP (Vilse/crGAP for Robo and α-chimaerin for Ephs) and a Rac GEF (Sos for Robo and Vav for Ephs) to mediate repulsion. In the context of repulsion, Rac cycling appears to be more important than the overall levels of Rac-GTP in a responding growth cone (reminiscent of the observation that cycling is required for malignant transformation, GEFs can transform cells, whereas constitutively active Rho GTPases cannot). Alternatively, these GAPs and GEFs may represent distinct steps in the repulsive signal transduction output, as in the example of Eph receptors where Vav- family GEFs likely mediate endocytosis of the ligand-receptor complex through Rac activation (Cowan et al., 2005). Rac activation in the case of Robo receptors may precede internalization, and intracellular accumulations of Sos and Robo have been observed in cultured cells (L. Yang & G. Bashaw, unpublished observations). Thus, parallel
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Signal Transduction Mechanisms Mediating the Regulation of Vascular G Protein-Coupled Receptors

Signal Transduction Mechanisms Mediating the Regulation of Vascular G Protein-Coupled Receptors

Blood pressure homeostasis is controlled via a complex network of cell signaling mechanisms. Among the broad network of receptors and signaling molecules regulating blood vessel reactivity, members of the G protein-coupled receptor (GPCR) family are known to play a central role. GPCR activity represents a delicate, but coordinated balance between molecular mechanisms governing receptor signaling, desensitization, and re- sensitization. GPCR kinase 2 (GRK2) modulates multiple cellular responses through GPCR desensitization and alterations in GRK2 activity are considered to play an important role in the development of hypertension. The main premise of our study was to test whether the inhibition of GRK2 expression leads to alterations in vascular reactivity, vascular tone, and vascular smooth muscle cell (VSMC) signaling. Genetic knockdown of GRK2 expression results in a mouse that shows indications of intrauterine growth retardation phenotype and becomes spontaneously hypertensive at 8-12 weeks of age due to alterations in the balance between mechanisms regulating vasodilatation and vasoconstriction. The extensive loss of GRK2 expression favors an increased in vasoconstriction associated with an increase in peripheral resistance and this is likely due to the reduced Gα q/11 -coupled
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[alpha]1-adrenoceptor subtypes in the rat isolated epididymal vas deferens, spleen and human prostate and their signal transduction mechanisms

[alpha]1-adrenoceptor subtypes in the rat isolated epididymal vas deferens, spleen and human prostate and their signal transduction mechanisms

G-protein-linked receptors, including the adrenoceptors, have a predicted structure containing seven putative transm em brane-spanning domains, highly suitable for detecting extracellular signals and transducing their presence into a cytoplasmic signal (Spiegel, 1992). These receptors w hen in their inactive conformation interact most efficiently w ith the heterotrim eric form of the G-protein, located on the cytoplasmic surface of the plasma membrane. W hen the receptor is changed to its active conformation, for example by agonist binding, conformational changes in the intracellular loops of the receptor are thought to catalyze the exchange of the tightly bound GDP for GXP (Strader et al., 1989). In the GDP-bound state the a subunit is in an inactive conformation and binding of GXP brings about a conformational change to the active state (Bourne et al., 1991). This leads to reduced affinity for the py subunit heterodim er, from which it dissociates and the activated a subunit can then interact w ith effector molecules. The a subunit only remains in the active state transiently however as it has intrinsic GXPase activity and upon hydrolysis of the GXP to GDP it reassociates w ith the py subunit heterodim er (Bourne et al., 1990).
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Signal transduction in cells of the immune system in microgravity

