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Gutierrez L, Zubow K, Nield J, Gambis A, Mollereau B, Lazaro FJ, Missirlis F
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Biophysical and genetic analysis of iron partitioning and ferritin function in Drosophila melanogaster
METALLOMICS 2013; 5(8):997-1005
Metals have vital functions as prosthetic groups in enzymes, but in labile form they can propagate oxidative stress. The primary function of ferritin is to store bioavailable iron in the form of ferrihydrite. In animals, ferritin is also used to traffic and recycle iron, and to modulate intestinal iron absorption. However, the effect of ferritin accumulation on cellular iron bioavailability remains poorly understood. Moreover, putative in vivo interactions of ferritin with other metal ions have been proposed, but their physiological relevance remains unclear. Here, heterozygous mutant and overexpression ferritin strains of Drosophila melanogaster were subjected to dietary iron manipulations to study the dynamics of iron partition between ferritin and other proteins. Quantitative magnetic analysis of whole fly samples indicated that iron loading of the ferritin core varied in the different genotypes. Total paramagnetic iron content, a likely correlate of bioavailable iron, was reduced in flies overexpressing ferritin when compared with control white flies. Further, three-dimensional maps of the ferritin protein shell and iron core were obtained from single particle transmission electron microscopy imaging and confirmed the similarity between Drosophila and Trichoplusia ferritin structures. Purified Drosophila ferritin also contained small amounts of zinc and manganese. Flies that overexpressed ferritin accumulated in their bodies half the amount of manganese compared to their respective controls. Our results indicate that ferritin may be involved in the homeostasis of other divalent metals, besides iron, and that overexpression of ferritin, sometimes employed to rescue neurodegenerative models of disease, serves to limit divalent metal bio-availability in cells.
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Malik S, Mesropian C, Arora S, Barker A, Chou JP, Contreras-Campana C, Contreras-Campana E, Duggan D, Ferencek D, Gershtein Y, Gray R, Halkiadakis E, Hidas D, Lath A, Panwalkar S, Park M, Patel R, Rekovic V, Robles J, Rose K, Salur S, Schnetzer S, Seitz C, Somalwar S, Stone R, Thomas S, Cerizza G, Hollingsworth M, Spanier S, Yang ZC, York A, Eusebi R, Flanagan W, Gilmore J, Kamon T, Khotilovich V, Montalvo R, Osipenkov I, Pakhotin Y, Perloff A, Roe J, Safonov A, Sakuma T, Sengupta S, Suarez I, Tatarinov A, Toback D, Akchurin N, Damgov J, Dudero PR, Jeong C, Kovitanggoon K, Lee SW, Libeiro T, Roh Y, Volobouev I, Appelt E, Delannoy AG, Florez C, Greene S, Gurrola A, Johns W, Johnston C, Kurt P, Maguire C, Melo A, Sharma M, Sheldon P, Snook B, Tuo S, Velkovska J, Arenton MW, Balazs M, Boutle S, Cox B, Francis B, Goodell J, Hirosky R, Ledovskoy A, Lin C, Neu C, Wood J, Yohay R, Gollapinni S, Harr R, Karchin PE, Don CKK, Lamichhane P, Sakharov A, Anderson M, Bachtis M, Belknap D, Borrello L, Carlsmith D, Cepeda M, Dasu S, Friis E, Gray L, Grogg KS, Grothe M, Hall-Wilton R, Herndon M, Herve A, Klabbers P, Klukas J, Lanaro A, Lazaridis C, Leonard J, Loveless R, Mohapatra A, Ojalvo I, Palmonari F, Pierro GA, Ross I, Savin A, Smith WH, Swanson J
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Observation of a diffractive contribution to dijet production in proton-proton collisions at root s = 7 TeV
PHYSICAL REVIEW D 2013 JAN 8; 87(1):? Article 012006
The cross section for dijet production in proton-proton collisions at root s = 7 TeV is presented as a function of (xi) over tilde, a variable that approximates the fractional momentum loss of the scattered proton in single-diffractive events. The analysis is based on an integrated luminosity of 2.7 nb(-1) collected with the CMS detector at the LHC at low instantaneous luminosities, and uses events with jet transverse momentum of at least 20 GeV. The dijet cross section results are compared to the predictions of diffractive and non-diffractive models. The low-(xi) over tilde data show a significant contribution from diffractive dijet production, observed for the first time at the LHC. The associated rapidity gap survival probability is estimated. DOI: 10.1103/PhysRevD.87.012006
Guermonprez Pierre, Helft Julie, Claser Carla, Deroubaix Stephanie, Karanje Henry, Gazumyan Anna, Darasse-Jeze Guillaume, Telerman Stephanie B, Breton Gaelle, Schreiber Heidi A, Frias-Staheli Natalia, Billerbeck Eva, Dorner Marcus, Rice Charles M, Ploss Alexander, Klein Florian, Swiecki Melissa, Colonna Marco, Kamphorst Alice O, Meredith Matthew, Niec Rachel, Takacs Constantin, Mikhail Fadi, Hari Aswin, Bosque David, Eisenreich Tom, Merad Miriam, Shi Yan, Ginhoux Florent, Renia Laurent, Urban Britta C, Nussenzweig Michel C
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Inflammatory Flt3l is essential to mobilize dendritic cells and for T cell responses during Plasmodium infection.
