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  • 1
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    A gate-latch-lock mechanism for hormone signalling by abscisic acid receptors (2009)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2009-11-10
    Description: Abscisic acid (ABA) is a ubiquitous hormone that regulates plant growth, development and responses to environmental stresses. Its action is mediated by the PYR/PYL/RCAR family of START proteins, but it remains unclear how these receptors bind ABA and, in turn, how hormone binding leads to inhibition of the downstream type 2C protein phosphatase (PP2C) effectors. Here we report crystal structures of apo and ABA-bound receptors as well as a ternary PYL2-ABA-PP2C complex. The apo receptors contain an open ligand-binding pocket flanked by a gate that closes in response to ABA by way of conformational changes in two highly conserved beta-loops that serve as a gate and latch. Moreover, ABA-induced closure of the gate creates a surface that enables the receptor to dock into and competitively inhibit the PP2C active site. A conserved tryptophan in the PP2C inserts directly between the gate and latch, which functions to further lock the receptor in a closed conformation. Together, our results identify a conserved gate-latch-lock mechanism underlying ABA signalling.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2810868/" 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/PMC2810868/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Melcher, Karsten -- Ng, Ley-Moy -- Zhou, X Edward -- Soon, Fen-Fen -- Xu, Yong -- Suino-Powell, Kelly M -- Park, Sang-Youl -- Weiner, Joshua J -- Fujii, Hiroaki -- Chinnusamy, Viswanathan -- Kovach, Amanda -- Li, Jun -- Wang, Yonghong -- Li, Jiayang -- Peterson, Francis C -- Jensen, Davin R -- Yong, Eu-Leong -- Volkman, Brian F -- Cutler, Sean R -- Zhu, Jian-Kang -- Xu, H Eric -- R01 DK066202/DK/NIDDK NIH HHS/ -- R01 DK066202-04/DK/NIDDK NIH HHS/ -- R01 DK071662/DK/NIDDK NIH HHS/ -- R01 DK071662-05/DK/NIDDK NIH HHS/ -- R01 GM087413/GM/NIGMS NIH HHS/ -- R01 GM087413-01/GM/NIGMS NIH HHS/ -- R01 HL089301/HL/NHLBI NIH HHS/ -- R01 HL089301-03/HL/NHLBI NIH HHS/ -- England -- Nature. 2009 Dec 3;462(7273):602-8. doi: 10.1038/nature08613.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Structural Sciences, Van Andel Research Institute, 333 Bostwick Avenue, N.E., Grand Rapids, Michigan 49503, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19898420" target="_blank"〉PubMed〈/a〉
    Keywords: Abscisic Acid/*metabolism ; Arabidopsis/genetics/metabolism/*physiology ; Arabidopsis Proteins/*chemistry/genetics/metabolism/*physiology ; Binding Sites ; DNA Mutational Analysis ; *Models, Molecular ; Plants, Genetically Modified ; Protein Binding ; Protein Structure, Tertiary ; Signal Transduction/*physiology
    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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  • 2
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    The abscisic acid receptor PYR1 in complex with abscisic acid (2009)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2009-11-10
    Description: The plant hormone abscisic acid (ABA) has a central role in coordinating the adaptive response in situations of decreased water availability as well as the regulation of plant growth and development. Recently, a 14-member family of intracellular ABA receptors, named PYR/PYL/RCAR, has been identified. These proteins inhibit in an ABA-dependent manner the activity of a family of key negative regulators of the ABA signalling pathway: the group-A protein phosphatases type 2C (PP2Cs). Here we present the crystal structure of Arabidopsis thaliana PYR1, which consists of a dimer in which one of the subunits is bound to ABA. In the ligand-bound subunit, the loops surrounding the entry to the binding cavity fold over the ABA molecule, enclosing it inside, whereas in the empty subunit they form a channel leaving an open access to the cavity, indicating that conformational changes in these loops have a critical role in the stabilization of the hormone-receptor complex. By providing structural details on the ABA-binding pocket, this work paves the way for the development of new small molecules able to activate the plant stress response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Santiago, Julia -- Dupeux, Florine -- Round, Adam -- Antoni, Regina -- Park, Sang-Youl -- Jamin, Marc -- Cutler, Sean R -- Rodriguez, Pedro Luis -- Marquez, Jose Antonio -- England -- Nature. 2009 Dec 3;462(7273):665-8. doi: 10.1038/nature08591. Epub 2009 Nov 8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Instituto de Biologia Molecular y Celular de Plantas, Consejo Superior de Investigaciones Cientificas-Universidad Politecnica de Valencia, ES-46022 Valencia, Spain.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19898494" target="_blank"〉PubMed〈/a〉
    Keywords: Abscisic Acid/*metabolism ; Arabidopsis ; Arabidopsis Proteins/*chemistry/*metabolism ; Membrane Transport Proteins/*chemistry/*metabolism ; *Models, Molecular ; Protein Binding ; Protein Structure, Tertiary
    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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    In vitro reconstitution of an abscisic acid signalling pathway (2009)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2009-11-20
