The decays h+- -> W-+ h0(a0) within an extension of the MSSM with one complex Higgs triplet

The vertex H+-W-+h0, involving the gauge bosons W-+, the charged (H+-) and the lightest neutral (h0) Higgs bosons, arises within the context of many extensions of the SM, and it can be used to probe the Higgs sector of such extensions via the decay H+- -> W+- h0. We discuss the strength of this vertex for an extension of the MSSM with an additional complex Higgs triplet. By using this model, we find regions of the parameter space where the decay H+- -> W+- h0 is not only kinematically allowed, but it also becomes an important decay mode and in some cases the dominant one.Comment: 10 figure

TRPC Channels in the SOCE Scenario

Transient receptor potential (TRP) proteins form non-selective Ca2+ permeable channels that contribute to the modulation of a number of physiological functions in a variety of cell types. Since the identification of TRP proteins in Drosophila, it is well known that these channels are activated by stimuli that induce PIP2 hydrolysis. The canonical TRP (TRPC) channels have long been suggested to be constituents of the store-operated Ca2+ (SOC) channels; however, none of the TRPC channels generate Ca2+ currents that resemble ICRAC. STIM1 and Orai1 have been identified as the components of the Ca2+ release-activated Ca2+ (CRAC) channels and there is a body of evidence supporting that STIM1 is able to gate Orai1 and TRPC1 in order to mediate non-selective cation currents named ISOC. STIM1 has been found to interact to and activate Orai1 and TRPC1 by different mechanisms and the involvement of TRPC1 in store-operated Ca2+ entry requires both STIM1 and Orai1. In addition to the participation of TRPC1 in the ISOC currents, TRPC1 and other TRPC proteins might play a relevant role modulating Orai1 channel function. This review summarizes the functional role of TRPC channels in the STIM1–Orai1 scenario.Junta de Extremadura Consejería de Economía e Infraestructura-FEDER Grant IB16046 y GR18061Junta de Extremadura TA18011 y TA18054Ministerio de Ciencia, Innovación y Universidade

EFHB is a Novel Cytosolic Ca2+ Sensor That Modulates STIM1-SARAF Interaction

Background/aims: STIM1 and Orai1 are the key components of store-operated Ca2+ entry (SOCE). Among the proteins involved in the regulation of SOCE, SARAF prevents spontaneous activation of SOCE and modulates STIM1 function. Methods: Cytosolic Ca2+ mobilization was estimated in fura-2-loaded cells using an epifluorescence inverted microscope. STIM1 interaction with Orai1, EFHB (EF-hand domain family member B, also known as CFAP21) and SARAF was detected by immunoprecipitation followed by Western blotting using specific antibodies. The involvement of EFHB in the translocation of NFAT to the nucleus was detected by confocal microscopy. Results: Here, we report the identification of EFHB as a new SOCE regulator. EFHB interacts with STIM1 upon store depletion and dissociates through a Ca2+-dependent mechanism. RNAi-mediated silencing as well as overexpression studies revealed that EFHB plays a relevant role in the interaction of STIM1 and Orai1 upon store depletion, the activation of SOCE and NFAT translocation from the cytosol to the nucleus. Silencing EFHB expression abolished the dissociation of SARAF from STIM1, which indicates that EFHB might play an important role in the dynamic interaction between both proteins, which is relevant for the activation of Orai1 channels upon Ca2+ store depletion and their subsequent modulation via slow Ca2+-dependent inactivation. Conclusion: Our results indicate that EFHB is a new SOCE regulator that modulates STIM1-SARAF interaction.MINECO BFU2013-45564-C2-1-P/2-P, BFU2016-74932-C2-1-P/2-P, BFU2016-74932-C2-1-PJunta de Extremadura-FEDER (Fondo Europeo de Desarrollo Regional Grants) IB16046, GR18061Junta de Extremadura-FEDER European Union (EU) IB16046Ministerio Economía y Competitividad, España IJCI-2015-25665MINECO Grant BFU2016-74932-C2-1-

Store-Operated Calcium Entry in Breast Cancer Cells Is Insensitive to Orai1 and STIM1 N-Linked Glycosylation.

N-linked glycosylation is a post-translational modification that affects protein function, structure, and interaction with other proteins. The store-operated Ca2+ entry (SOCE) core proteins, Orai1 and STIM1, exhibit N-glycosylation consensus motifs. Abnormal SOCE has been associated to a number of disorders, including cancer, and alterations in Orai1 glycosylation have been related to cancer invasiveness and metastasis. Here we show that treatment of non-tumoral breast epithelial cells with tunicamycin attenuates SOCE. Meanwhile, tunicamycin was without effect on SOCE in luminal MCF7 and triple negative breast cancer (TNBC) MDA-MB-231 cells. Ca2+ imaging experiments revealed that expression of the glycosylation-deficient Orai1 mutant (Orai1N223A) did not alter SOCE in MCF10A, MCF7 and MDA-MB-231 cells. However, expression of the non-glycosylable STIM1 mutant (STIM1N131/171Q) significantly attenuated SOCE in MCF10A cells but was without effect in SOCE in MCF7 and MDA-MB-231 cells. In non-tumoral cells impairment of STIM1 N-linked glycosylation attenuated thapsigargin (TG)-induced caspase-3 activation while in breast cancer cells, which exhibit a smaller caspase-3 activity in response to TG, expression of the non-glycosylable STIM1 mutant (STIM1N131/171Q) was without effect on TG-evoked caspase-3 activation. Summarizing, STIM1 N-linked glycosylation is essential for full SOCE activation in non-tumoral breast epithelial cells; by contrast, SOCE in breast cancer MCF7 and MDA-MB-231 cells is insensitive to Orai1 and STIM1 N-linked glycosylation, and this event might participate in the development of apoptosis resistance

