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34 results on '"Clapham, D.E."'

1. Structure of SARS-CoV-2 Orf3a in plasma membrane-like environment, MSP1D1 nanodisc

Author

Miller, A.N., primary, Houlihan, P.R., additional, Matamala, E., additional, Cabezas-Bratesco, D., additional, Lee, G.Y., additional, Cristofori-Armstrong, B., additional, Dilan, T.L., additional, Sanchez-Martinez, S., additional, Matthies, D., additional, Yan, R., additional, Yu, Z., additional, Ren, D., additional, Brauchi, S.E., additional, and Clapham, D.E., additional

Published
2023
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2. Structure of SARS-CoV-1 Orf3a in late endosome/lysosome-like environment, MSP1D1 nanodisc

Author

Miller, A.N., primary, Houlihan, P.R., additional, Matamala, E., additional, Cabezas-Bratesco, D., additional, Lee, G.Y., additional, Cristofori-Armstrong, B., additional, Dilan, T.L., additional, Sanchez-Martinez, S., additional, Matthies, D., additional, Yan, R., additional, Yu, Z., additional, Ren, D., additional, Brauchi, S.E., additional, and Clapham, D.E., additional

Published
2023
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3. Structure of SARS-CoV-2 Orf3a in late endosome/lysosome-like environment, Saposin A nanodisc

Author

Miller, A.N., primary, Houlihan, P.R., additional, Matamala, E., additional, Cabezas-Bratesco, D., additional, Lee, G.Y., additional, Cristofori-Armstrong, B., additional, Dilan, T.L., additional, Sanchez-Martinez, S., additional, Matthies, D., additional, Yan, R., additional, Yu, Z., additional, Ren, D., additional, Brauchi, S.E., additional, and Clapham, D.E., additional

Published
2023
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4. Structure of SARS-CoV-2 Orf3a in late endosome/lysosome-like membrane environment, MSP1D1 nanodisc

Author

Miller, A.N., primary, Houlihan, P.R., additional, Matamala, E., additional, Cabezas-Bratesco, D., additional, Lee, G.Y., additional, Cristofori-Armstrong, B., additional, Dilan, T.L., additional, Sanchez-Martinez, S., additional, Matthies, D., additional, Yan, R., additional, Yu, Z., additional, Ren, D., additional, Brauchi, S.E., additional, and Clapham, D.E., additional

Published
2023
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5. Primary cilia are not calcium-responsive mechanosensors

Author

Delling, M., Indzhykulian, A., Liu, X., Li, Y., Xie, T., Corey, D.P., and Clapham, D.E.

Subjects
Research, Calcium metabolism -- Research, Mechanoreceptors -- Research, Kidney research, Cilia -- Research, Kidney diseases -- Research, Cilia and ciliary motion -- Research
Abstract

Primary cilia are solitary, generally non-motile, hair-like protrusions that extend from the surface of cells between cell divisions. Their antenna-like structure leads naturally to the assumption that they sense the [...]

Published
2016

7. Melanopsin signalling in mammalian iris and retina

Author

Xue, T., Do, M.T.H., Riccio, A., Jiang, Z., Hsieh, J., Wang, H.C., Merbs, S.L., Welsbie, D.S., Yoshioka, T., Weissgerber, P., Stolz, S., Flockerzi, V., Freichel, M., Simon, M.I., Clapham, D.E., and Yau, K.-W.

Subjects
Physiological aspects, Research, Retina -- Physiological aspects -- Research, Melanopsin -- Physiological aspects -- Research, Iris (Eye) -- Physiological aspects -- Research
Abstract

The discovery of ipRGCs has overturned the century-old belief that rods and cones are the only mammalian retinal photoreceptors (1-6). These ganglion-cell photoreceptors serve primarily non-image visual functions, one of [...], Non-mammalian vertebrates have an intrinsically photosensitive iris and thus a local pupillary light reflex (PLR). In contrast, it is thought that the PLR in mammals generally requires neuronal circuitry connecting the eye and the brain. Here we report that an intrinsic component of the PLR is in fact widespread in nocturnal and crepuscular mammals. In mouse, this intrinsic PLR requires the visual pigment melanopsin; it also requires PLCβ4, a vertebrate homologue of the Drosophila NorpA phospholipase C which mediates rhabdomeric phototransduction. The [Plcb4.sup.-/-] genotype, in addition to removing the intrinsic PLR, also essentially eliminates the intrinsic light response of the M1 subtype of melanopsin-expressing, intrinsically photosensitive retinal ganglion cells (M1-ipRGCs), which are by far the most photosensitive ipRGC subtype and also have the largest response to light. Ablating in mouse the expression of both TRPC6 and TRPC7, members of the TRP channel superfamily, also essentially eliminated the M1-ipRGC light response but the intrinsic PLR was not affected. Thus, melanopsin signalling exists in both iris and retina, involving a PLCβ4-mediated pathway that nonetheless diverges in the two locations.

