37 research outputs found
The osmoresponsiveness of oxytocin and vasopressin neurones: mechanisms, allostasis and evolution
The Value in Science-Art Partnerships for Science Education and Science Communication
AbstractJust a fraction of the scientific knowledge produced in laboratories reaches a lay audience. Most of our communication with the public gets lost in translation because of the difficulties that science communication poses to scientists. Among other obstacles, differential exposure to scientific and critical thinking, discrepancies with social narratives, and communication training based in the deficit model add on top of a practice established on avoiding emotionality. In this context, effective communication requires the use of emotions, which are crucial to establishing trust. This commentary provides a rationale for collaboration with graphic design and fine arts to use emotions in science communication and education. It starts by proposing the two-way engagement model as a replacement for the deficit model. Next, it offers a neuroscientific basis for the use of emotions in establishing trust. Finally, it finishes profiling the Convergence Initiative’s efforts to establish bridges across disciplines and communicating science with the public through art.</jats:p
Clock-driven vasopressin neurotransmission mediates anticipatory thirst prior to sleep
Structure–functional intimacies of transient receptor potential channels
AbstractAlthough a unifying characteristic common to all transient receptor potential (TRP) channel functions remains elusive, they could be described as tetramers formed by subunits with six transmembrane domains and containing cation-selective pores, which in several cases show high calcium permeability. TRP channels constitute a large superfamily of ion channels, and can be grouped into seven subfamilies based on their amino acid sequence homology: the canonical or classic TRPs, the vanilloid receptor TRPs, the melastatin or long TRPs, ankyrin (whose only member is the transmembrane protein 1 [TRPA1]), TRPN after the nonmechanoreceptor potential C (nonpC), and the more distant cousins, the polycystins and mucolipins. Because of their role as cellular sensors, polymodal activation and gating properties, many TRP channels are activated by a variety of different stimuli and function as signal integrators. Thus, how TRP channels function and how function relates to given structural determinants contained in the channel-forming protein has attracted the attention of biophysicists as well as molecular and cell biologists. The main purpose of this review is to summarize our present knowledge on the structure of channels of the TRP ion channel family. In the absence of crystal structure information for a complete TRP channel, we will describe important protein domains present in TRP channels, structure–function mutagenesis studies, the few crystal structures available for some TRP channel modules, and the recent determination of some TRP channel structures using electron microscopy.</jats:p
Allosteric interactions and the modular nature of the voltage- and Ca2+-activated (BK) channel
The high conductance voltage- and Ca2+-activated K+ channel is one of the most broadly expressed channels in mammals. This channel is named BK for ‘big K’ because of its single-channel conductance that can be as large as 250 pS in 100 mm symmetrical K+. BK channels increase their activity by membrane depolarization or an increase in cytosolic Ca2+. One of the key features that defines the behaviour of BK channels is that neither Ca2+ nor voltage is strictly necessary for channel activation. This and several other observations led to the idea that both Ca2+ and voltage increase the open probability by an allosteric mechanism. In this type of mechanism, the processes of voltage sensor displacement, Ca2+ binding and pore opening are independent equilibria that interact allosterically with each other. These allosteric interactions in BK channels reside in the structural characteristics of the BK channel in the sense that voltage and Ca2+ sensors and the pore need to be contained in different structures or ‘modules’. Through electrophysiological, mutagenesis, biochemical and fluorescence studies these modules have been identified and, more important, some of the interactions between them have been unveiled. In this review, we have covered the main advances achieved during the last few years in the elucidation of the structure of the BK channel and how this is related with its function as an allosteric protein
In Vivo Measurements Of a Ca2+- And Voltage-Activated K+ Channel Intramolecular Distances Using Genetically Encoded Reporters
In Vivo Measurements Of a Ca2+- And Voltage-Activated K+ Channel Intramolecular Distances Using Genetically Encoded Reporters
Modulation of spike clustering by NMDA receptors and neurotensin in rat supraoptic nucleus neurons
Photograph of a scene at the Dinosaur Tracks area, along the Santa Fe Trail
