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  • 1
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    Cellular differentiation regulated by gibberellin in the Arabidopsis thaliana pickle mutant (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-07-04
    Description: The plant growth regulator gibberellin (GA) has a profound effect on shoot development and promotes developmental transitions such as flowering. Little is known about any analogous effect GA might have on root development. In a screen for mutants, Arabidopsis plants carrying a mutation designated pickle (pkl) were isolated in which the primary root meristem retained characteristics of embryonic tissue. Expression of this aberrant differentiation state was suppressed by GA. Root tissue from plants carrying the pkl mutation spontaneously regenerated new embryos and plants.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ogas, J -- Cheng, J C -- Sung, Z R -- Somerville, C -- New York, N.Y. -- Science. 1997 Jul 4;277(5322):91-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant Biology, Carnegie Institution of Washington, 290 Panama Street, Stanford, CA 94305, USA. jogas@andrew.stanford.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9204906" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/*cytology/drug effects/genetics/metabolism ; *Arabidopsis Proteins ; Cell Differentiation/drug effects ; Fatty Acids/analysis ; Genes, Plant ; Germination ; Gibberellins/*metabolism/pharmacology ; Meristem/*cytology/drug effects/metabolism ; Mutation ; Phenotype ; Plant Growth Regulators/pharmacology ; Plant Proteins/genetics ; Plant Roots/*cytology/drug effects/metabolism ; Signal Transduction ; Triazoles/pharmacology ; Triglycerides/analysis
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    CLEC5A is critical for dengue-virus-induced lethal disease (2008)
    Nature Publishing Group (NPG)
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    Publication Date: 2008-05-23
    Description: Dengue haemorrhagic fever and dengue shock syndrome, the most severe responses to dengue virus (DV) infection, are characterized by plasma leakage (due to increased vascular permeability) and low platelet counts. CLEC5A (C-type lectin domain family 5, member A; also known as myeloid DAP12-associating lectin (MDL-1)) contains a C-type lectin-like fold similar to the natural-killer T-cell C-type lectin domains and associates with a 12-kDa DNAX-activating protein (DAP12) on myeloid cells. Here we show that CLEC5A interacts with the dengue virion directly and thereby brings about DAP12 phosphorylation. The CLEC5A-DV interaction does not result in viral entry but stimulates the release of proinflammatory cytokines. Blockade of CLEC5A-DV interaction suppresses the secretion of proinflammatory cytokines without affecting the release of interferon-alpha, supporting the notion that CLEC5A acts as a signalling receptor for proinflammatory cytokine release. Moreover, anti-CLEC5A monoclonal antibodies inhibit DV-induced plasma leakage, as well as subcutaneous and vital-organ haemorrhaging, and reduce the mortality of DV infection by about 50% in STAT1-deficient mice. Our observation that blockade of CLEC5A-mediated signalling attenuates the production of proinflammatory cytokines by macrophages infected with DV (either alone or complexed with an enhancing antibody) offers a promising strategy for alleviating tissue damage and increasing the survival of patients suffering from dengue haemorrhagic fever and dengue shock syndrome, and possibly even other virus-induced inflammatory diseases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, Szu-Ting -- Lin, Yi-Ling -- Huang, Ming-Ting -- Wu, Ming-Fang -- Cheng, Shih-Chin -- Lei, Huan-Yao -- Lee, Chien-Kuo -- Chiou, Tzyy-Wen -- Wong, Chi-Huey -- Hsieh, Shie-Liang -- GM62116/GM/NIGMS NIH HHS/ -- England -- Nature. 2008 May 29;453(7195):672-6. doi: 10.1038/nature07013. Epub 2008 May 21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department and Institute of Microbiology and Immunology, National Yang-Ming University, Taipei 112, Taiwan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18496526" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing/metabolism ; Animals ; Cell Adhesion Molecules/genetics/metabolism ; Cell Line ; Dengue Virus/*metabolism/*pathogenicity ; Host-Pathogen Interactions ; Humans ; Interferon-alpha ; Lectins, C-Type/antagonists & inhibitors/genetics/immunology/*metabolism ; Macrophages/virology ; Membrane Proteins/metabolism ; Mice ; Phosphorylation ; Protein Binding ; Receptors, Cell Surface/antagonists & inhibitors/genetics/immunology/*metabolism ; STAT1 Transcription Factor/deficiency/genetics ; Tumor Necrosis Factor-alpha/secretion ; Virus Replication
