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Makke, M.

Publications and source records attributed to Makke, M..

3 recordsLinked to original sources

ATP1A3 E815K Disrupts Sodium Homeostasis and Excitability in Human Alternating Hemiplegia of Childhood Neurons

Alternating hemiplegia of childhood (AHC) is a rare neurodevelopmental disorder primarily caused by heterozygous de novo mutations in the ATP1A3 gene, which encodes the neuron-specific catalytic 3 subunit of the P-type Na/K-ATPase. Among these, the E815K variant is the second most frequent ATP1A3 mutation in AHC and is associated with the most severe clinical phenotypes, characterized by frequent epileptic and dystonic episodes and profound developmental impairment, making it a key target for mechanistic study. Although E815K was shown to disrupt pump function in heterologous systems and animal models, its impact on human neurons remain poorly understood. To investigate its disease-relevant pathophysiology, we generated induced pluripotent stem cells (iPSCs) from an AHC patient carrying the E815K mutation and differentiated them into mature neurons. Patient-derived neurons displayed normal differentiation and synaptogenesis, with preserved evoked synaptic transmission. However, 3-specific Na/K pump currents were nearly abolished, whereas 1 activity remained intact. This selective dysfunction was associated with a depolarized resting membrane potential, reduced input resistance, and diminished intrinsic excitability. Patient neurons generated fewer action potentials in response to depolarizing current steps, displayed altered firing patterns, and showed significantly decreased voltage-gated sodium current densities, while potassium conductance remained unaffected. Taken together, these results indicate that the ATP1A3 E815K mutation disrupts intracellular sodium homeostasis and consequently modifies the excitability of human neurons. Overall, these findings provide mechanistic insight into the molecular pathophysiology underlying this AHC variant and thereby establish a patient-derived neuronal model which serves as a platform for future drug screening approaches and therapeutic investigation.

neuroscience↗

Ideal efficacy photoswitches for TRPC4/5 channels harness high potency for spatiotemporally-resolved control of TRPC function in live tissues

Directly probing the endogenous biological roles of target proteins with high spatial and temporal resolution, as non-invasively and reproducibly as possible, is a shared conceptual goal for research across many fields, as well as for targeted therapies. Here we describe the rational conceptual design and test-case practical implementation of a photopharmacological paradigm to empower high-performance photomodulation studies in vivo. TRPC4/5 ion channels are involved in many spatiotemporally resolved circuits, from pain and anxiety, to reproductive signaling, digestion, and obesity. To unpick their biology requires spatiotemporally precise tools, which were lacking. We developed "ideal efficacy photoswitch" ligands to control their diverse functions in situ. These E{leftrightarrows}Z-photoswitchable ligands bias TRPC[4]/5 channel activity with exquisite photocontrol, from strong agonism under 360 nm, to low agonism at 385 nm, to strong antagonism at 410-460 nm. Cryo-EM structures of both TRPC4 and TRPC5 with both Z-agonists and E-antagonists support the rationale for efficacy switching through competitive E/Z isomer binding. Crucially, since the E/Z ratio is exclusively determined by the light wavelength applied, their channel photocontrol is exclusively wavelength-dependent, yet drug-concentration-independent: so is reproducible from cell culture to >millimetre-depth tissues. Indeed, we were able to photocontrol both direct and downstream TRPC4/5 biology in cell lines or primary cells in culture, from calcium flux, to primary neuron excitability and adrenaline release; and even in tissues, photoswitching small intestine motility and peristalsis. The TRPC4/5 ligands we develop will thus unlock a range of high-precision investigations in TRP biology. More broadly, we propose that the success of this efficacy photoswitch program, from concept to tissue level translation, is mainly a consequence of how biology has evolved proteins for efficacy control. We therefore foresee that a variety of functionally responsive protein targets, not only sensory and signaling ion channels and receptors, will be amenable to similarly high-performance photocontrol even in vivo, if a new generation of reagent development adopts this paradigm of ideal efficacy photoswitching. Table of Contents Graphic O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=84 SRC="FIGDIR/small/602451v1_ufig1.gif" ALT="Figure 1"> View larger version (24K): org.highwire.dtl.DTLVardef@1f8e527org.highwire.dtl.DTLVardef@18c72d0org.highwire.dtl.DTLVardef@1c5d648org.highwire.dtl.DTLVardef@177203d_HPS_FORMAT_FIGEXP M_FIG C_FIG

cell biology↗

Key determinants of the dual clamp/activator function of Complexin

Complexin determines magnitude and kinetics of synchronized secretion, but the underlying molecular mechanisms remained unclear. Here, we show that the hydrophobic face of the amphipathic helix at the C-terminus of Complexin II (CpxII, amino acids 115- 134) binds to fusion-promoting SNARE proteins, prevents premature secretion and allows vesicles to accumulate in a release-ready state. Specifically, we demonstrate that an unrelated amphipathic helix functionally substitutes for the CTD of CpxII and that amino acid substitutions on the hydrophobic side compromise the arrest of the prefusion intermediate. To facilitate synchronous vesicle fusion, the N-terminal domain (NTD) of CpxII (amino acids 1-27) specifically cooperates with synaptotagmin I (SytI), but not with synaptotagmin VII. Expression of CpxII rescues the slow release kinetics of the Ca2+- binding mutant Syt I R233Q, whereas the N-terminally truncated variant of CpxII further delays it. These results indicate that the CpxII NTD regulates mechanisms which are governed by the forward rate of Ca2+ binding to Syt I. Overall, our results shed new light on key molecular properties of CpxII that hinder premature exocytosis and accelerate synchronous exocytosis.

neuroscience↗