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  • 1
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    Alteration of stimulus-specific guard cell calcium oscillations and stomatal closing in Arabidopsis det3 mutant (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-09-29
    Description: Cytosolic calcium oscillations control signaling in animal cells, whereas in plants their importance remains largely unknown. In wild-type Arabidopsis guard cells abscisic acid, oxidative stress, cold, and external calcium elicited cytosolic calcium oscillations of differing amplitudes and frequencies and induced stomatal closure. In guard cells of the V-ATPase mutant det3, external calcium and oxidative stress elicited prolonged calcium increases, which did not oscillate, and stomatal closure was abolished. Conversely, cold and abscisic acid elicited calcium oscillations in det3, and stomatal closure occurred normally. Moreover, in det3 guard cells, experimentally imposing external calcium-induced oscillations rescued stomatal closure. These data provide genetic evidence that stimulus-specific calcium oscillations are necessary for stomatal closure.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Allen, G J -- Chu, S P -- Schumacher, K -- Shimazaki, C T -- Vafeados, D -- Kemper, A -- Hawke, S D -- Tallman, G -- Tsien, R Y -- Harper, J F -- Chory, J -- Schroeder, J I -- R01 GM60396-01/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Sep 29;289(5488):2338-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell and Developmental Biology Section, Division of Biology and Center for Molecular Genetics, University of California, San Diego, La Jolla, CA 92093-0116, USA. gallen@biomail.ucsd.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11009417" target="_blank"〉PubMed〈/a〉
    Keywords: Abscisic Acid/pharmacology ; Arabidopsis/cytology/genetics/*physiology ; Calcium/metabolism ; *Calcium Signaling ; Cell Membrane/metabolism ; Cold Temperature ; Endoplasmic Reticulum/metabolism ; Genes, Plant ; Hydrogen Peroxide/pharmacology ; Membrane Potentials ; Mutation ; Oxidative Stress ; Plant Leaves/cytology/*physiology ; Potassium/metabolism ; Proton-Translocating ATPases/genetics/metabolism ; *Vacuolar Proton-Translocating ATPases ; Vacuoles/metabolism
    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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    Developmental biology. Tubulogenesis CLICs into place (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-12-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Paul, Sarah M -- Beitel, Greg J -- New York, N.Y. -- Science. 2003 Dec 19;302(5653):2077-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, IL 60208, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14684810" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Caenorhabditis elegans/cytology/*embryology/growth & development/*physiology ; Caenorhabditis elegans Proteins/chemistry/genetics/*metabolism ; Cell Membrane/metabolism ; Chloride Channels/chemistry/*metabolism ; Cytoskeleton/metabolism ; Hot Temperature ; Humans ; Intracellular Membranes/metabolism ; Ion Transport ; Membrane Fusion ; Morphogenesis ; Mutation ; Pinocytosis ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/metabolism ; Vacuoles/*metabolism/ultrastructure
    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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  • 3
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    Regulated cleavage of a contact-mediated axon repellent (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-08-26
    Description: Contact-mediated axon repulsion by ephrins raises an unresolved question: these cell surface ligands form a high-affinity multivalent complex with their receptors present on axons, yet rather than being bound, axons can be rapidly repelled. We show here that ephrin-A2 forms a stable complex with the metalloprotease Kuzbanian, involving interactions outside the cleavage region and the protease domain. Eph receptor binding triggered ephrin-A2 cleavage in a localized reaction specific to the cognate ligand. A cleavage-inhibiting mutation in ephrin-A2 delayed axon withdrawal. These studies reveal mechanisms for protease recognition and control of cell surface proteins, and, for ephrin-A2, they may provide a means for efficient axon detachment and termination of signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hattori, M -- Osterfield, M -- Flanagan, J G -- EY11559/EY/NEI NIH HHS/ -- HD29417/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 2000 Aug 25;289(5483):1360-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology and Program in Neuroscience, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10958785" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Axons/*physiology ; Cell Adhesion ; Cell Communication ; Cell Membrane/metabolism ; Cells, Cultured ; Disintegrins/genetics/*metabolism ; *Drosophila Proteins ; Ephrin-A2 ; Gene Expression ; Glycosylphosphatidylinositols/metabolism ; Growth Cones/physiology ; Humans ; Ligands ; Metalloendopeptidases/genetics/*metabolism ; Mice ; Molecular Sequence Data ; Mutation ; Nervous System/embryology/enzymology ; Receptor Protein-Tyrosine Kinases/metabolism ; Receptor, EphA3 ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Transcription Factors/chemistry/genetics/*metabolism ; Tumor Cells, Cultured