Published
2011
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10. The G-protein-gated atrial K+ channel I(KACh) is a heteromultimer of two inwardly rectifying K(+)-channel proteins

Author

Krapivinsky, G., Gordon, E.A., Wickman, K., Velimirovic, B., Krapivinsky, L., and Clapham, D.E.

Subjects
G proteins -- Research, Potassium in the body -- Research, Potassium metabolism -- Research, Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

The structure of the native I(KACh), an inward rectifier of the potassium ion channel family, is found to be made up of two homologus subunits with GIRK1 and CIR gene products. The structure of the I(KACh) is determined by the use of antibodies specific to the encoding regions of the rectifier. The I(KACh) structure will enable the study at the process of regulation of the G proteins.

Published
1995

12. 3.3 angstrom structure of mouse TRPM7 with EDTA

Author

Zhang, J., primary, Li, Z., additional, Duan, J., additional, Li, J., additional, Hulse, R.E., additional, Santa-Cruz, A., additional, Abiria, S.A., additional, Krapivinsky, G., additional, and Clapham, D.E., additional

Published
2018
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15. Human Polycsytin 2-l1

Author

Hulse, R.E., primary, Clapham, D.E., additional, Li, Z., additional, Huang, R.K., additional, and Zhang, J., additional

Published
2018
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17. Role of the C-terminal domain in the structure and function of tetrameric sodium channels

Author

Bagneris, Claire, DeCaen, P.G., Hall, B.A., Naylor, Claire E., Clapham, D.E., Kay, C.W.M., and Wallace, Bonnie A.

Subjects
bcs
Abstract

Voltage-gated sodium channels have essential roles in electrical signalling. Prokaryotic sodium channels are tetramers consisting of transmembrane (TM) voltage-sensing and pore domains, and a cytoplasmic carboxy-terminal domain. Previous crystal structures of bacterial sodium channels revealed the nature of their TM domains but not their C-terminal domains (CTDs). Here, using electron paramagnetic resonance (EPR) spectroscopy combined with molecular dynamics, we show that the CTD of the NavMs channel from Magnetococcus marinus includes a flexible region linking the TM domains to a four-helix coiled-coil bundle. A 2.9 Å resolution crystal structure of the NavMs pore indicates the position of the CTD, which is consistent with the EPR-derived structure. Functional analyses demonstrate that the coiled-coil domain couples inactivation with channel opening, and is enabled by negatively charged residues in the linker region. A mechanism for gating is proposed based on the structure, whereby splaying of the bottom of the pore is possible without requiring unravelling of the coiled-coil.

Published
2013

18. Molecular dynamics of ion transport through the open conformation of a bacterial voltage-gated sodium channel

Author

Ulmschneider, Martin B., Bagneris, Claire, McCusker, Emily C., DeCaen, P.G., Delling, M., Clapham, D.E., Ulmschneider, J.P., and Wallace, Bonnie A.

Subjects
bcs
Abstract

The crystal structure of the open conformation of a bacterial voltage-gated sodium channel pore from Magnetococcus sp. (NaVMs) has provided the basis for a molecular dynamics study defining the channel’s full ion translocation pathway and conductance process, selectivity, electrophysiological characteristics, and ion-binding sites. Microsecond molecular dynamics simulations permitted a complete time-course characterization of the protein in a membrane system, capturing the plethora of conductance events and revealing a complex mixture of single and multi-ion phenomena with decoupled rapid bidirectional water transport. The simulations suggest specific localization sites for the sodium ions, which correspond with experimentally determined electron density found in the selectivity filter of the crystal structure. These studies have also allowed us to identify the ion conductance mechanism and its relation to water movement for the NavMs channel pore and to make realistic predictions of its conductance properties. The calculated single-channel conductance and selectivity ratio correspond closely with the electrophysiology measurements of the NavMs channel expressed in HEK 293 cells. The ion translocation process seen in this voltage-gated sodium channel is clearly different from that exhibited by members of the closely related family of voltage-gated potassium channels and also differs considerably from existing proposals for the conductance process in sodium channels. These studies simulate sodium channel conductance based on an experimentally determined structure of a sodium channel pore that has a completely open transmembrane pathway and activation gate.