Nature medicine 2013 2013-Jun; 19(6):730-8
Innate sensing mechanisms trigger a variety of humoral and cellular events that are essential to adaptive immune responses. Here we describe an innate sensing pathway triggered by Plasmodium infection that regulates dendritic cell homeostasis and adaptive immunity through Flt3 ligand (Flt3l) release. Plasmodium-induced Flt3l release in mice requires Toll-like receptor (TLR) activation and type I interferon (IFN) production. We found that type I IFN supports the upregulation of xanthine dehydrogenase, which metabolizes the xanthine accumulating in infected erythrocytes to uric acid. Uric acid crystals trigger mast cells to release soluble Flt3l from a pre-synthesized membrane-associated precursor. During infection, Flt3l preferentially stimulates expansion of the CD8-alpha(+) dendritic cell subset or its BDCA3(+) human dendritic cell equivalent and has a substantial impact on the magnitude of T cell activation, mostly in the CD8(+) compartment. Our findings highlight a new mechanism that regulates dendritic cell homeostasis and T cell responses to infection.
Mollereau B, Perez-Garijo A, Bergmann A, Miura M, Gerlitz O, Ryoo HD, Steller H, Morata G
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Compensatory proliferation and apoptosis-induced proliferation: a need for clarification
CELL DEATH AND DIFFERENTIATION 2013 JAN; 20(1):181-181
Goulianos K
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Diffractive dijet production at CDF
DIFFRACTION 2012 2013; 1523(?):298-301
We present a CDF measurement of diffractive dijet production in (p) over barp collisions at 1.96 TeV at the Fermi lab Tevatron Collider using data from an integrated luminosity of approximate to 310 pb(-1) collected by triggering on a high transverse momentum jet in coincidence with a recoil antiproton detected in a roman pot spectrometer. We report final results for 4-momentum transfer squared t > -4 GeV2, antiproton-momentum-loss fraction within 0.03-0.09, Bjorken-x of the interacting parton in the antiproton in the range 0.001-0.1, and jet transverse energies from 10 to 100 GeV.
Dhingra Nikhil, Suarez-Farinas Mayte, Fuentes-Duculan Judilyn, Gittler Julia K, Shemer Avner, Raz Assaf, Fischetti Vincent A, Krueger James G, Guttman-Yassky Emma
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Attenuated neutrophil axis in atopic dermatitis compared to psoriasis reflects TH17 pathway differences between these diseases.
The Journal of allergy and clinical immunology 2013 2013-Aug; 132(2):498-501.e3
Foley EA, Kapoor TM
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Microtubule attachment and spindle assembly checkpoint signalling at the kinetochore
NATURE REVIEWS MOLECULAR CELL BIOLOGY 2013 JAN; 14(1):25-37
In eukaryotes, chromosome segregation during cell division is facilitated by the kinetochore, a multiprotein structure that is assembled on centromeric DNA. The kinetochore attaches chromosomes to spindle microtubules, modulates the stability of these attachments and relays the microtubule-binding status to the spindle assembly checkpoint (SAC), a cell cycle surveillance pathway that delays chromosome segregation in response to unattached kinetochores. Recent studies are shaping current thinking on how each of these kinetochore-centred processes is achieved, and how their integration ensures faithful chromosome segregation, focusing on the essential roles of kinase-phosphatase signalling and the microtubule-binding KMN protein network.
