Journal ArticleDOI
Threonine at position 306 of the KAT1 potassium channel is essential for channel activity and is a target site for ABA-activated SnRK2/OST1/SnRK2.6 protein kinase
Aiko Sato,Yuki Sato,Yoichiro Fukao,Masayuki Fujiwara,Taishi Umezawa,Kazuo Shinozaki,Takao Hibi,Mitsutaka Taniguchi,Hiroshi Miyake,Derek B. Goto,Nobuyuki Uozumi +10 more
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TLDR
It is demonstrated that the C-terminal region of KAT1 acts as a phosphorylation target for the Arabidopsis calcium-independent ABA (abscisic acid)-activated protein kinase SnRK2.6 (Snf1-relatedprotein kinase 2.6).Abstract:
The Arabidopsis thaliana K+ channel KAT1 has been suggested to have a key role in mediating the aperture of stomata pores on the surface of plant leaves. Although the activity of KAT1 is thought to be regulated by phosphorylation, the endogenous pathway and the primary target site for this modification remained unknown. In the present study, we have demonstrated that the C-terminal region of KAT1 acts as a phosphorylation target for the Arabidopsis calcium-independent ABA (abscisic acid)-activated protein kinase SnRK2.6 (Snf1-related protein kinase 2.6). This was confirmed by LC-MS/MS (liquid chromatography tandem MS) analysis, which showed that Thr306 and Thr308 of KAT1 were modified by phosphorylation. The role of these specific residues was examined by single point mutations and measurement of KAT1 channel activities in Xenopus oocyte and yeast systems. Modification of Thr308 had minimal effect on KAT1 activity. On the other hand, modification of Thr306 reduced the K+ transport uptake activity of KAT1 in both systems, indicating that Thr306 is responsible for the functional regulation of KAT1. These results suggest that negative regulation of KAT1 activity, required for stomatal closure, probably occurs by phosphorylation of KAT1 Thr306 by the stress-activated endogenous SnRK2.6 protein kinase.read more
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Response of plants to water stress
TL;DR: The systems that regulate plant adaptation to water stress through a sophisticated regulatory network are the subject of the current review and molecular mechanisms that plants use to increase stress tolerance, maintain appropriate hormone homeostasis and responses and prevent excess light damage are discussed.
Journal ArticleDOI
ABA perception and signalling.
TL;DR: This work has shown a unique hormone perception mechanism where binding of ABA to the ABA receptors RCARs/PYR1/PYLs leads to inactivation of type 2C protein phosphatases such as ABI1 and ABI2 which targets ABA-dependent gene expression and ion channels.
Journal ArticleDOI
Abscisic Acid synthesis and response.
TL;DR: This chapter reviews the current understanding of ABA synthesis, metabolism, transport, and signal transduction, emphasizing knowledge gained from studies of Arabidopsis.
Journal ArticleDOI
Abscisic Acid and Abiotic Stress Tolerance in Crop Plants
TL;DR: The role of ABA in response to abiotic stress at the molecular level and ABA signaling is discussed and the effect of A BA in respect to gene expression is dealt with.
Journal ArticleDOI
Molecular basis of the core regulatory network in ABA responses: sensing, signaling and transport.
Taishi Umezawa,Kazuo Nakashima,Takuya Miyakawa,Takashi Kuromori,Masaru Tanokura,Kazuo Shinozaki,Kazuko Yamaguchi-Shinozaki +6 more
TL;DR: Understanding of the molecular basis of ABA responses in plants improved dramatically in 2009 and 2010, banner years for ABA research, and two plasma membrane-type ABC transporters were identified and shed light on the influx/efflux system of A BA, resolving how ABA is transported from cell to cell in plants.
References
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Journal ArticleDOI
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products.
Journal Article
Cleavage of structural proteins during the assemble of the head of bacterio-phage T4
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products as mentioned in this paper.
Journal ArticleDOI
Crystal Structure of a Mammalian Voltage-Dependent Shaker Family K + Channel
TL;DR: In this paper, the authors reported the crystal structure of a mammalian voltage-dependent potassium ion (K+) channel, Kv1.2, which is a member of the Shaker K+ channel family.
Journal ArticleDOI
The open pore conformation of potassium channels.
TL;DR: Amino-acid sequence conservation suggests a common structural basis for gating in a wide range of K+ channels, both ligand- and voltage-gated.
Journal ArticleDOI
Guard cell signal transduction
TL;DR: Stomatal guard cells have become a highly developed model system for characterizing early signal transduction mechanisms in plants and for elucidating how individual signaling mechanisms can interact within a network in a single cell.
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