Published
2013

19. Calbindin-D28K dynamically controls TRPV5-mediated Ca2+ transport.

Author

Lambers, T.T., Mahieu, F., Oancea, E., Hoofd, L.J.C., Lange, F. de, Mensenkamp, A.R., Voets, T., Nilius, B., Clapham, D.E., Hoenderop, J.G.J., Bindels, R.J.M., Lambers, T.T., Mahieu, F., Oancea, E., Hoofd, L.J.C., Lange, F. de, Mensenkamp, A.R., Voets, T., Nilius, B., Clapham, D.E., Hoenderop, J.G.J., and Bindels, R.J.M.

Abstract

Contains fulltext : 49350.pdf (publisher's version ) (Closed access), In Ca(2+)-transporting epithelia, calbindin-D(28K) (CaBP(28K)) facilitates Ca(2+) diffusion from the luminal Ca(2+) entry side of the cell to the basolateral side, where Ca(2+) is extruded into the extracellular compartment. Simultaneously, CaBP(28K) provides protection against toxic high Ca(2+) levels by buffering the cytosolic Ca(2+) concentration ([Ca(2+)](i)) during high Ca(2+) influx. CaBP(28K) consistently colocalizes with the epithelial Ca(2+) channel TRPV5, which constitutes the apical entry step in renal Ca(2+)-transporting epithelial cells. Here, we demonstrate using protein-binding analysis, subcellular fractionation and evanescent-field microscopy that CaBP(28K) translocates towards the plasma membrane and directly associates with TRPV5 at a low [Ca(2+)](i). (45)Ca(2+) uptake measurements, electrophysiological recordings and transcellular Ca(2+) transport assays of lentivirus-infected primary rabbit connecting tubule/distal convolute tubule cells revealed that associated CaBP(28K) tightly buffers the flux of Ca(2+) entering the cell via TRPV5, facilitating high Ca(2+) transport rates by preventing channel inactivation. In summary, CaBP(28K) acts in Ca(2+)-transporting epithelia as a dynamic Ca(2+) buffer, regulating [Ca(2+)] in close vicinity to the TRPV5 pore by direct association with the channel.

Published
2006

20. A unified nomenclature for the superfamily of TRP cation channels.

Author

Montell, C., Birnbaumer, L., Flockerzi, V., Bindels, R.J.M., Bruford, E.A., Caterina, M.J., Clapham, D.E., Harteneck, C., Heller, S., Julius, D., Kojima, I., Mori, Y., Penner, R., Prawitt, D., Scharenberg, A.M., Schultz, G., Shimizu, N., Zhu, M., Montell, C., Birnbaumer, L., Flockerzi, V., Bindels, R.J.M., Bruford, E.A., Caterina, M.J., Clapham, D.E., Harteneck, C., Heller, S., Julius, D., Kojima, I., Mori, Y., Penner, R., Prawitt, D., Scharenberg, A.M., Schultz, G., Shimizu, N., and Zhu, M.

Abstract

Item does not contain fulltext

Published
2002

26. Functional Expression and Characterization of G-protein-gated Inwardly Rectifying K+ Channels Containing GIRK3

Author

Jelacic, T.M., Sims, S.M., and Clapham, D.E.

Abstract

Abstract.: The G-protein-gated inwardly rectifying K +(GIRK) family of ion channels form functional Gβγ-sensitive channels as heteromultimers of GIRK1 and either the GIRK2 or GIRK4 subunits. However, the homologous mouse brain GIRK3 clone failed to express in the earliest reported functional experiments in Xenopus oocytes. We recloned the GIRK3 subunit from mouse brain and found that the new clone differed significantly from that originally reported. The functional aspects of GIRK3 were reinvestigated by expression in CHO cells. The single channel properties of GIRK1/GIRK3 were characterized and compared to those of the GIRK1/GIRK2 and GIRK1/GIRK4 channels. All three GIRK1/GIRKx combinations produced channels with nearly indistinguishable conductances and kinetics. The response of GIRK1/GIRK3 to Gβγ in the 1–47 nm range was examined and found to be indistinguishable from that of GIRK1/GIRK4 channels. We conclude that GIRK1, with either GIRK2, 3, or 4, gives rise to heteromultimeric channels with virtually identical conductances, kinetics, and Gβγ sensitivities.