    Description: The phytohormone abscisic acid (ABA) regulates the expression of many genes in plants; it has critical functions in stress resistance and in growth and development. Several proteins have been reported to function as ABA receptors, and many more are known to be involved in ABA signalling. However, the identities of ABA receptors remain controversial and the mechanism of signalling from perception to downstream gene expression is unclear. Here we show that by combining the recently identified ABA receptor PYR1 with the type 2C protein phosphatase (PP2C) ABI1, the serine/threonine protein kinase SnRK2.6/OST1 and the transcription factor ABF2/AREB1, we can reconstitute ABA-triggered phosphorylation of the transcription factor in vitro. Introduction of these four components into plant protoplasts results in ABA-responsive gene expression. Protoplast and test-tube reconstitution assays were used to test the function of various members of the receptor, protein phosphatase and kinase families. Our results suggest that the default state of the SnRK2 kinases is an autophosphorylated, active state and that the SnRK2 kinases are kept inactive by the PP2Cs through physical interaction and dephosphorylation. We found that in the presence of ABA, the PYR/PYL (pyrabactin resistance 1/PYR1-like) receptor proteins can disrupt the interaction between the SnRK2s and PP2Cs, thus preventing the PP2C-mediated dephosphorylation of the SnRK2s and resulting in the activation of the SnRK2 kinases. Our results reveal new insights into ABA signalling mechanisms and define a minimal set of core components of a complete major ABA signalling pathway.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2803041/" 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/PMC2803041/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fujii, Hiroaki -- Chinnusamy, Viswanathan -- Rodrigues, Americo -- Rubio, Silvia -- Antoni, Regina -- Park, Sang-Youl -- Cutler, Sean R -- Sheen, Jen -- Rodriguez, Pedro L -- Zhu, Jian-Kang -- R01 GM059138/GM/NIGMS NIH HHS/ -- R01 GM059138-12/GM/NIGMS NIH HHS/ -- England -- Nature. 2009 Dec 3;462(7273):660-4. doi: 10.1038/nature08599. Epub 2009 Nov 18.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Botany and Plant Sciences, University of California at Riverside, Riverside, California 92521, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19924127" target="_blank"〉PubMed〈/a〉
    Keywords: Abscisic Acid/*physiology ; Arabidopsis/enzymology/*physiology ; Arabidopsis Proteins/genetics/metabolism/*physiology ; *Gene Expression Regulation, Plant ; Mutation ; Phenotype ; Phosphorylation ; Protoplasts/physiology ; *Signal Transduction ; Stress, Physiological/*physiology
    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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  • 4
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    Reciprocal TH17 and regulatory T cell differentiation mediated by retinoic acid (2007)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2007-06-16
    Description: The cytokine transforming growth factor-beta (TGF-beta) converts naive T cells into regulatory T (Treg) cells that prevent autoimmunity. However, in the presence of interleukin-6 (IL-6), TGF-beta has also been found to promote the differentiation of naive T lymphocytes into proinflammatory IL-17 cytokine-producing T helper 17 (T(H)17) cells, which promote autoimmunity and inflammation. This raises the question of how TGF-beta can generate such distinct outcomes. We identified the vitamin A metabolite retinoic acid as a key regulator of TGF-beta-dependent immune responses, capable of inhibiting the IL-6-driven induction of proinflammatory T(H)17 cells and promoting anti-inflammatory Treg cell differentiation. These findings indicate that a common metabolite can regulate the balance between pro- and anti-inflammatory immunity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mucida, Daniel -- Park, Yunji -- Kim, Gisen -- Turovskaya, Olga -- Scott, Iain -- Kronenberg, Mitchell -- Cheroutre, Hilde -- R01 AI050265-06/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2007 Jul 13;317(5835):256-60. Epub 2007 Jun 14.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉La Jolla Institute for Allergy and Immunology, 9420 Athena Circle, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17569825" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation ; Cells, Cultured ; Colitis/immunology ; Dendritic Cells/immunology ; Dibenzazepines/pharmacology ; Forkhead Transcription Factors/biosynthesis ; Interleukin-17/*biosynthesis ; Interleukin-2/immunology ; Interleukin-6/immunology ; Intestinal Mucosa/cytology/immunology ; Listeriosis/immunology ; Lymphocyte Activation ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; Spleen/cytology/immunology ; T-Lymphocyte Subsets/cytology/*immunology ; T-Lymphocytes, Helper-Inducer/cytology/*immunology ; T-Lymphocytes, Regulatory/cytology/*immunology ; Transforming Growth Factor beta/metabolism/pharmacology ; Tretinoin/pharmacology/*physiology
    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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