Signal transduction in cells of the immune system in microgravity

Cell migration is an essential characteristic of life. Multicel- lular organisms must be motile to obtain nourishment, evade being eaten in their own right, respond to environ- mental changes and reproduce. Likewise, unicellular organisms such as Paramecium or Loxodes must dynami- cally respond to fluctuations in ever-changing surround- ings to assure survival [6]. However, cell migration is also an essential characteristic of many normal and abnormal biological processes within the human organism includ- ing embryonic development, defense against infections, wound healing and tumor metastasis [36,37]. In previous studies using simulated microgravity, changes in gravity demonstrated an inhibition of lymphocyte locomotion through type I collagen [38,39], and culture of human bone marrow CD34+ cells using NASA 's rotating wall ves- sels resulted in a decreased migration potential [40]. An altered movement in real microgravity was shown for leu- kocytes and Jurkat T cells, too [41,42], whereas the under- lying signal transduction mechanisms are still illusive. On the other side, T cells become more motile after being cul- tured in 10 g hypergravity [43].
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Role of protein kinases in signal transduction and their inhibitors

Role of protein kinases in signal transduction and their inhibitors

transduction is fundamental to the process. Proteins or lipids in the presence of ATPs (Adenosine triphosphates) and kinases undergo phosphorylation. The modified protein may subsequently have functional outcomes such as 1) Binding together with new protein 2) Stabilization or degradation of particular target 3) Movement of protein to new location such as nucleus or mitochondria. The human genome contains about 500 protein kinase genes; they constitute about 2% of all eukaryotic genes. Up to 30% of all proteins may be modified by kinase activity, especially those involved in signal transduction, the transmission of signals within the cell 57 .
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Prion protein and its role in signal transduction

Prion protein and its role in signal transduction

Abbreviations used: Ab – antibody; AD – Alzheimer’s disease; BSE – bovine spongiform encephalopathy; cAMP – cyclic adenosine mono-phosphate; CJD – Creutzfeldt-Jakob disease; CNS – central nervous system; CWD – chronic wasting disease; ER – endoplasmic reticulum; ERK – extracellular signal-related kinase; FFI – fatal familial insomnia; GPI – glycophosphatidylinositol; GSS – Gerstmann-Sträussler-Scheinker syndrome; ICAT – isotope-coded affinity tagging; LR – laminin receptor; LRP – laminin receptor precursor; MAP – mitogen-activated protein; MEK – MAP/ERK kinase; MHC – major histocompatibility complex; NADPH – nicotinamide adenine dinucleotide phosphate; NCAM – neural cell adhesion molecule; NMDA – N-methyl-D-aspartate; PI3K – phosphatidylinositol 3-kinase; PKA – protein kinase A; PKC – protein kinase C; PMCA – plasma membrane calcium ATPase; PrP – prion protein; PrP C – cellular prion protein;
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Proposed Role for KaiC Like ATPases as Major Signal Transduction Hubs in Archaea

