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Squishing Cellular H2O
Author(s) -
Bartolomei Barrett,
Bogdon Phoebe,
Frazer Mandy,
Johnson Robert,
Lopez Dayana,
Mergens Steven,
Nichols Andrew,
Owens Jonathan,
Rall Tanner,
Rhodes Abigail,
Shipley Ashley Willow,
Simmons Emily,
Wright Zachary,
GaleaMartinez Sandra Ann,
Bresniker Catherine
Publication year - 2019
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2019.33.1_supplement.lb349
Subject(s) - aquaporin , biophysics , phosphorylation , transmembrane protein , conductance , chemistry , water channel , microbiology and biotechnology , membrane , cytoplasm , transmembrane domain , biochemistry , biology , physics , receptor , mechanical engineering , engineering , inlet , condensed matter physics
Water is an essential part of the function of all living organisms. If water does not function normally, neurodegenerative and autoimmune diseases can become everyday occurrences affecting the health of humans. A research study was conducted about the structure and relative significance of the water channel, aquaporin 4 (AQP4), and it's possible conformational changes. Though structural details concerning the molecular mechanism of human AQP4 regulation are still unknown, this study has assisted in gaining insight into its structure and its interactions. The protein AQP4 consists of six‐transmembrane domains and five connecting loops that form a channel, and similar to other aquaporin channels, the monomers of AQP4 assemble into tetramers. AQP4 is namely arranged in clusters, known as orthogonal array particles, which allow for better anchoring to the membrane. Similar to other aquaporins, the pathway through the channel is amphipathic; this disposition allows for the bidirectional conductance of water. The physiological aspect (which is a 4‐fold axis structure) insulates against all solutes and water; the cytoplasmic side of the channel stabilizes the backbone amides. The mid‐membrane section, containing Phe‐195, Leu‐191, and Leu‐75, create a hydrophobic block (when repeated 4‐times). The research also revealed that AQP4 is subject to posttranslational regulation by phosphorylation. Water conductance is affected in AQP4 when SER‐111 (associated with the B loop) and Ser‐180 (associated with the D loop) are in a state of phosphorylation. Phosphorylated Ser‐180 is believed to possibly block the water channel by creating a tether to the C‐terminal domain. When Ser‐111 goes through phosphorylation, it mimics the gating mechanism in plants. This study of AQP4 suggests that the brain, spinal cord, and circadian rhythm are affected by its expression, as AQP4 is concentrated in the ends of astrocytes, of the brain. As new research comes to fruition, it is clear that these conformational changes will have broad implications with a variety of cell communication through that of water transport. The science community is on the frontier of research which could lead to therapeutic strategies and treatment of not only neurodegenerative diseases but autoimmune diseases as well. The El Capitan High School MSOE Center for BioMolecular Modeling MAPS Team used 3D modeling and printing technology to examine structure‐function relationships of Aquaporin 4. This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .