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  • 1
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    A mutually assured destruction mechanism attenuates light signaling in Arabidopsis (2014)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2014-06-07
    Description: After light-induced nuclear translocation, phytochrome photoreceptors interact with and induce rapid phosphorylation and degradation of basic helix-loop-helix transcription factors, such as PHYTOCHROME-INTERACTING FACTOR 3 (PIF3), to regulate gene expression. Concomitantly, this interaction triggers feedback reduction of phytochrome B (phyB) levels. Light-induced phosphorylation of PIF3 is necessary for the degradation of both proteins. We report that this PIF3 phosphorylation induces, and is necessary for, recruitment of LRB [Light-Response Bric-a-Brack/Tramtrack/Broad (BTB)] E3 ubiquitin ligases to the PIF3-phyB complex. The recruited LRBs promote concurrent polyubiqutination and degradation of both PIF3 and phyB in vivo. These data reveal a linked signal-transmission and attenuation mechanism involving mutually assured destruction of the receptor and its immediate signaling partner.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4414656/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4414656/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ni, Weimin -- Xu, Shou-Ling -- Tepperman, James M -- Stanley, David J -- Maltby, Dave A -- Gross, John D -- Burlingame, Alma L -- Wang, Zhi-Yong -- Quail, Peter H -- 2R01 GM-047475/GM/NIGMS NIH HHS/ -- 5R01GM066258/GM/NIGMS NIH HHS/ -- 8P41GM103481/GM/NIGMS NIH HHS/ -- P41 GM103481/GM/NIGMS NIH HHS/ -- P50 GM082250/GM/NIGMS NIH HHS/ -- R01 GM047475/GM/NIGMS NIH HHS/ -- R01 GM066258/GM/NIGMS NIH HHS/ -- T32 GM008284/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2014 Jun 6;344(6188):1160-4. doi: 10.1126/science.1250778.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant and Microbial Biology, University of California, Berkeley, Berkeley, CA 94720, USA. Plant Gene Expression Center, Agriculture Research Service (ARS), U.S. Department of Agriculture (USDA), Albany, CA 94710, USA. ; Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA 94143, USA. Department of Plant Biology, Carnegie Institution for Science, Stanford, CA 94305, USA. ; Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA 94143, USA. ; Department of Plant Biology, Carnegie Institution for Science, Stanford, CA 94305, USA. ; Department of Plant and Microbial Biology, University of California, Berkeley, Berkeley, CA 94720, USA. Plant Gene Expression Center, Agriculture Research Service (ARS), U.S. Department of Agriculture (USDA), Albany, CA 94710, USA. quail@berkeley.edu.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24904166" target="_blank"〉PubMed〈/a〉
    Keywords: Active Transport, Cell Nucleus ; Arabidopsis/genetics/*growth & development/metabolism ; Arabidopsis Proteins/genetics/*metabolism ; Basic Helix-Loop-Helix Transcription Factors/genetics/*metabolism ; Cell Nucleus/metabolism ; Cullin Proteins/*metabolism ; Gene Expression Regulation, Plant ; HeLa Cells ; Humans ; *Light Signal Transduction ; Nuclear Proteins/genetics/metabolism ; Phosphorylation ; Phytochrome B/*metabolism ; Polyubiquitin/metabolism ; Proteolysis ; *Ubiquitination
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    A Raf-induced allosteric transition of KSR stimulates phosphorylation of MEK (2011)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2011-03-29
    Description: In metazoans, the Ras-Raf-MEK (mitogen-activated protein-kinase kinase)-ERK (extracellular signal-regulated kinase) signalling pathway relays extracellular stimuli to elicit changes in cellular function and gene expression. Aberrant activation of this pathway through oncogenic mutations is responsible for a large proportion of human cancer. Kinase suppressor of Ras (KSR) functions as an essential scaffolding protein to coordinate the assembly of Raf-MEK-ERK complexes. Here we integrate structural and biochemical studies to understand how KSR promotes stimulatory Raf phosphorylation of MEK (refs 6, 7). We show, from the crystal structure of the kinase domain of human KSR2 (KSR2(KD)) in complex with rabbit MEK1, that interactions between KSR2(KD) and MEK1 are mediated by their respective activation segments and C-lobe alphaG helices. Analogous to BRAF (refs 8, 9), KSR2 self-associates through a side-to-side interface involving Arg 718, a residue identified in a genetic screen as a suppressor of Ras signalling. ATP is bound to the KSR2(KD) catalytic site, and we demonstrate KSR2 kinase activity towards MEK1 by in vitro assays and chemical genetics. In the KSR2(KD)-MEK1 complex, the activation segments of both kinases are mutually constrained, and KSR2 adopts an inactive conformation. BRAF allosterically stimulates the kinase activity of KSR2, which is dependent on formation of a side-to-side KSR2-BRAF heterodimer. Furthermore, KSR2-BRAF heterodimerization results in an increase of BRAF-induced MEK phosphorylation via the KSR2-mediated relay of a signal from BRAF to release the activation segment of MEK for phosphorylation. We propose that KSR interacts with a regulatory Raf molecule in cis to induce a conformational switch of MEK, facilitating MEK's phosphorylation by a separate catalytic Raf molecule in trans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brennan, Damian F -- Dar, Arvin C -- Hertz, Nicholas T -- Chao, William C H -- Burlingame, Alma L -- Shokat, Kevan M -- Barford, David -- RR001614/RR/NCRR NIH HHS/ -- RR015804/RR/NCRR NIH HHS/ -- Cancer Research UK/United Kingdom -- Howard Hughes Medical Institute/ -- England -- Nature. 