    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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    Structural mechanism of WASP activation by the enterohaemorrhagic E. coli effector EspF(U) (2008)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2008-07-25
    Description: During infection, enterohaemorrhagic Escherichia coli (EHEC) takes over the actin cytoskeleton of eukaryotic cells by injecting the EspF(U) protein into the host cytoplasm. EspF(U) controls actin by activating members of the Wiskott-Aldrich syndrome protein (WASP) family. Here we show that EspF(U) binds to the autoinhibitory GTPase binding domain (GBD) in WASP proteins and displaces it from the activity-bearing VCA domain (for verprolin homology, central hydrophobic and acidic regions). This interaction potently activates WASP and neural (N)-WASP in vitro and induces localized actin assembly in cells. In the solution structure of the GBD-EspF(U) complex, EspF(U) forms an amphipathic helix that binds the GBD, mimicking interactions of the VCA domain in autoinhibited WASP. Thus, EspF(U) activates WASP by competing directly for the VCA binding site on the GBD. This mechanism is distinct from that used by the eukaryotic activators Cdc42 and SH2 domains, which globally destabilize the GBD fold to release the VCA. Such diversity of mechanism in WASP proteins is distinct from other multimodular systems, and may result from the intrinsically unstructured nature of the isolated GBD and VCA elements. The structural incompatibility of the GBD complexes with EspF(U) and Cdc42/SH2, plus high-affinity EspF(U) binding, enable EHEC to hijack the eukaryotic cytoskeletal machinery effectively.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2719906/" 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/PMC2719906/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cheng, Hui-Chun -- Skehan, Brian M -- Campellone, Kenneth G -- Leong, John M -- Rosen, Michael K -- R01 AI046454/AI/NIAID NIH HHS/ -- R01 AI046454-09/AI/NIAID NIH HHS/ -- R01 GM056322/GM/NIGMS NIH HHS/ -- R01 GM056322-12A1/GM/NIGMS NIH HHS/ -- R01-AI46454/AI/NIAID NIH HHS/ -- R01-GM56322/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- England -- Nature. 2008 Aug 21;454(7207):1009-13. doi: 10.1038/nature07160. Epub 2008 Jul 23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, Texas 75390, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18650809" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/metabolism ; Amino Acid Sequence ; Animals ; Carrier Proteins/chemistry/*metabolism ; Cells, Cultured ; Enterohemorrhagic Escherichia coli/chemistry/genetics/*metabolism ; Escherichia coli Proteins/chemistry/*metabolism ; Fibroblasts/cytology ; Mice ; Models, Molecular ; Molecular Sequence Data ; Protein Structure, Tertiary ; Wiskott-Aldrich Syndrome Protein/chemistry/*metabolism ; Wiskott-Aldrich Syndrome Protein, Neuronal/chemistry/metabolism
    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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    Structure of the formate transporter FocA reveals a pentameric aquaporin-like channel (2009)
    Nature Publishing Group (NPG)
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    Publication Date: 2009-11-27