    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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  • 4
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    A seven-transmembrane RGS protein that modulates plant cell proliferation (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-09-23
    Description: G protein-coupled receptors (GPCRs) at the cell surface activate heterotrimeric G proteins by inducing the G protein alpha (Galpha) subunit to exchange guanosine diphosphate for guanosine triphosphate. Regulators of G protein signaling (RGS) proteins accelerate the deactivation of Galpha subunits to reduce GPCR signaling. Here we identified an RGS protein (AtRGS1) in Arabidopsis that has a predicted structure similar to a GPCR as well as an RGS box with GTPase accelerating activity. Expression of AtRGS1 complemented the pheromone supersensitivity phenotype of a yeast RGS mutant, sst2Delta. Loss of AtRGS1 increased the activity of the Arabidopsis Galpha subunit, resulting in increased cell elongation in hypocotyls in darkness and increased cell production in roots grown in light. These findings suggest that AtRGS1 is a critical modulator of plant cell proliferation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, Jin-Gui -- Willard, Francis S -- Huang, Jirong -- Liang, Jiansheng -- Chasse, Scott A -- Jones, Alan M -- Siderovski, David P -- GM055316/GM/NIGMS NIH HHS/ -- GM62338/GM/NIGMS NIH HHS/ -- GM65533/GM/NIGMS NIH HHS/ -- GM65989/GM/NIGMS NIH HHS/ -- R01 GM065989/GM/NIGMS NIH HHS/ -- R01 GM065989-01/GM/NIGMS NIH HHS/ -- R01 GM065989-02/GM/NIGMS NIH HHS/ -- R01 GM065989-03/GM/NIGMS NIH HHS/ -- R01 GM065989-04/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2003 Sep 19;301(5640):1728-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, The University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-3280, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14500984" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Arabidopsis/*cytology/genetics/*metabolism ; Arabidopsis Proteins/chemistry/genetics/*metabolism ; Cell Differentiation ; *Cell Division ; Cell Membrane/metabolism ; *GTP-Binding Protein alpha Subunits ; Heterotrimeric GTP-Binding Proteins/metabolism ; Meristem/metabolism ; Mitosis ; Molecular Sequence Data ; Mutation ; Open Reading Frames ; Phenotype ; Plant Roots/cytology/growth & development/metabolism ; Protein Precursors/metabolism ; Protein Structure, Tertiary ; RGS Proteins/chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; Saccharomyces cerevisiae/genetics/metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; Transgenes
    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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  • 5
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    Recycling endosomes supply AMPA receptors for LTP (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-09-28
    Description: Long-term potentiation (LTP) of synaptic strength, the most established cellular model of information storage in the brain, is expressed by an increase in the number of postsynaptic AMPA receptors. However, the source of AMPA receptors mobilized during LTP is unknown. We report that AMPA receptors are transported from recycling endosomes to the plasma membrane for LTP. Stimuli that triggered LTP promoted not only AMPA receptor insertion but also generalized recycling of cargo and membrane from endocytic compartments. Thus, recycling endosomes supply AMPA receptors for LTP and provide a mechanistic link between synaptic potentiation and membrane remodeling during synapse modification.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Park, Mikyoung -- Penick, Esther C -- Edwards, Jeffrey G -- Kauer, Julie A -- Ehlers, Michael D -- DA11289/DA/NIDA NIH HHS/ -- MH64748/MH/NIMH NIH HHS/ -- NS39402/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2004 Sep 24;305(5692):1972-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Duke University Medical Center, Box 3209, Durham, NC 27710, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15448273" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carrier Proteins/genetics/metabolism ; Cell Membrane/metabolism ; Cells, Cultured ; Endosomes/*metabolism ; Hippocampus/cytology ; *Long-Term Potentiation ; Neurons/metabolism ; Patch-Clamp Techniques ; Protein Transport ; Rats ; Rats, Sprague-Dawley ; Receptors, AMPA/*metabolism ; Synapses ; Transfection ; rab 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
    Published by American Association for the Advancement of Science (AAAS)
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