Proposed Role for KaiC Like ATPases as Major Signal Transduction Hubs in Archaea

Proteins with two ATPase domains, which most closely resemble the bona fide cyanobacterial KaiC protein, are typically associated with a small protein, either KaiB (branches A5a and A5b) or a member of an uncharacterized protein family (e.g., arCOG07117, arCOG03757, arCOG03758, arCOG11224, and arCOG10037) in ancestral branch A3 (Fig. 2B). The structure of one protein of this family has been solved (PDB code 2p9x), revealing a four-helix bundle fold. Structural comparison by using VAST (47) shows that the best match for this protein is the eukaryotic DEATH domain (a domain named for death, meaning its involvement in apoptosis, also often referred to as DD) with a root mean square deviation of 0.97 Å from the DD of the human RAIDD (DD-containing protein; the abbreviation is complex and is explained in reference 48) protein (PDB code 2O71) (49, 50) (Fig. S1). The DDs and related ␣ -helical adapter domains are key components of eukaryotic signal transduction pathways, particularly those involved in programmed cell death (apoptosis), where these domains mediate connections between different components through homotypic interactions (i.e., dif- ferent DD-related adapter domains interact with one another) (49, 50). Exceptions to this association are the two-domain ATPases from the halobacteria-specific clade of branch A11 and from mostly methanomicrobial branch A1, for which no small partner protein encoded in the same locus could be identified. Bacterial branch B1 lies within an archaeal subtree that includes branches A1 to A4; several internal branches within this subtree are strongly supported ( ⬎ 90%) (Fig. 2A), suggesting horizontal transfer from archaea to bacteria. The majority of the kaiC genes associated with branch B1 are located next to genes related to two-component systems, suggesting that archaeal KaiC of branch A1 could interact with the analogous components encoded in other loci in the respective archaeal genomes. DD-like domains are specifically expanded in the class Thermococci and several members of the phylum Thaumarchaeota (Fig. S1B; Table S1). Some of them are fused to a diverged iKaiC domain, REC domain, or ferritin domain, further linking these proteins to KaiC. Moreover, genes encoding DD-like domain proteins are found in several conserved neighborhoods together with other uncharacterized genes, suggesting that additional components could be linked to the KaiC-based signal transduction network (Fig. S1B). Taking these observations into account, we predict that the DD-like domains also serve as modulators of the auto- phosphorylation activity of KaiC.
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Mechanism and evolution of cytosolic Hedgehog signal transduction

Mechanism and evolution of cytosolic Hedgehog signal transduction

Hh signal transduction in mammals utilizes the primary cilium, an evolutionarily conserved microtubule-based organelle analogous to the flagella found in single-celled eukaryotes, such as Chlamydomonas reinhardtii (Berbari et al., 2009; Eggenschwiler and Anderson, 2007; Gerdes et al., 2009). The assembly and disassembly of the cilium is mediated by intraflagellar transport (IFT) proteins and their associated kinesin II (Kif3 family) and dynein motors (Rosenbaum and Witman, 2002). Mice deficient in genes essential for cilium assembly and maintenance, such as Kif3a and Ift88, display a loss of both Gli repressor and activator function in vivo, implicating the primary cilium in the reception and interpretation of Hh signals (Huangfu and Anderson, 2005; Huangfu et al., 2003; Liu et al., 2005; May et al., 2005). Analyses of endogenous and overexpressed Smo, Ptch1, Gli1, Gli2, Gli3 and Suppressor of fused (Sufu), all core components of vertebrate Hh signaling (Table 1), have indicated that these proteins localize to the primary cilium (Chen et al., 2009; Corbit et al., 2005; Haycraft et al., 2005; Rohatgi et al., 2007). The dynamic trafficking of endogenous Ptch1, Smo, Gli2 and Gli3 has been observed at various time points after Hh stimulation (Chen et al., 2009; Corbit et al., 2005; Rohatgi et al., 2009; Rohatgi et al., 2007; Wang et al., 2009; Wilson et al., 2009a). Cultured cells that lack cilia, such as Kif3a-null mouse embryonic fibroblasts (MEFs), are refractory to stimulation by exogenous Hh ligands, and the overexpression of constitutively active forms of Smo or the treatment of these cells with Smo agonists fails to activate the pathway in the absence of the cilium (Chen et al., 2009; Ocbina et al., 2009). By contrast, primary cilia do not seem to be involved in Drosophila Hh
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2R and remodeling of vertebrate signal transduction engine