    Description: FocA is a representative member of the formate-nitrite transporter family, which transports short-chain acids in bacteria, archaea, fungi, algae and parasites. The structure and transport mechanism of the formate-nitrite transporter family remain unknown. Here we report the crystal structure of Escherichia coli FocA at 2.25 A resolution. FocA forms a symmetric pentamer, with each protomer consisting of six transmembrane segments. Despite a lack of sequence homology, the overall structure of the FocA protomer closely resembles that of aquaporin and strongly argues that FocA is a channel, rather than a transporter. Structural analysis identifies potentially important channel residues, defines the channel path and reveals two constriction sites. Unlike aquaporin, FocA is impermeable to water but allows the passage of formate. A structural and biochemical investigation provides mechanistic insights into the channel activity of FocA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Yi -- Huang, Yongjian -- Wang, Jiawei -- Cheng, Chao -- Huang, Weijiao -- Lu, Peilong -- Xu, Ya-Nan -- Wang, Pengye -- Yan, Nieng -- Shi, Yigong -- England -- Nature. 2009 Nov 26;462(7272):467-72. doi: 10.1038/nature08610.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Ministry of Education Protein Science Laboratory, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University, Beijing 100084, China.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19940917" target="_blank"〉PubMed〈/a〉
    Keywords: Aquaporins/*chemistry/metabolism ; Crystallography, X-Ray ; Escherichia coli/chemistry/genetics/metabolism ; Escherichia coli Proteins/*chemistry/genetics/metabolism ; Formates/metabolism ; Liposomes/chemistry/metabolism ; Membrane Transport Proteins/*chemistry/genetics/metabolism ; Models, Molecular ; Molecular Mimicry ; Mutation ; Permeability ; Protein Structure, Quaternary ; Structure-Activity Relationship ; Water/analysis/metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 5
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    Direct ubiquitination of pattern recognition receptor FLS2 attenuates plant innate immunity (2011)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2011-06-18
    Description: Innate immune responses are triggered by the activation of pattern-recognition receptors (PRRs). The Arabidopsis PRR FLAGELLIN-SENSING 2 (FLS2) senses bacterial flagellin and initiates immune signaling through association with BAK1. The molecular mechanisms underlying the attenuation of FLS2 activation are largely unknown. We report that flagellin induces recruitment of two closely related U-box E3 ubiquitin ligases, PUB12 and PUB13, to FLS2 receptor complex in Arabidopsis. BAK1 phosphorylates PUB12 and PUB13 and is required for FLS2-PUB12/13 association. PUB12 and PUB13 polyubiquitinate FLS2 and promote flagellin-induced FLS2 degradation, and the pub12 and pub13 mutants displayed elevated immune responses to flagellin treatment. Our study has revealed a unique regulatory circuit of direct ubiquitination and turnover of FLS2 by BAK1-mediated phosphorylation and recruitment of specific E3 ligases for attenuation of immune signaling.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3243913/" 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/PMC3243913/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lu, Dongping -- Lin, Wenwei -- Gao, Xiquan -- Wu, Shujing -- Cheng, Cheng -- Avila, Julian -- Heese, Antje -- Devarenne, Timothy P -- He, Ping -- Shan, Libo -- R01 GM092893/GM/NIGMS NIH HHS/ -- R01 GM092893-02/GM/NIGMS NIH HHS/ -- R01 GM097247/GM/NIGMS NIH HHS/ -- R01GM092893/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2011 Jun 17;332(6036):1439-42. doi: 10.1126/science.1204903.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21680842" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Arabidopsis/genetics/*immunology/metabolism/microbiology ; Arabidopsis Proteins/chemistry/genetics/*metabolism ; Flagellin/*immunology ; *Immunity, Innate ; Molecular Sequence Data ; Mutant Proteins/chemistry/metabolism ; Peptide Fragments/immunology ; Phosphorylation ; Plant Diseases/*immunology/microbiology ; Protein Interaction Domains and Motifs ; Protein Kinases/chemistry/*metabolism ; Protein-Serine-Threonine Kinases/*metabolism ; Pseudomonas syringae/growth & development/immunology ; Receptors, Pattern Recognition/chemistry/*metabolism ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Ubiquitin-Protein Ligases/chemistry/genetics/*metabolism ; Ubiquitinated Proteins/metabolism ; Ubiquitination
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 6
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    Chemical genomic profiling for antimalarial therapies, response signatures, and molecular targets (2011)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2011-08-06
