2 resultados para Interaction kissing-loop
Resumo:
Aims: On 13 June 1998, the TRACE satellite was fortuitously well placed to observe the effects of a flare-induced EIT wave in the corona, and its subsequent interaction with coronal magnetic loops. In this study, we use these TRACE observations to corroborate previous theoretical work, which determined the response of a coronal loop to a harmonic driver in the context of ideal magnetohydrodynamics, as well as estimate the magnetic field strength and the degree of longitudinal inhomogeneity. Methods: Loop edges are tracked, both spatially and temporally, using wavelet modulus maxima algorithms, with corresponding loop displacements from its quiescent state analysed by fitting scaled sinusoidal functions. The physical parameters of the coronal loop are subsequently determined using seismological techniques. Results: The studied coronal loop is found to oscillate with two distinct periods, 501 ± 5 s and 274 ± 7 s, which could be interpreted as belonging to the fundamental kink mode and first harmonic, or could reflect the stage of an overdriven loop. Additional scenarios for explaining the two periods are listed, each resulting in a different value of the magnetic field and the intrinsic and sub-resolution properties of the coronal loop. When assuming the periods belong to the fundamental kink mode and its first harmonic, we obtain a magnetic field strength inside the oscillating coronal loop of 2.0 ± 0.7 G. In contrast, interpreting the oscillations as a combination of the loop's natural kink frequency and a harmonic EIT wave provides a magnetic field strength of 5.8 ± 1.5 G. Using the ratio of the two periods, we find that the gravitational scale height in the loop is 73 ± 3 Mm. Conclusions: We show that the observation of two distinct periods in a coronal loop does not necessarily lead to a unique conclusion. Multiple plausible scenarios exist, suggesting that both the derived strength of the magnetic field and the sub-resolution properties of the coronal loop depend entirely on which interpretation is chosen. The interpretation of the observations in terms of a combination of the natural kink mode of the coronal loop, driven by a harmonic EIT wave seems to result in values of the magnetic field consistent with previous findings. Other interpretations, which are realistic, such as kink fundamental mode/first harmonic and the oscillations of two sub-resolution threads result in magnetic field strengths that are below the average values found before.
Resumo:
Plasma membrane calmodulin-dependent calcium ATPases (PMCAs) are enzymatic systems implicated in the extrusion of calcium from the cell. We and others have previously identified molecular interactions between the cytoplasmic COOH-terminal end of PMCA and PDZ domain-containing proteins. These interactions suggested a new role for PMCA as a modulator of signal transduction pathways. The existence of other intracellular regions in the PMCA molecule prompted us to investigate the possible participation of other domains in interactions with different partner proteins. A two-hybrid screen of a human fetal heart cDNA library, using the region 652-840 of human PMCA4b (located in the catalytic, second intracellular loop) as bait, revealed a novel interaction between PMCA4b and the tumor suppressor RASSF1, a Ras effector protein involved in H-Ras-mediated apoptosis. Immunofluorescence co-localization, immunoprecipitation, and glutathione S-transferase pull-down experiments performed in mammalian cells provided further confirmation of the physical interaction between the two proteins. The interaction domain has been narrowed down to region 74-123 of RASSF1C (144-193 in RASSF1A) and 652-748 of human PMCA4b. The functionality of this interaction was demonstrated by the inhibition of the epidermal growth factor-dependent activation of the Erk pathway when PMCA4b and RASSF1 were co-expressed. This inhibition was abolished by blocking PMCA/RASSSF1 association with an excess of a green fluorescent protein fusion protein containing the region 50-123 of RASSF1C. This work describes a novel protein-protein interaction involving a domain of PMCA other than the COOH terminus. It suggests a function for PMCA4b as an organizer of macromolecular protein complexes, where PMCA4b could recruit diverse proteins through interaction with different domains. Furthermore, the functional association with RASSF1 indicates a role for PMCA4b in the modulation of Ras-mediated signaling.