2R and remodeling of vertebrate signal transduction engine

2R-WGD occurred more than 450 million years ago, and most resulting gene duplicates were lost, leading to redi- ploidisation. Here we set out to functionally characterize retained 2ROs. First, we found that signal transduction was the most enriched GO term (in stark contrast to tan- dem or segmental duplications, where this term was underrepresented). In total, 74% of human signalling genes were descendants of 2ROs. Foreshadowing later findings, several GO terms were associated with the ner- vous system: neurogenesis, synaptic transmission, axon guidance, nervous system development and neuron dif- ferentiation (Additional file 2, Table S2_bp). Next, we searched for protein domains enriched among 2ROs and found many classic signalling domains, as well as well- known protein interaction (PI) domains, such as Src homology 2 (SH2), Src homology 3 (SH3), phosphotyro- sine-binding domain (PTB) and PDZ (reviewed in [24]). The PI domains aid signalling by enabling dynamic for- mation of signalling protein complexes. For example, SH2 and PTB selectively recognise phosphorylated tyro- sines, while SH3 binds proline-rich sequences with a characteristic motif Pro-X-X-Pro. SH2 proteins fre- quently form membrane-attached signal-processing com- plexes at autophosphorylated receptors and participate in positive and negative feedback loops of phosphorylation cascades. PTB-bearing proteins, in turn, are predomi- nantly adaptors and docking stations, frequently anchored in the cell membrane (sometimes by means of a lipid-binding PH domain), and promoting assembly of large signalling complexes at autophosphorylated tyro- sine kinases. Finally, PDZ domains recognise internal valine or leucine residues and are abundant in synapses, serving as scaffolds for the assembly of large signalling complexes involved in neurotransmission.
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Signal transduction inhibitors in treatment of myelodysplastic syndromes

Signal transduction inhibitors in treatment of myelodysplastic syndromes

therapeutically targeted by small molecule inhibitor of the TGF- β receptor kinase, LY-2157299, with encouraging preclinical results. Apart from TGF- β receptor kinase inhibition, members of TGF- β super family and BMP ligands have also been targeted by ligand trap compounds like Sotatercept (ACE-011) and ACE-536. The multikinase inhibitor, ON-01910.Na (Rigosertib) has demonstrated early signs of efficacy in reducing the percentage of leukemic blasts and is in advanced stages of clinical testing. Temsirolimus, Deforolimus and other mTOR inhibitors are being tested in clinical trials and have shown preclinical efficacy in CMML. EGF receptor inhibitors, Erlotinib and Gefitinib have shown efficacy in small trials that may be related to off target effects. Cell cycle regulator inhibitors such as Farnesyl transferase inhibitors (Tipifarnib, Lonafarnib) and MEK inhibitor (GSK1120212) have shown acceptable toxicity profiles in small studies and efforts are underway to select mutational subgroups of MDS and AML that may benefit from these inhibitors. Altogether, these studies show that targeting various signal transduction pathways that regulate hematopoiesis offers promising therapeutic potential in this disease. Future studies in combination with high resolution correlative studies will clarify the subgroup specific efficacies of these agents.
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Wnt signal transduction pathway and apoptosis: a review

Wnt signal transduction pathway and apoptosis: a review

Very interesting and novel are the data on the tumor suppressor protein, adenomatous polyposis coli (APC), and its role in apoptosis [14,17,18]. The gene encodes a large multidomain 2843 amino acid protein that is expressed in a number of fetal and adult human tissues. The wild type protein of ~310 kDa has multiple func- tional domains. APC is illustrative of the multiple roles that certain tumor suppressors play in a cell. The protein of this tumor suppressor gene has many cellular func- tions: as a component of the wnt signal transduction pathway, of adherens junctions, and the mechanism of cytoskeleton stabilization. Mutation analysis of the APC gene revealed over 400 different germline mutations responsible for familial adenomatous polyposis coli (FAP), but the overall number of detected mutations, ger- mline and somatic [19] exceeds 700 according to the Human Gene Mutation Database [HGMD, http:// www.hgmd.org]. The majority of detected mutations result in a truncated (shorter) protein product. The majority of cancer mutations occur in the mutation clus- ter region (MCR) located within exon 15, introducing premature stop codons. Multiple truncated proteins lack- ing C-terminal end are produced in such a fashion. APC's role in apoptosis regulation is dependent on whether it is comprised of full length (wild type) or truncated (mutant) proteins. Overexpression of wild type APC (310 kDa) induces apoptosis, while overexpression of mutant trun- cated proteins maintains an anti-apoptotic mode of action. Brocardo and Henderson [14] have recently iden- tified APC at mitochondria and noticed that the strongest accumulation is this protein's shorter truncated polypep- tide sequences. Mitochondrial localization of the endoge- nous APC mutants with sequence 1-1309 correlated with tumor cell survival, i.e. reduced apoptosis. Parallel find- ings indicated that overexpressed APC mutant proteins Table 1: Chromosomal distribution of the Bcl-2 family members in the human genome.
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Signal transduction, receptors, mediators and genes: younger than ever - the 13th meeting of the Signal Transduction Society focused on aging and immunology