    Description: Malaria remains a devastating disease largely because of widespread drug resistance. New drugs and a better understanding of the mechanisms of drug action and resistance are essential for fulfilling the promise of eradicating malaria. Using high-throughput chemical screening and genome-wide association analysis, we identified 32 highly active compounds and genetic loci associated with differential chemical phenotypes (DCPs), defined as greater than or equal to fivefold differences in half-maximum inhibitor concentration (IC(50)) between parasite lines. Chromosomal loci associated with 49 DCPs were confirmed by linkage analysis and tests of genetically modified parasites, including three genes that were linked to 96% of the DCPs. Drugs whose responses mapped to wild-type or mutant pfcrt alleles were tested in combination in vitro and in vivo, which yielded promising new leads for antimalarial treatments.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3396183/" 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/PMC3396183/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yuan, Jing -- Cheng, Ken Chih-Chien -- Johnson, Ronald L -- Huang, Ruili -- Pattaradilokrat, Sittiporn -- Liu, Anna -- Guha, Rajarshi -- Fidock, David A -- Inglese, James -- Wellems, Thomas E -- Austin, Christopher P -- Su, Xin-zhuan -- R01 AI050234/AI/NIAID NIH HHS/ -- R01 AI50234/AI/NIAID NIH HHS/ -- ZIB HG200319-08/Intramural NIH HHS/ -- New York, N.Y. -- Science. 2011 Aug 5;333(6043):724-9. doi: 10.1126/science.1205216.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Malaria and Vector Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21817045" target="_blank"〉PubMed〈/a〉
    Keywords: Antimalarials/chemistry/*pharmacology ; Biological Evolution ; Chromosome Mapping ; Drug Combinations ; *Drug Resistance/genetics ; *Genes, Protozoan ; Genetic Linkage ; Genetic Loci ; *Genome, Protozoan ; Genome-Wide Association Study ; High-Throughput Screening Assays ; Inhibitory Concentration 50 ; Membrane Transport Proteins/genetics ; Molecular Structure ; Multidrug Resistance-Associated Proteins/genetics ; Mutation ; *Parasitic Sensitivity Tests ; Plasmodium falciparum/*drug effects/*genetics/growth & development/metabolism ; Polymorphism, Single Nucleotide ; Protozoan Proteins/genetics ; Structure-Activity Relationship
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    SLC24A5, a putative cation exchanger, affects pigmentation in zebrafish and humans (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-12-17
    Description: Lighter variations of pigmentation in humans are associated with diminished number, size, and density of melanosomes, the pigmented organelles of melanocytes. Here we show that zebrafish golden mutants share these melanosomal changes and that golden encodes a putative cation exchanger slc24a5 (nckx5) that localizes to an intracellular membrane, likely the melanosome or its precursor. The human ortholog is highly similar in sequence and functional in zebrafish. The evolutionarily conserved ancestral allele of a human coding polymorphism predominates in African and East Asian populations. In contrast, the variant allele is nearly fixed in European populations, is associated with a substantial reduction in regional heterozygosity, and correlates with lighter skin pigmentation in admixed populations, suggesting a key role for the SLC24A5 gene in human pigmentation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lamason, Rebecca L -- Mohideen, Manzoor-Ali P K -- Mest, Jason R -- Wong, Andrew C -- Norton, Heather L -- Aros, Michele C -- Jurynec, Michael J -- Mao, Xianyun -- Humphreville, Vanessa R -- Humbert, Jasper E -- Sinha, Soniya -- Moore, Jessica L -- Jagadeeswaran, Pudur -- Zhao, Wei -- Ning, Gang -- Makalowska, Izabela -- McKeigue, Paul M -- O'donnell, David -- Kittles, Rick -- Parra, Esteban J -- Mangini, Nancy J -- Grunwald, David J -- Shriver, Mark D -- Canfield, Victor A -- Cheng, Keith C -- CA73935/CA/NCI NIH HHS/ -- EY11308/EY/NEI NIH HHS/ -- HD37572/HD/NICHD NIH HHS/ -- HD40179/HD/NICHD NIH HHS/ -- HG002154/HG/NHGRI NIH HHS/ -- HL077910/HL/NHLBI NIH HHS/ -- RR017441/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2005 Dec 16;310(5755):1782-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Jake Gittlen Cancer Research Foundation, Department of Pathology, The Pennsylvania State University College of Medicine, Hershey, PA 17033, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16357253" target="_blank"〉PubMed〈/a〉