Published
1999
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27. Localization and Interaction of Epitope-tagged GIRK1 and CIR Inward Rectifier K+Channel Subunits

Author

KENNEDY, M.E, NEMEC, J, and CLAPHAM, D.E

Abstract

GIRK1 and CIR are G-protein activated inward rectifier K+channel subunits that combine to form the heteromultimer IKACh, the Gβγ-activated atrial K channel responsible for the vagal slowing of heart rate. Epitope-tagged channel subunits were constructed by the introduction of distinct six amino acid epitopes into the C-termini or putative extracellular domains of GIRK1 and CIR. Carboxyl-terminal tagged subunits were activated by purified Gβγsubunits in inside-out patches when expressed in Cos cells. Interestingly, insertion of three amino acids into the putative extracellular domain of GIRK1 resulted in an inactive subunit that acted as a dominant negative subunit when coexpressed with wild type GIRK1 and CIR in Xenopusoocytes. The epitope-tagged CIR-AU1 subunit coimmunoprecipitated GIRK1-AU5 from metabolically labeled Cos cells. Immunofluorescence labeling of Cos cells localized GIRK1-AU5 to internal cytoskeletal structures that co-stained with antibodies against the intermediate filament protein, vimentin. CIR-AU1 localized primarily to the plasma membrane. Double immunofluorescence labeling showed that GIRK1-AU5 plasma membrane staining was detectable only when coexpressed with CIR-AU1. Copyright © 1996 Elsevier Science Ltd

Published
1996
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28. Inositol 1,3,4,5-tretrakisphosphate activates an endothelial Ca2+ -permeable channel.

Author

Luckhoff, A. and Clapham, D.E.

Subjects
*CHEMISTRY
Abstract

Finds that Inositol 1,4,5,-triphosphate (Insp3) which induces Ca2+ influx into cinar cells, enhances the activity of the Ca2+ -permeable channel when exposed to the intracellular surface of endothelial cell inside-out patches. Results that suggest a molecular mechanism which is likely to be important for receptor-mediated Ca2+ entry. Use of patch-clamp techniques; More.

Published
1992

29. Potassium channels in cardiac cells activated by arachidonic acid and phospholipids.

Author

Kimble, D. and Clapham, D.E.

Subjects
*CARDIOVASCULAR system
Abstract

Describes two types of potassium-selective channels, found in neonatal rat atrial cells, that are activated by intracellular arachidonic acid or phosphatidylcholine. These potassium-selective channels may help explain the increase in potassium conductance observed in ischemic cells, and show that fatty acid derivatives, tested for their ability to activate potassium-selective channel conductances, may act as second messengers.

Published
1989

30. Functions of G-protein Subunits

Author

Neer, E.J., primary, Kim, S.-Y., additional, Ang, S.-L., additional, Bloch, D.B., additional, Bloch, K.D., additional, Kawahara, Y., additional, Tolman, C., additional, Lee, R., additional, Logothetis, D., additional, Kim, D., additional, Seidman, J.G., additional, and Clapham, D.E., additional

Published
1988
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34. THE CONCISE GUIDE TO PHARMACOLOGY 2017/18: Overview

