E for the recycling of contractile vacuole membrane may need during the osmoregulation in Dictyostelium on ben, A tribute to G��nther Gerisch. EUR J Cell Biol 85: masitinib 790299-79-5 859 871st Recovery of V-ATPase PLoS ONE | Published in PloSOne 14th January 2010 | Volume 5 | Issue 1 | e8585 protein phosphatase 2A interacts with the ATPase Na, K, and modulates its Bek attenuation by inhibiting its association with arrestin Toru Kimura1, 2 WonSun Han2, Philip Pagel2, Angus C. Nairn3, Michael J . Caplan2 1 Institute of Pharmacology and Toxicology, Kyorin University School of Medicine, Mitaka, Tokyo, Japan, 2 cellular compartments re and Molecular Physiology and Psychiatry 3, Yale University School of Medicine in New Haven, Connecticut, United States of America Background : The P-type ATPase family is a collection of ion pumps, the phosphorylated intermediates formed during the transport of ions.
One of the best known representatives of this family is the Na, K-ATPase. The catalytic subunit of Na, K-ATPase consists of several functional Brivanib VEGFR inhibitor NEN Dom, Which has the enzymatic properties and determine trade. Results Methodology / Principal: the yeast two-hybrid system, we found that the C-protein phosphatase 2A catalytic subunit, a specific Na, K-ATPase interacting protein. PP2A C subunit interacts with the ATPase Na, K, but not with the homologous sequences of H-, K-ATPase. We best term That the Na, K-ATPase interacts with a complex of subunits A and C in the native kidneys of rats. Arrestins and G-protein coupled receptor kinases are important regulators of G protein-coupled receptor signaling, and they also regulate Na, K-ATPase trafficking through direct association.
PP2A inhibits the ATPase association between Na, K, and arrestin, and arrestin reduces the effect of Na, K-ATPase trafficking. GRK phosphorylates the Na, K-ATPase and PP2A can at least partially Feedb Ngig this phosphorylation. Conclusions / significance: Taken together, these data indicate that the sodium pump to a growing list of ion transport proteins that are regulated by direct interaction with the catalytic subunit of protein phosphatase go rt. Quote: Kimura T, Han W, Pagel P, Nairn AC, interacts MJ Caplan protein phosphatase 2A with the ATPase Na, K, and modulates its trafficking by inhibiting its association with arrestin. PLoS ONE 6: e29269. doi: 10.1371/journal.pone.
0029269 Editor: David Holowka, Cornell University, the United States of America 22nd Re u July 2011, Accepted 23rd November 2011, VER Published 29th December 2011 Copyright: 2011 Kimura and al. This is an Open Access article distributed under the terms of the Creative Commons Attribution License, which uneingeschr Distribution of spaces permitted use, distribution, and reproduction in any medium, provided the original author and source are credited. Funding: This work was supported by National Institutes of Health DK17433 and DK072612 and MH40899 and MH074866 supported. F Sponsors played no R In the study design, data collection and analysis, decision to Ver Publication or preparation of this manuscript. Conflicts of interest: The authors have explained rt that no competing interests exist. : Ion Transport Pr sentation michael.
caplanyale pumps generate ion gradients across membranes, and these gradients are re cellular homeostasis of essential Hom. The P-type ATPase family includes Na, K-ATPase, Ca2 ATPase, H, K-ATPase, heavy metal transport ATPases and plasma membrane H ATPase of yeast. Have the catalytic subunits of these ATPases Similar structures and functions. But their intracellular Re distributions. transported ions, and their regulation are very different. Obviously, there must be specific function to areas in each ATPase, which may be defined to identify their individual characteristics. Moreover, each ATPase is able, with certain proteins to determine their individual traffic and regulatory properties. Na, K-ATPase, or sodium pump is ubiquitous, expressed R in virtually all tissues and plays a The key to maintaining intracellular Ren electrolyte homeostasis Hom. The Na, K AT