    Keywords: African Americans/genetics ; African Continental Ancestry Group/genetics ; Alanine/genetics ; Alleles ; Amino Acid Sequence ; Animals ; Antiporters/chemistry/*genetics/physiology ; Asian Continental Ancestry Group/genetics ; Biological Evolution ; Calcium/metabolism ; European Continental Ancestry Group/genetics ; Gene Frequency ; Genes ; Genetic Variation ; Haplotypes ; Heterozygote ; Humans ; Ion Transport ; Melanins/analysis ; Melanosomes/chemistry/ultrastructure ; Mice ; Molecular Sequence Data ; Multifactorial Inheritance ; Mutation ; Pigment Epithelium of Eye/chemistry/ultrastructure ; Polymorphism, Single Nucleotide ; Selection, Genetic ; Skin Pigmentation/*genetics ; Threonine/genetics ; Zebrafish/embryology/*genetics/metabolism ; Zebrafish Proteins/chemistry/*genetics/physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 8
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    Cell corpse engulfment mediated by C. elegans phosphatidylserine receptor through CED-5 and CED-12 (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-12-04
    Description: During apoptosis, phosphatidylserine, which is normally restricted to the inner leaflet of the plasma membrane, is exposed on the surface of apoptotic cells and has been suggested to act as an "eat-me" signal to trigger phagocytosis. It is unclear how phagocytes recognize phosphatidylserine. Recently, a putative phosphatidylserine receptor (PSR) was identified and proposed to mediate recognition of phosphatidylserine and phagocytosis. We report that psr-1, the Caenorhabditis elegans homolog of PSR, is important for cell corpse engulfment. In vitro PSR-1 binds preferentially phosphatidylserine or cells with exposed phosphatidylserine. In C. elegans, PSR-1 acts in the same cell corpse engulfment pathway mediated by intracellular signaling molecules CED-2 (homologous to the human CrkII protein), CED-5 (DOCK180), CED-10 (Rac GTPase), and CED-12 (ELMO), possibly through direct interaction with CED-5 and CED-12. Our findings suggest that PSR-1 is likely an upstream receptor for the signaling pathway containing CED-2, CED-5, CED-10, and CED-12 proteins and plays an important role in recognizing phosphatidylserine during phagocytosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Xiaochen -- Wu, Yi-Chun -- Fadok, Valerie A -- Lee, Ming-Chia -- Gengyo-Ando, Keiko -- Cheng, Li-Chun -- Ledwich, Duncan -- Hsu, Pei-Ken -- Chen, Jia-Yun -- Chou, Bin-Kuan -- Henson, Peter -- Mitani, Shohei -- Xue, Ding -- New York, N.Y. -- Science. 2003 Nov 28;302(5650):1563-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder, CO 80309, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14645848" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Animals ; *Apoptosis ; Caenorhabditis elegans/cytology/embryology/metabolism/*physiology ; Caenorhabditis elegans Proteins/genetics/*metabolism ; Carrier Proteins/genetics/*metabolism ; *Cytoskeletal Proteins ; Embryo, Nonmammalian/cytology/metabolism ; Embryonic Development ; Humans ; Jumonji Domain-Containing Histone Demethylases ; Membrane Proteins/genetics/*metabolism ; Molecular Sequence Data ; Mutation ; *Phagocytosis ; Phosphatidylserines/metabolism ; Protein Binding ; Receptors, Cell Surface/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Recombinant Proteins/metabolism ; Signal Transduction ; rac GTP-Binding Proteins/genetics/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
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    Phase transitions in the assembly of multivalent signalling proteins (2012)
    Nature Publishing Group (NPG)
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    Publication Date: 2012-03-09