2011 Apr 21;472(7343):366-9. doi: 10.1038/nature09860. Epub 2011 Mar 27.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Structural Biology, Institute of Cancer Research, Chester Beatty Laboratories, 237 Fulham Road, London SW3 6JB, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21441910" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Allosteric Regulation/physiology ; Animals ; Biocatalysis ; Catalytic Domain ; Crystallography, X-Ray ; Enzyme Activation ; Extracellular Signal-Regulated MAP Kinases/metabolism ; Humans ; MAP Kinase Kinase 1/*chemistry/*metabolism ; Models, Molecular ; Phosphorylation ; Protein Multimerization ; Protein Structure, Quaternary ; Protein-Serine-Threonine Kinases/*chemistry/*metabolism ; Proto-Oncogene Proteins B-raf/chemistry/genetics/*metabolism ; Rabbits ; Signal Transduction
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 3
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    A heteromeric Texas coral snake toxin targets acid-sensing ion channels to produce pain (2011)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2011-11-19
    Description: Natural products that elicit discomfort or pain represent invaluable tools for probing molecular mechanisms underlying pain sensation. Plant-derived irritants have predominated in this regard, but animal venoms have also evolved to avert predators by targeting neurons and receptors whose activation produces noxious sensations. As such, venoms provide a rich and varied source of small molecule and protein pharmacophores that can be exploited to characterize and manipulate key components of the pain-signalling pathway. With this in mind, here we perform an unbiased in vitro screen to identify snake venoms capable of activating somatosensory neurons. Venom from the Texas coral snake (Micrurus tener tener), whose bite produces intense and unremitting pain, excites a large cohort of sensory neurons. The purified active species (MitTx) consists of a heteromeric complex between Kunitz- and phospholipase-A2-like proteins that together function as a potent, persistent and selective agonist for acid-sensing ion channels (ASICs), showing equal or greater efficacy compared with acidic pH. MitTx is highly selective for the ASIC1 subtype at neutral pH; under more acidic conditions (pH 〈 6.5), MitTx massively potentiates (〉100-fold) proton-evoked activation of ASIC2a channels. These observations raise the possibility that ASIC channels function as coincidence detectors for extracellular protons and other, as yet unidentified, endogenous factors. Purified MitTx elicits robust pain-related behaviour in mice by activation of ASIC1 channels on capsaicin-sensitive nerve fibres. These findings reveal a mechanism whereby snake venoms produce pain, and highlight an unexpected contribution of ASIC1 channels to nociception.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3226747/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3226747/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bohlen, Christopher J -- Chesler, Alexander T -- Sharif-Naeini, Reza -- Medzihradszky, Katalin F -- Zhou, Sharleen -- King, David -- Sanchez, Elda E -- Burlingame, Alma L -- Basbaum, Allan I -- Julius, David -- F31NS065597/NS/NINDS NIH HHS/ -- P40 RR018300-09/RR/NCRR NIH HHS/ -- P40RR018300-09/RR/NCRR NIH HHS/ -- P41 GM103481/GM/NIGMS NIH HHS/ -- P41RR001614/RR/NCRR NIH HHS/ -- R01NS065071/NS/NINDS NIH HHS/ -- Canadian Institutes of Health Research/Canada -- Howard Hughes Medical Institute/ -- England -- Nature. 2011 Nov 16;479(7373):410-4. doi: 10.1038/nature10607.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of California, San Francisco, California 94158-2517, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22094702" target="_blank"〉PubMed〈/a〉
    Keywords: Acid Sensing Ion Channels ; Amino Acid Sequence ; Animals ; Capsaicin/pharmacology ; Cells, Cultured ; Elapid Venoms/*chemistry/*pharmacology ; *Elapidae ; Hindlimb/drug effects/physiopathology ; Humans ; Hydrogen-Ion Concentration ; Ion Channel Gating/drug effects ; Male ; Mice ; Mice, Knockout ; Molecular Sequence Data ; Nerve Tissue Proteins/agonists/deficiency/genetics/*metabolism ; Nociception/drug effects/physiology ; Oocytes ; Pain/*chemically induced/metabolism/physiopathology ; *Protein Multimerization ; Protein Structure, Quaternary ; Protons ; Rats ; Sensory Receptor Cells/drug effects/metabolism ; Sodium Channel Agonists ; Sodium Channels/deficiency/genetics/*metabolism ; TRPV Cation Channels/metabolism ; Xenopus laevis
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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