Signal transduction, receptors, mediators and genes: younger than ever - the 13th meeting of the Signal Transduction Society focused on aging and immunology

The 13th meeting of the Signal Transduction Society was held in Weimar, from October 28 to 30, 2009. Special focus of the 2009 conference was “ Aging and Senescence ” , which was co-organized by the SFB 728 “ Environmen- tally-Induced Aging Processes ” of the University of Düsseldorf and the study group ‘ Signal Transduction ’ of the Ger- man Society for Cell Biology (DGZ). In addition, several other areas of signal transduction research were covered and supported by different consortia associated with the Signal Transduction Society including the long-term asso- ciated study groups of the German Society for Immunology and the Society for Biochemistry and Molecular Biol- ogy, and for instance the SFB/Transregio 52 “Transcriptional Programming of Individual T Cell Subsets” located in Würzburg, Mainz and Berlin. The different research areas that were introduced by outstanding keynote speakers attracted more than 250 scientists, showing the timeliness and relevance of the interdisciplinary concept and exchange of knowledge during the three days of the scientific program. This report gives an overview of the pre- sentations of the conference.
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The involvement of Rho GTPases in plexin mediated signal transduction

The involvement of Rho GTPases in plexin mediated signal transduction

Alternatively, it is of course possible that the ability of constitutively active GTPase mutants to inhibit Sema3A-Fc induced collapse truly reflects the need for Sema3A-Fc to downregulate these GTPases at some point during the collapse process. One interpretation could simply be that these GTPases are involved at two independent points in signal transduction pathways downstream of Sema3A-Fc. Initially, GTPases may need to be active for a specific period o f time during collapse. Later on, GTPase activity may be downregulated. In this case, the constitutively active and dominant negative GTPase mutants would be inhibiting collapse by acting at completely different points within a Sema3A-Fc induced signal transduction pathway. In the case of Rac this seems unlikely, as Rac.GTP levels are highest at 30 min when approximately 80% of cells are collapsed. If this model is true, parallels may be drawn between the effects of Sema3A and the repulsive guidance factor Slit. The interaction between Slit and the transmembrane receptor Robo results in the activation of a Cdc42 GAP, srGAPl and the subsequent inactivation o f Cdc42. In addition, the sustained rather than transient activation of constitutively active GTPases might be enough to prevent collapse.
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Protein dynamics and conformational selection in bidirectional signal transduction

Protein dynamics and conformational selection in bidirectional signal transduction

the Eph­ephrin binding is bidirectional, relaying the signal into both the receptor (‘forward signaling’) and the ligand (‘reverse signaling’) cells. The signal crosses the membrane to trigger activation of receptor tyrosine kinases as well as other downstream kinases. Long dis­ tance signal transduction across the membrane and the cell inevitably involves allosteric regulation through protein conformational dynamics [9]. Protein conforma­ tional change at one site is cooperatively coupled with a change in another site, in either the same or another domain. If the energy barrier is low, even a minor perturbation is sufficient to shift the protein confor ma­ tional ensemble. Long range signaling takes place
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Regulatory control of signal transduction during morphogenesis in Drosophila

