Literature DB >> 15110265

How do P-type ATPases transport ions?

Hans-Jürgen Apell1.   

Abstract

P-type ATPases are a large family of membrane proteins that perform active ion transport across biological membranes. In these proteins, the energy-providing ATP hydrolysis is coupled to ion transport of one or two ion species across the respective membrane. The pump function of the investigated pumps is described by a so-called Post-Albers cycle. Main features of the pumping process are (1) a Ping-Pong mechanism, i.e. both transported ion species are transferred successively and in opposite direction across the membrane, (2) the transport process for each ion species consists of a sequence of reaction steps, which are ion binding, ion occlusion, conformational transition of the protein, successive deocclusion of the ions and release to the other side of the membrane. (3) Recent experimental evidence shows that the ion-binding sites are placed in the transmembrane section of the proteins and that ion movements occur preferentially during the ion binding and release processes. The main features of the mechanism include narrow access channels from both sides, one gate per access channel, and an ion-binding moiety that is adapted specifically to the ions that are transported, and differently in both principal conformations.

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Year:  2004        PMID: 15110265     DOI: 10.1016/j.bioelechem.2003.09.021

Source DB:  PubMed          Journal:  Bioelectrochemistry        ISSN: 1567-5394            Impact factor:   5.373


  21 in total

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Authors:  Miguel Holmgren; Robert F Rakowski
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Journal:  World J Microbiol Biotechnol       Date:  2017-01-24       Impact factor: 3.312

Review 4.  P2C-Type ATPases and Their Regulation.

Authors:  Rocío Retamales-Ortega; Carlos P Vio; Nibaldo C Inestrosa
Journal:  Mol Neurobiol       Date:  2015-01-29       Impact factor: 5.590

5.  Active transport of the Ca(2+)-pump: introduction of the temperature difference as a driving force.

Authors:  Anders Lervik; Dick Bedeaux; Signe Kjelstrup
Journal:  Eur Biophys J       Date:  2013-01-09       Impact factor: 1.733

6.  Palytoxin-induced effects on partial reactions of the Na,K-ATPase.

Authors:  Nadine Harmel; Hans-Jürgen Apell
Journal:  J Gen Physiol       Date:  2006-07       Impact factor: 4.086

7.  Altered intracellular localization and valosin-containing protein (p97 VCP) interaction underlie ATP7A-related distal motor neuropathy.

Authors:  Ling Yi; Anthony Donsante; Marina L Kennerson; Julian F B Mercer; James Y Garbern; Stephen G Kaler
Journal:  Hum Mol Genet       Date:  2011-12-30       Impact factor: 6.150

8.  Kinetics of Ca2+ binding to the SR Ca-ATPase in the E1 state.

Authors:  Christine Peinelt; Hans-Jürgen Apell
Journal:  Biophys J       Date:  2005-07-22       Impact factor: 4.033

9.  Stimulation, inhibition, or stabilization of Na,K-ATPase caused by specific lipid interactions at distinct sites.

Authors:  Michael Habeck; Haim Haviv; Adriana Katz; Einat Kapri-Pardes; Sophie Ayciriex; Andrej Shevchenko; Haruo Ogawa; Chikashi Toyoshima; Steven J D Karlish
Journal:  J Biol Chem       Date:  2014-12-22       Impact factor: 5.157

10.  Divalent cation interactions with Na,K-ATPase cytoplasmic cation sites: implications for the para-nitrophenyl phosphatase reaction mechanism.

Authors:  Craig Gatto; Krista L Arnett; Mark A Milanick
Journal:  J Membr Biol       Date:  2007-06-17       Impact factor: 1.843

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