Literature DB >> 22542572

On the definition, nomenclature and classification of water channel proteins (aquaporins and relatives).

Gheorghe Benga1.   

Abstract

A water channel protein (WCP) or a water channel can be defined as a transmembrane protein that has a specific three-dimensional structure with a pore that provides a pathway for water permeation across biological membranes. The pore is formed by two highly conserved regions in the amino acid sequence, called NPA boxes (or motifs) with three amino acid residues (asparagine-proline-alanine, NPA) and several surrounding amino acids. The NPA boxes have been called the "signature" sequence of WCPs. WCPs are a family of proteins belonging to the Membrane Intrinsic Proteins (MIPs) superfamily. In addition, in the MIP superfamily (with more than 1000 members) there are also proteins with no channel activity. The WCP family include three subfamilies: aquaporins, aquaglyceroporins and S-aquaporins. (1) The aquaporins (AQPs) are water selective or specific water channels, also named by various authors as "orthodox", "ordinary", "conventional", "classical", "pure", "normal", or "sensu strictu" aquaporins); (2) The aquaglyceroporins are permeable to water, but also to other small uncharged molecules, in particular glycerol; this family includes the glycerol facilitators, abbreviated as GlpFs, from glycerol permease facilitators. The "signature" sequence for aquaglyceroporins is the aspartic acid residue (D) in the second NPA box. (3) The third subfamily of WCPs have little conserved amino acid sequences around the NPA boxes, unclassifiable to the first two subfamilies. I recommend to use always for this subfamily the name S-aquaporins. They are also named "superaquaporins", "aquaporins with unusual (or deviated) NPA boxes", "subcellular aquaporins", or "sip-like aquaporins". I also recommend to use always the spelling aquaporin (not aquaporine), and, for various AQPs, the abbreviation AQP followed immediately by the number, (e.g. AQP1), with no space or--which might create confusions with "minus".
Copyright © 2012 Elsevier Ltd. All rights reserved.

Entities:  

Mesh:

Substances:

Year:  2012        PMID: 22542572     DOI: 10.1016/j.mam.2012.04.003

Source DB:  PubMed          Journal:  Mol Aspects Med        ISSN: 0098-2997


  32 in total

1.  Bioinformatics analysis and construction of phylogenetic tree of aquaporins from Echinococcus granulosus.

Authors:  Fen Wang; Bin Ye
Journal:  Parasitol Res       Date:  2016-05-11       Impact factor: 2.289

2.  Erythritol predicted to inhibit permeation of water and solutes through the conducting pore of P. falciparum aquaporin.

Authors:  Liao Y Chen
Journal:  Biophys Chem       Date:  2015-01-14       Impact factor: 2.352

3.  1,3-propanediol binds deep inside the channel to inhibit water permeation through aquaporins.

Authors:  Lili Yu; Roberto A Rodriguez; L Laurie Chen; Liao Y Chen; George Perry; Stanton F McHardy; Chih-Ko Yeh
Journal:  Protein Sci       Date:  2016-02       Impact factor: 6.725

4.  Application of the Brown dynamics fluctuation-dissipation theorem to the study of Plasmodium berghei transporter protein PbAQP.

Authors:  Liao Y Chen
Journal:  Front Phys       Date:  2020-04-17

5.  Morphology and water permeability of red blood cells from green sea turtle (Chelonia mydas).

Authors:  Gheorghe Benga; Bogdan E Chapman; Tony Romeo; Guy C Cox; Philip W Kuchel
Journal:  Protoplasma       Date:  2014-12-23       Impact factor: 3.356

6.  Computing osmotic permeabilities of aquaporins AQP4, AQP5, and GlpF from near-equilibrium simulations.

Authors:  Thierry O Wambo; Roberto A Rodriguez; Liao Y Chen
Journal:  Biochim Biophys Acta Biomembr       Date:  2017-04-25       Impact factor: 3.747

Review 7.  Comparative studies of water permeability of red blood cells from humans and over 30 animal species: an overview of 20 years of collaboration with Philip Kuchel.

Authors:  Gheorghe Benga
Journal:  Eur Biophys J       Date:  2012-10-27       Impact factor: 1.733

8.  [Role of aquaporin-5 in regulating colorectal cancer cell growth in vitro].

Authors:  Shuo Chen; Tao Shan; Li Wang; Xi Chen; Xi-Juan Cui; Xian-Ni Gao
Journal:  Nan Fang Yi Ke Da Xue Xue Bao       Date:  2017-10-20

Review 9.  Aquaporin-5: from structure to function and dysfunction in cancer.

Authors:  Inês Direito; Ana Madeira; Maria Alexandra Brito; Graça Soveral
Journal:  Cell Mol Life Sci       Date:  2016-02-02       Impact factor: 9.261

10.  1,3-Propanediol binds inside the water-conducting pore of aquaporin 4: Does this efficacious inhibitor have sufficient potency?

Authors:  Lili Yu; Oscar D Villarreal; L Laurie Chen; Liao Y Chen
Journal:  J Syst Integr Neurosci       Date:  2016-01-23
View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.