Regulatory control of signal transduction during morphogenesis in Drosophila

ABSTRACT Morphogenesis shapes pattern and size during development. The initiation and propagation of morphogenetic processes is led by the integrated activation of signaling cascades. Much is known about regulatory control of signaling cascades in cell culture systems. However, how this regulatory elements act when cells need to behave coordinately is still unknown territory. The morphogenetic process of dorsal closure proceeds through changes in cell shape and polarity under the control of JNK signaling. Amongst other regulatory elements, Puckered, a Drosophila MAPK phosphatase, is involved in a negative feedback loop that controls JNK signaling activity. puckered is expressed in many other tissues, could influence other developmental events and might regulate different signaling cascades. The negative regulatory control of signal transduction pathways could be a general mechanism regulating differentiation and morphogenesis.
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Protein phosphorylation and its role in archaeal signal transduction

Protein phosphorylation and its role in archaeal signal transduction

A detailed classification of ePKs in Archaea has not been per- formed so far. However, in 2014, it was shown that many Archaea contain at least one ePK and usually two phosphatases in their genome (Kennelly 2014). The most detailed studies regarding the presence of ePKs were performed with species of the Sulfolob- ales and so far only eSTKs were characterized (see Table 3). Blast searches (BlastP) with typical BY-kinases (PtkA, Bacillus subtilis and Wzc, Escherichia coli) reveal no obvious homologs in Archaea (Shi et al. 2014). Therefore, the PKs involved in Tyr phosphoryla- tion remain to be elucidated in Archaea. As Crenarcharchaeota possess no TCSs, they solely rely on eSTKs for signal transduc- tion and so they possess several of these kinases. For example, Sulfolobus solfataricus encodes 8 eSTKs and for S. acidocaldarius 11 are predicted based on arCOG functional annotation (Kennelly 2003; Esser et al. 2011). In contrast, euryarchaeal species were re- ported to have less eSTKs, but encode a variety of TCS (Ponting et al. 1999; Kennelly 2003).
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The role of phosphoinositide metabolism in signal transduction in secretory cells

The role of phosphoinositide metabolism in signal transduction in secretory cells

Thus the role of InsP4 in these cells may be a permissive one for Insl,4,5P 3 , and the actual biphasic mobilization of Ca 2+ may then be accomplished through the capacitative mechanism [r]

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MDA5 and LGP2: Accomplices and Antagonists of Antiviral Signal Transduction

MDA5 and LGP2: Accomplices and Antagonists of Antiviral Signal Transduction

Mice with a targeted disruption in the LGP2 locus are more sus- ceptible to certain virus infections than heterozygous littermates and have defects in generating antiviral responses, supporting a positive role for LGP2 in antiviral signaling (64). LGP2 deficiency reduces IFN-␤ production and other host responses to several RNA viruses, notably including the picornaviruses EMCV and poliovirus that had been previously linked to detection by MDA5 (32, 64). The effect of LGP2 deficiency extends to cytokine re- sponses triggered by cytosolic dsDNA and DNA-genome patho- gens, which are impaired in the absence of LGP2 (67). Experi- ments in cells lacking both LGP2 and MDA5 revealed a synergistic signal transduction activity resulting from coexpression of LGP2 with MDA5 that was not attributable to either RLR alone (64), suggesting that LGP2 may synergize with MDA5 to promote effi- cient signal transduction. Replacing LGP2 with an enzymatically inactive mutant did not reconstitute defective positive signaling responses in vivo, indicating the importance of ATP hydrolysis in LGP2 positive regulation of antiviral signaling. This requirement distinguishes positive regulation by LGP2 from its negative regu- lation, which is independent of enzymatic activity (38, 39).
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Transcriptional Pathways in Hypoxic Inflammation

Transcriptional Pathways in Hypoxic Inflammation

Although, major DnA-binding factors are well described, the precise mechanisms by which they activate or repress transcription of their target genes are still unclear. it is generally believed that chromatin assembly within target promoters and activation of partner transcription factors and co-regulators controls gene- specific transcriptional responses.

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