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Loop B serine of a plasma membrane aquaporin type PIP2 but not PIP1 plays a key role in pH sensing.
Biochim Biophys Acta
November 2016
Departamento de Biodiversidad y Biología Experimental, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Instituto de Biodiversidad y Biología Experimental (IBBEA, UBA-CONICET), Buenos Aires, Argentina; Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Buenos Aires, Argentina. Electronic address:
In the plant kingdom, the plasma membrane intrinsic aquaporins (PIPs) constitute a highly conserved group of water channels with the capacity of rapidly adjusting the water permeability (P) of a cell by a gating response. Most evidence regarding this mechanism was obtained by different biophysical approaches including the crystallization of a Spinaca olaracea PIP2 aquaporin (SoPIP2;1) in an open and close conformation. A close state seems to prevail under certain stimuli such as cytosolic pH decrease, intracellular Ca concentration increase and dephosphorylation of specific serines.
View Article and Find Full Text PDFConvergent evolution in the assembly of polyubiquitin degradation signals by the Shigella flexneri IpaH9.8 ligase.
J Biol Chem
December 2014
From the Department of Biochemistry and Molecular Biology and the Stanley S. Scott Cancer Center, Louisiana State University Health Science Center, New Orleans, Louisiana 70112
The human pathogen Shigella flexneri subverts host function and defenses by deploying a cohort of effector proteins via a type III secretion system. The IpaH family of 10 such effectors mimics ubiquitin ligases but bears no sequence or structural homology to their eukaryotic counterpoints. Using rates of (125)I-polyubiquitin chain formation as a functional read out, IpaH9.
View Article and Find Full Text PDFCounterpoint: Pulmonary edema does not occur in human athletes performing heavy sea-level exercise.
J Appl Physiol (1985)
October 2010
School of Human Kinetics, Faculty of Medicine, University of British Columbia, Vancouver, British Columbia, Canada.
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