Palmer, AJ, Baker, A orcid.org/0000-0003-2181-4057 and Muench, SP orcid.org/0000-0001-6869-4414 (2016) The varied functions of aluminium-activated malate transporters–much more than aluminium resistance. Biochemical Society Transactions, 44 (3). pp. 856-862. ISSN 0300-5127
Abstract
The ALMT (aluminium-activated malate transporter) family comprises a functionally diverse but structurally similar group of ion channels. They are found ubiquitously in plant species, expressed throughout different tissues, and located in either the plasma membrane or tonoplast. The first family member identified was TaALMT1, discovered in wheat root tips, which was found to be involved in aluminium resistance by means of malate exudation into the soil. However, since this discovery other family members have been shown to have many other functions such as roles in stomatal opening, general anionic homoeostasis, and in economically valuable traits such as fruit flavour. Recent evidence has also shown that ALMT proteins can act as key molecular actors in GABA (γ-aminobutyric acid) signalling, the first evidence that GABA can act as a signal transducer in plants.
Metadata
Item Type: | Article |
---|---|
Authors/Creators: |
|
Copyright, Publisher and Additional Information: | © 2016 The Author(s). This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution Licence 4.0 (CC BY). |
Keywords: | aluminium-activated malate transporter (ALMT); aluminium resistance; gamma-aminobutyric acid (GABA); ion channel; malate; stomata |
Dates: |
|
Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Biomedical Sciences (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 18 Oct 2016 08:57 |
Last Modified: | 23 Jun 2023 22:10 |
Published Version: | https://doi.org/10.1042/BST20160027 |
Status: | Published |
Publisher: | Portland Press |
Identification Number: | 10.1042/BST20160027 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:102989 |