Mayo Kevin H
Department of Biochemistry, Molecular Biology & Biophysics, University of Minnesota Health Sciences Center, 6-155 Jackson Hall, Minneapolis, MN 55455, USA.
Int J Mol Sci. 2023 Sep 14;24(18):14083. doi: 10.3390/ijms241814083.
Extra- and intra-cellular activity occurs under the direction of numerous inter-molecular interactions, and in any tissue or cell, molecules are densely packed, thus promoting those molecular interactions. Galectins and chemokines, the focus of this review, are small, protein effector molecules that mediate various cellular functions-in particular, cell adhesion and migration-as well as cell signaling/activation. In the past, researchers have reported that combinations of these (and other) effector molecules act separately, yet sometimes in concert, but nevertheless physically apart and via their individual cell receptors. This view that each effector molecule functions independently of the other limits our thinking about functional versatility and cooperation, and, in turn, ignores the prospect of physiologically important inter-molecular interactions, especially when both molecules are present or co-expressed in the same cellular environment. This review is focused on such protein-protein interactions with chemokines and galectins, the homo- and hetero-oligomeric structures that they can form, and the functional consequences of those paired interactions.
细胞外和细胞内的活动在众多分子间相互作用的指导下发生，在任何组织或细胞中，分子都紧密堆积，从而促进了这些分子间的相互作用。半乳糖凝集素和趋化因子是本综述的重点，它们是小的蛋白质效应分子，介导各种细胞功能，特别是细胞粘附和迁移，以及细胞信号传导/激活。过去，研究人员报道这些（以及其他）效应分子的组合有时单独起作用，但有时协同作用，不过它们在物理上是分开的，通过各自的细胞受体发挥作用。这种认为每个效应分子独立发挥功能的观点限制了我们对功能多样性和协同作用的思考，进而忽视了生理上重要的分子间相互作用的可能性，尤其是当两种分子同时存在或在同一细胞环境中共表达时。本综述聚焦于趋化因子和半乳糖凝集素之间的这种蛋白质-蛋白质相互作用、它们能够形成的同型和异型寡聚结构以及这些配对相互作用的功能后果。