Author

Alexander, S.P., Kelly, E., Marrion, N.V., Peters, J.A., Faccenda, E., Harding, S.D., Pawson, A.J., Sharman, J.L., Southan, C., Buneman, O.P., Cidlowski, J.A., Christopoulos, A., Davenport, A.P., Fabbro, D., Spedding, M., Striessnig, J., Davies, J.A., CGTP Collaborators, Abbracchio, M.P., Aldrich, R., Al-Hosaini, K., Arumugam, T.V., Attali, B., Bäck, M., Barnes, N.M., Bathgate, R., Beart, P.M., Becirovic, E., Bettler, B., Biel, M., Birdsall, N.J., Blaho, V., Boison, D., Bräuner-Osborne, H., Bröer, S., Bryant, C., Burnstock, G., Calo, G., Catterall, W.A., Ceruti, S., Chan, S.L., Chandy, K.G., Chazot, P., Chiang, N., Chun, J.J., Chung, J.J., Clapham, D.E., Clapp, L., Connor, M.A., Cox, H.M., Davies, P., Dawson, P.A., Decaen, P., Dent, G., Doherty, P., Douglas, S.D., Dubocovich, M.L., Fong, T.M., Fowler, C.J., Frantz, A., Fuller, P., Fumagalli, M., Futerman, A.H., Gainetdinov, R.R., Gershengorn, M.A., Goldin, A., Goldstein, S., Goudet, C., Gregory, K., Grissmer, S., Gundlach, A.L., Hagenbuch, B., Hamann, J., Hammond, J.R., Hancox, J.C., Hanson, J., Hanukoglu, I., Hay, D.L., Hobbs, A.J., Hollenberg, A.N., Holliday, N.D., Hoyer, D., Ijzerman, A.P., Inui, K.I., Irving, A.J., Ishii, S., Jacobson, K.A., Jan, L.Y., Jarvis, M.F., Jensen, R., Jockers, R., Kaczmarek, L.K., Kanai, Y., Karnik, S., Kellenberger, S., Kemp, S., Kennedy, C., Kerr, I.D., Kihara, Y., Kukkonen, J., Larhammar, D., Leach, K., Lecca, D., Leeman, S., Leprince, J., Lolait, S.J., Macewan, D., Maguire, J.J., Marshall, F., Mazella, J., Mcardle, C.A., Michel, M.C., Miller, L.J., Mitolo, V., Mizuno, H., Monk, P.N., Mouillac, B., Murphy, P.M., Nahon, J.L., Nerbonne, J., Nichols, C.G., Norel, X., Offermanns, S., Palmer, L.G., Panaro, M.A., Papapetropoulos, A., Perez-Reyes, E., Pertwee, R.G., Pintor, S., Pisegna, J.R., Plant, L.D., Poyner, D.R., Prossnitz, E.R., Pyne, S., Ramachandran, R., Ren, D., Rondard, P., Ruzza, C., Sackin, H., Sanger, G., Sanguinetti, M.C., Schild, L., Schiöth, H., Schulte, G., Schulz, S., Segaloff, D.L., Serhan, C.N., Singh, K.D., Slesinger, P.A., Snutch, T.P., Sobey, C.G., Stewart, G., Stoddart, L.A., Summers, R.J., Szabo, C., Thwaites, D., Toll, L., Trimmer, J.S., Tucker, S., Vaudry, H., Verri, T., Vilargada, J.P., Waldman, S.A., Ward, D.T., Waxman, S.G., Wei, A.D., Willars, G.B., Wong, S.S., Woodruff, T.M., Wulff, H., Ye, R.D., Yung, Y., and Zajac, J.M.

Subjects
Databases, Pharmaceutical, Humans, Knowledge Bases, Ligands, Proteins
Abstract

The Concise Guide to PHARMACOLOGY 2017/18 is the third in this series of biennial publications. This version provides concise overviews of the key properties of nearly 1800 human drug targets with an emphasis on selective pharmacology (where available), plus links to an open access knowledgebase of drug targets and their ligands (www.guidetopharmacology.org), which provides more detailed views of target and ligand properties. Although the Concise Guide represents approximately 400 pages, the material presented is substantially reduced compared to information and links presented on the website. It provides a permanent, citable, point-in-time record that will survive database updates. The full contents of this section can be found at http://onlinelibrary.wiley.com/doi/10.1111/bph.13882/full. In addition to this overview, in which are identified 'Other protein targets' which fall outside of the subsequent categorisation, there are eight areas of focus: G protein-coupled receptors, ligand-gated ion channels, voltage-gated ion channels, other ion channels, nuclear hormone receptors, catalytic receptors, enzymes and transporters. These are presented with nomenclature guidance and summary information on the best available pharmacological tools, alongside key references and suggestions for further reading. The landscape format of the Concise Guide is designed to facilitate comparison of related targets from material contemporary to mid-2017, and supersedes data presented in the 2015/16 and 2013/14 Concise Guides and previous Guides to Receptors and Channels. It is produced in close conjunction with the Nomenclature Committee of the Union of Basic and Clinical Pharmacology (NC-IUPHAR), therefore, providing official IUPHAR classification and nomenclature for human drug targets, where appropriate.

Published
2017

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