Bukovics Péter, Lőrinczy Dénes
Department of Biophysics, Medical School, University of Pécs, Szigeti Str. 12, H-7624 Pécs, Hungary.
Int J Mol Sci. 2025 Apr 3;26(7):3336. doi: 10.3390/ijms26073336.
Actin, a key component of the cytoskeleton, undergoes significant structural and thermal changes in response to various regulatory factors, including the neuropeptide pituitary adenylate cyclase-activating polypeptide (PACAP). In this study, we applied deconvolution analysis to previously obtained differential scanning calorimetry (DSC) data to resolve overlapping thermal transitions in G- and F-actin unfolding. Our findings reveal that PACAP38 and PACAP6-38 significantly alter actin stability, increasing structural cooperativity in G-actin while reducing monomer-monomer interactions in F-actin. These thermodynamic changes suggest a potential role for PACAP in modulating actin polymerization and depolymerization dynamics, contributing to cytoskeletal remodeling.
肌动蛋白是细胞骨架的关键组成部分，会响应包括神经肽垂体腺苷酸环化酶激活多肽（PACAP）在内的各种调节因子而发生显著的结构和热变化。在本研究中，我们对先前获得的差示扫描量热法（DSC）数据应用去卷积分析，以解析G-肌动蛋白和F-肌动蛋白解折叠过程中重叠的热转变。我们的研究结果表明，PACAP38和PACAP6-38显著改变肌动蛋白稳定性，增加G-肌动蛋白的结构协同性，同时减少F-肌动蛋白中单体与单体之间的相互作用。这些热力学变化表明PACAP在调节肌动蛋白聚合和解聚动力学方面具有潜在作用，有助于细胞骨架重塑。
