Post-translational modification acts as a digital like switch influencing AtPIP2;1 water and cation permeability.

Plant aquaporins (AQPs) were initially described as a family of membrane-localized proteins exclusively facilitating water transport. Subsequently, sub-sets of plant AQPs have exhibited diverse functionalities beyond water transport. The aquaporin AtPIP2;1, an abundant Plasma membrane Intrinsic Protein in Arabidopsis thaliana, can transport water but also CO, HO and monovalent cations under certain conditions.

A high-throughput yeast approach to characterize aquaporin permeabilities: Profiling the Arabidopsis PIP aquaporin sub-family.

Introduction: Engineering membrane transporters to achieve desired functionality is reliant on availability of experimental data informing structure-function relationships and intelligent design. Plant aquaporin (AQP) isoforms are capable of transporting diverse substrates such as signaling molecules, nutrients, metalloids, and gases, as well as water. AQPs can act as multifunctional channels and their transport function is reliant on many factors, with few studies having assessed transport function of specific isoforms for multiple substrates.

An algal PIP-like aquaporin facilitates water transport and ionic conductance.

Aquaporins are water and solute channel proteins found throughout the kingdoms of life. Ion-conducting aquaporins (icAQPs) have been identified in both plants and animals indicating that this function may be conserved through evolution. In higher plants icAQP function has been demonstrated for isoforms from two of five aquaporin subfamilies indicating that this function could have existed before the divergence of higher plants from green algae.

Phosphorylation influences water and ion channel function of AtPIP2;1.

The phosphorylation state of two serine residues within the C-terminal domain of AtPIP2;1 (S280, S283) regulates its plasma membrane localization in response to salt and osmotic stress. Here, we investigated whether the phosphorylation state of S280 and S283 also influence AtPIP2;1 facilitated water and cation transport. A series of single and double S280 and S283 phosphomimic and phosphonull AtPIP2;1 mutants were tested in heterologous systems.

Deciphering aquaporin regulation and roles in seed biology.

Seeds are the typical dispersal and propagation units of angiosperms and gymnosperms. Water movement into and out of seeds plays a crucial role from the point of fertilization through to imbibition and seed germination. A class of membrane intrinsic proteins called aquaporins (AQPs) assist with the movement of water and other solutes within seeds.

Roles of Aquaporins in Stem Development and Sugar Storage.

is a C grass used as a model for bioenergy feedstocks. The elongating internodes in developing stems grow from an intercalary meristem at the base, and progress acropetally toward fully expanded cells that store sugar. During stem development and maturation, water flow is a driver of cell expansion and sugar delivery.