JGP study identifies a novel peptide in scorpion venom that inhibits KV1.2 and KV1.3 channels and could form the basis for new treatments for autoimmune diseases.
Cm28, a scorpion toxin having a unique primary structure, inhibits KV1.2 and KV1.3 with high affinity
Naseem et al. show that the Cm28 peptide found in scorpion venom is a potent inhibitor of the KV1.2 and KV1.3 K+ channels. Cm28 is a pore blocker that obeys a unique primary structure with only 27 amino acid residues and the lack of the functional dyad characteristic of other α-KTx peptides.
The authors develop a stochastic model for calcium influx in dendritic spines in idealized and realistic geometries. Using this model, they show that spine morphology alters calcium transients and synaptic weight updates.
De Jesús-Pérez et al. show that a reciprocal regulation between key gating elements and permeant anions sets the calcium and voltage sensitivities and the anion selectivity of the calcium-activated chloride channel TMEM16A.
Del Rosario and Gabrielle et al. show that TMEM120A/TACAN inhibits mechanically activated PIEZO2 channels both in heterologous systems and in dorsal root ganglion neurons. TMEM120A does not inhibit PIEZO1 and TREK1 channel activity and its expression alone does not lead to appearance of mechanically activated currents.