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B, Lellouch J, Marinov A, Mccartin J, Rios AAO, Ryckbosch D, Strobbe N, Thyssen F, Tytgat M, Walsh S, Yazgan E, Zaganidis N, Basegmez S, Bruno G, Castello R, Ceard L, Delaere C, du Pree T, Favart D, Forthomme L, Giammanco A, Hollar J, Lemaitre V, Liao J, Militaru O, Nuttens C, Pagano D, Pin A, Piotrzkowski K, Schul N, Garcia JMV, Beliy N, Caebergs T, Daubie E, Hammad GH, Alves GA, Martins MC, Martins T, Pol ME, Souza MHG, Alda WL, Carvalho W, Custodio A, Da Costa EM, Damiao DD, Martins CD, De Souza SF, Figueiredo DM, Mundim L, Nogima H, Da Silva WLP, Santoro A, Jorge LS, Sznajder A, Pereira AV, Anjos TS, Bernardes CA, Dias FA, Tomei TRFP, Gregores EM, Lagana C, Marinho F, Mercadante PG, Novaes SF, Padula SS, Genchev V, Iaydjiev P, Piperov S, Rodozov M, Stoykova S, Sultanov G, Tcholakov V, Trayanov R, Vutova M, Dimitrov A, Hadjiiska R, Kozhuharov V, Litov L, Pavlov B, Petkov P, Bian JG, Chen GM, Chen HS, Jiang CH, Liang D, Liang S, Meng X, Tao J, Wang J, Wang X, Wang Z, Xiao H, Xu M, 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R, Herndon M, Herve A, Klabbers P, Klukas J, Lanaro A, Lazaridis C, Leonard J, Loveless R, Mohapatra A, Ojalvo I, Palmonari F, Pierro GA, Ross I, Savin A, Smith WH, Swanson J
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Measurement of the ZZ production cross section and search for anomalous couplings in 2l2l' final states in pp collisions at root s=7 TeV
JOURNAL OF HIGH ENERGY PHYSICS 2013 JAN; ?(1):? Article 063
A measurement is presented of the ZZ production cross section in the ZZ -> 2l2l' decay mode with l = e, mu and l' = e, mu, tau in proton-proton collisions at root s = 7 TeV with the CMS experiment at the LHC. Results are based on data corresponding to an integrated luminosity of 5.0 fb(-1). The measured cross section sigma(pp -> ZZ) = 6.24(-080)(+0.86) (stat.)(-0.32)(+0.41) (syst.) +/- 0.14 (lumi.) pb is consistent with the standard model predictions. The following limits on ZZZ and ZZ-gamma anomalous trilinear gauge couplings are set at 95% confidence level: -0.011 < f(4)(Z) < 0.012, -0.012 < f(5)(Z) < 0.012, -0.013 < f(4)(gamma) < 0.015, and -0.014 < f(5)(gamma) < 0.014.
Banerjee Anirban, Lee Alice, Campbell Ernest, Mackinnon Roderick
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Structure of a pore-blocking toxin in complex with a eukaryotic voltage-dependent K(+) channel.
eLife 2013 2013 May 21; 2(?):e00594-e00594
Pore-blocking toxins inhibit voltage-dependent K(+) channels (Kv channels) by plugging the ion-conduction pathway. We have solved the crystal structure of paddle chimera, a Kv channel in complex with charybdotoxin (CTX), a pore-blocking toxin. The toxin binds to the extracellular pore entryway without producing discernable alteration of the selectivity filter structure and is oriented to project its Lys27 into the pore. The most extracellular K(+) binding site (S1) is devoid of K(+) electron-density when wild-type CTX is bound, but K(+) density is present to some extent in a Lys27Met mutant. In crystals with Cs(+) replacing K(+), S1 electron-density is present even in the presence of Lys27, a finding compatible with the differential effects of Cs(+) vs K(+) on CTX affinity for the channel. Together, these results show that CTX binds to a K(+) channel in a lock and key manner and interacts directly with conducting ions inside the selectivity filter. DOI:http://dx.doi.org/10.7554/eLife.00594.001.
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Measurement of the B-c(-) meson lifetime in the decay B-c(-) -> J/psi pi(-)
PHYSICAL REVIEW D 2013 JAN 2; 87(1):? Article 011101
The lifetime of the B-c(-) meson is measured using 272 exclusive B-c(-) -> J/psi (-> mu(+) mu(-))pi(-) decays reconstructed in data from proton-antiproton collisions corresponding to an integrated luminosity of 6.7 fb(-1) recorded by the CDF II detector at the Fermilab Tevatron. The lifetime of the B-c(-) meson is measured to be tau(B-c(-)) = 0.452 +/- 0.048(stat) +/- 0.027(syst) ps. This is the first measurement of the B-c(-) meson lifetime in a fully reconstructed hadronic channel, and it agrees with previous results and has comparable precision. DOI: 10.1103/PhysRevD.87.011101