Metal-THINGS: The association and optical characterization of SNRs with HI holes in NGC 6946

NGC~6946, also known as the `Fireworks' galaxy, is an unusual galaxy that hosts a total of 225 supernova remnant (SNR) candidates, including 147 optically identified with high [SII]/Ha line ratios. In addition, this galaxy shows prominent HI holes, which were analyzed in previous studies. Indeed, the connection between SNRs and HI holes together with their physical implications in the surrounding gas is worth of attention. This paper explores the connection between the SNRs and the HI holes, including an analysis of their physical link to observational optical properties inside and around the rims of the holes, using new integral field unit (IFU) data from the Metal-THINGS survey. We present an analysis combining previously identified HI holes, SNRs candidates, and new integral field unit (IFU) data from Metal-THINGS of the spiral galaxy NGC 6946. We analyze the distributions of the oxygen abundance, star formation rate surface density, extinction, ionization, diffuse ionized gas, and the Baldwin-Phillips-Terlevich classification throughout the galaxy. By analyzing in detail the optical properties of the 121 previously identify HI holes in NGC 6946, we find that the SNRs are concentrated at the rims of the HI holes. Furthermore, our IFU data shows that the star formation rate and extinction are enhanced at the rims of the holes. To a lesser degree, the oxygen abundance and ionization parameter show hints of enhancement on the rims of the holes. Altogether, this provides evidence of induced star formation taking place at the rims of the holes, whose origin can be explained by the expansion of superbubbles created by multiple supernova explosions in large stellar clusters dozens of Myr ago.Comment: Accepted by A&

Nuclear astrophysics with radioactive ions at FAIR

R. Reifarth et al: ; 12 págs.; 9 figs.; Open Access funded by Creative Commons Atribution Licence 3.0 ; Nuclear Physics in Astrophysics VI (NPA6)The nucleosynthesis of elements beyond iron is dominated by neutron captures in the s and r processes. However, 32 stable, proton-rich isotopes cannot be formed during those processes, because they are shielded from the s-process ow and r-process -decay chains. These nuclei are attributed to the p and rp process. For all those processes, current research in nuclear astrophysics addresses the need for more precise reaction data involving radioactive isotopes. Depending on the particular reaction, direct or inverse kinematics, forward or time-reversed direction are investigated to determine or at least to constrain the desired reaction cross sections. The Facility for Antiproton and Ion Research (FAIR) will oer unique, unprecedented opportunities to investigate many of the important reactions. The high yield of radioactive isotopes, even far away from the valley of stability, allows the investigation of isotopes involved in processes as exotic as the r or rp processes.This project was supported by the HGF Young Investigators Project VH-NG-327, EMMI, H4F, HGS-HIRe, JINA, NAVI, DFG and ATHENA.Peer Reviewe

EFHB is a Novel Cytosolic Ca2+ Sensor That Modulates STIM1-SARAF Interaction

Background/Aims: STIM1 and Orai1 are the key components of store-operated Ca2+ entry (SOCE). Among the proteins involved in the regulation of SOCE, SARAF prevents spontaneous activation of SOCE and modulates STIM1 function. Methods: Cytosolic Ca2+ mobilization was estimated in fura-2-loaded cells using an epifluorescence inverted microscope. STIM1 interaction with Orai1, EFHB (EF-hand domain family member B, also known as CFAP21) and SARAF was detected by immunoprecipitation followed by Western blotting using specific antibodies. The involvement of EFHB in the translocation of NFAT to the nucleus was detected by confocal microscopy. Results: Here, we report the identification of EFHB as a new SOCE regulator. EFHB interacts with STIM1 upon store depletion and dissociates through a Ca2+-dependent mechanism. RNAi-mediated silencing as well as overexpression studies revealed that EFHB plays a relevant role in the interaction of STIM1 and Orai1 upon store depletion, the activation of SOCE and NFAT translocation from the cytosol to the nucleus. Silencing EFHB expression abolished the dissociation of SARAF from STIM1, which indicates that EFHB might play an important role in the dynamic interaction between both proteins, which is relevant for the activation of Orai1 channels upon Ca2+ store depletion and their subsequent modulation via slow Ca2+-dependent inactivation. Conclusion: Our results indicate that EFHB is a new SOCE regulator that modulates STIM1-SARAF interaction