    Description: Cells are organized on length scales ranging from angstrom to micrometres. However, the mechanisms by which angstrom-scale molecular properties are translated to micrometre-scale macroscopic properties are not well understood. Here we show that interactions between diverse synthetic, multivalent macromolecules (including multi-domain proteins and RNA) produce sharp liquid-liquid-demixing phase separations, generating micrometre-sized liquid droplets in aqueous solution. This macroscopic transition corresponds to a molecular transition between small complexes and large, dynamic supramolecular polymers. The concentrations needed for phase transition are directly related to the valency of the interacting species. In the case of the actin-regulatory protein called neural Wiskott-Aldrich syndrome protein (N-WASP) interacting with its established biological partners NCK and phosphorylated nephrin, the phase transition corresponds to a sharp increase in activity towards an actin nucleation factor, the Arp2/3 complex. The transition is governed by the degree of phosphorylation of nephrin, explaining how this property of the system can be controlled to regulatory effect by kinases. The widespread occurrence of multivalent systems suggests that phase transitions may be used to spatially organize and biochemically regulate information throughout biology.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3343696/" 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/PMC3343696/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, Pilong -- Banjade, Sudeep -- Cheng, Hui-Chun -- Kim, Soyeon -- Chen, Baoyu -- Guo, Liang -- Llaguno, Marc -- Hollingsworth, Javoris V -- King, David S -- Banani, Salman F -- Russo, Paul S -- Jiang, Qiu-Xing -- Nixon, B Tracy -- Rosen, Michael K -- P30 CA142543/CA/NCI NIH HHS/ -- P41 GM103622/GM/NIGMS NIH HHS/ -- R01 GM056322/GM/NIGMS NIH HHS/ -- R01 GM056322-13/GM/NIGMS NIH HHS/ -- R01-GM088745/GM/NIGMS NIH HHS/ -- R01-GM56322/GM/NIGMS NIH HHS/ -- RR-08630/RR/NCRR NIH HHS/ -- Howard Hughes Medical Institute/ -- England -- Nature. 2012 Mar 7;483(7389):336-40. doi: 10.1038/nature10879.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, Texas 75390-8812, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22398450" target="_blank"〉PubMed〈/a〉
    Keywords: Actin-Related Protein 2-3 Complex/metabolism ; Adaptor Proteins, Signal Transducing/chemistry/metabolism ; Binding Sites ; Biopolymers/chemistry/metabolism ; Fluorescence Recovery After Photobleaching ; HeLa Cells ; Humans ; Ligands ; Membrane Proteins/chemistry/metabolism ; Multiprotein Complexes/*chemistry/*metabolism ; Oncogene Proteins/chemistry/metabolism ; *Phase Transition ; Phosphorylation ; Proline-Rich Protein Domains ; Protein Structure, Quaternary ; Proteins/*chemistry/*metabolism ; *Signal Transduction ; Wiskott-Aldrich Syndrome Protein, Neuronal/chemistry/metabolism ; src Homology Domains
    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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  • 10
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    Separable regulatory elements governing myogenin transcription in mouse embryogenesis (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-07-09
    Description: Expression of the myogenic helix-loop-helix (HLH) protein myogenin in muscle cell precursors within somites and limb buds is among the earliest events associated with myogenic lineage determination in vertebrates. Mutations in the myogenin promoter that abolish binding sites for myogenic HLH proteins or myocyte enhancer factor-2 (MEF-2) suppressed transcription of a linked lacZ transgene in subsets of myogenic precursors in mouse embryos. These results suggest that myogenic HLH proteins and MEF-2 participate in separable regulatory circuits leading to myogenin transcription and provide evidence for positional regulation of myogenic regulators in the embryo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cheng, T C -- Wallace, M C -- Merlie, J P -- Olson, E N -- New York, N.Y. -- Science. 1993 Jul 9;261(5118):215-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, University of Texas M.D. Anderson Cancer Center, Houston 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8392225" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; DNA-Binding Proteins/genetics/metabolism ; Embryo, Mammalian/*metabolism ; Extremities/embryology ; Female ; MEF2 Transcription Factors ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Inbred CBA ; Mice, Transgenic ; Muscle Proteins/*genetics ; Muscles/*embryology/metabolism ; Mutation ; Myogenic Regulatory Factors ; Myogenin ; Promoter Regions, Genetic ; Trans-Activators/*genetics ; Transcription Factors/genetics/metabolism ; *Transcription, Genetic
    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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