Aquaporins: More Than Functional Monomers in a Tetrameric Arrangement.

ABSTRACT: Aquaporins (AQPs) function as tetrameric structures in which each monomer has its own permeable pathway. The combination of structural biology, molecular dynamics simulations, and experimental approaches has contributed to improve our knowledge of how protein conformational changes can challenge its transport capacity, rapidly altering the membrane permeability. This review is focused on evidence that highlights the functional relationship between the monomers and the tetramer. In this sense, we address AQP permeation capacity as well as regulatory mechanisms that affect the monomer, the tetramer, or tetramers combined in complex structures. We therefore explore: (i) water permeation and recent evidence on ion permeation, including the permeation pathway controversy-each monomer versus the

SUBMITTER: Ozu M 

PROVIDER: S-EPMC6262540 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature