Your browser doesn't support javascript.
loading
Adaptable and Multifunctional Ion-Conducting Aquaporins.
Tyerman, Stephen D; McGaughey, Samantha A; Qiu, Jiaen; Yool, Andrea J; Byrt, Caitlin S.
Afiliação
  • Tyerman SD; Australian Research Council (ARC) Centre of Excellence in Plant Energy Biology, School of Agriculture, Food and Wine, University of Adelaide, Glen Osmond, South Australia 5064, Australia; email: steve.tyerman@adelaide.edu.au, Jiaen.Qiu@adelaide.edu.au.
  • McGaughey SA; ARC Centre of Excellence for Translational Photosynthesis, Division of Plant Sciences, Research School of Biology, Australian National University, Acton, Australian Capital Territory 0200, Australia; email: Samantha.McGaughey@anu.edu.au, Caitlin.Byrt@anu.edu.au.
  • Qiu J; Australian Research Council (ARC) Centre of Excellence in Plant Energy Biology, School of Agriculture, Food and Wine, University of Adelaide, Glen Osmond, South Australia 5064, Australia; email: steve.tyerman@adelaide.edu.au, Jiaen.Qiu@adelaide.edu.au.
  • Yool AJ; Adelaide Medical School, University of Adelaide, Adelaide, South Australia 5005, Australia; email: andrea.yool@adelaide.edu.au.
  • Byrt CS; ARC Centre of Excellence for Translational Photosynthesis, Division of Plant Sciences, Research School of Biology, Australian National University, Acton, Australian Capital Territory 0200, Australia; email: Samantha.McGaughey@anu.edu.au, Caitlin.Byrt@anu.edu.au.
Annu Rev Plant Biol ; 72: 703-736, 2021 06 17.
Article em En | MEDLINE | ID: mdl-33577345
ABSTRACT
Aquaporins function as water and neutral solute channels, signaling hubs, disease virulence factors, and metabolon components. We consider plant aquaporins that transport ions compared to some animal counterparts. These are candidates for important, as yet unidentified, cation and anion channels in plasma, tonoplast, and symbiotic membranes. For those individual isoforms that transport ions, water, and gases, the permeability spans 12 orders of magnitude. This requires tight regulation of selectivity via protein interactions and posttranslational modifications. A phosphorylation-dependent switch between ion and water permeation in AtPIP2;1 might be explained by coupling between the gates of the four monomer water channels and the central pore of the tetramer. We consider the potential for coupling between ion and water fluxes that could form the basis of an electroosmotic transducer. A grand challenge in understanding the roles of ion transporting aquaporins is their multifunctional modes that are dependent on location, stress, time, and development.
Assuntos
Palavras-chave

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Aquaporinas / Aquagliceroporinas Idioma: En Ano de publicação: 2021 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Aquaporinas / Aquagliceroporinas Idioma: En Ano de publicação: 2021 Tipo de documento: Article