ABI1 (At4g26080; UniProt P49597) in *Arabidopsis thaliana* Falcon Edison Scientific Literature 44 citations 1 artifacts 2026-09-11T20:55:41.492544
Edison artifact artifact-00 (text/markdown)

The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.

You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.

We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.

We are interested in where in or outside the cell the gene product carries out its function.

We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.

Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.

ABI1 (At4g26080; UniProt P49597) in Arabidopsis thaliana

Executive summary

ABI1 is ABSCISIC ACID-INSENSITIVE 1, locus At4g26080, in Arabidopsis thaliana. The literature explicitly identifies At4g26080 as a clade-A type-2C protein phosphatase (PP2C), matching UniProt P49597 and the supplied PP2C/PPM-family domain annotation. This report is restricted to this plant protein; same-symbol proteins from other organisms are not included. (krzywinska2016phosphataseabi1and pages 2-4)

ABI1 is principally a metal-dependent Ser/Thr phosphoprotein phosphatase and negative regulator of abscisic-acid (ABA) signaling. Its best-established physiological substrates are SnRK2 protein kinases. In unstressed or low-ABA conditions, ABI1 binds SnRK2s, removes activating phosphates from their activation loops, and holds ABA outputs off. ABA-bound PYR/PYL/RCAR receptors inhibit ABI1, permitting SnRK2 activation and downstream control of transcription, ion transport, stomatal closure, germination, and growth. (umezawa2009type2cprotein pages 4-4, xie2012molecularmechanismfor pages 1-2)

Identity verification

Annotation dimension Best-supported conclusion Experimental evidence Representative source/date/DOI
Identity and family ABI1 is the Arabidopsis thaliana gene At4g26080 encoding a clade-A type 2C protein phosphatase, consistent with UniProt P49597 and its PP2C-family domains. This annotation does not refer to same-symbol proteins in other organisms. The locus-to-protein mapping and clade-A PP2C classification are stated explicitly in an Arabidopsis biochemical study. Krzywińska et al.; June 2016; 10.1186/s12870-016-0817-1 (krzywinska2016phosphataseabi1and pages 2-4)
Catalytic reaction and metal dependence ABI1 is a metal-dependent Ser/Thr phosphoprotein phosphatase: phosphoprotein + H₂O → dephosphorylated protein + orthophosphate. Mg²⁺ supports PP2C catalysis; wild-type ABI1 and abi1-1 show comparable activity at optimal Mg²⁺, whereas abi1-1 has impaired Mg²⁺ binding under limiting conditions. Loss of substrate radiolabel and activation-loop phosphorylation demonstrated dephosphorylation. Mg²⁺-dependent behavior was assessed biochemically for wild-type and G180D proteins. Umezawa et al.; October 2009; 10.1073/pnas.0907095106; Moes et al.; June 2008; 10.1111/j.1365-313X.2008.03454.x (umezawa2009type2cprotein pages 4-4, umezawa2009type2cprotein pages 3-4, moes2008nuclearlocalizationof pages 10-11)
Direct substrates Best-established physiological substrates are SnRK2 kinases. ABI1 directly dephosphorylates and inactivates ABA-responsive SnRK2.2/SRK2D, SnRK2.3/SRK2I, and SnRK2.6/OST1/SRK2E; it also dephosphorylates SnRK2.4 at activation-loop Ser158 and inhibits SnRK2.8. Artificial-substrate activity does not reliably predict SnRK2 inactivation, indicating recognition beyond generic phosphoserine/threonine hydrolysis. Purified-protein dephosphorylation, loss of kinase activity, yeast two-hybrid/BiFC interaction, protoplast assays, and salt-treated cell assays; a clade-B PP2C control did not inhibit SnRK2.4. Umezawa et al.; October 2009; 10.1073/pnas.0907095106; Krzywińska et al.; June 2016; 10.1186/s12870-016-0817-1 (umezawa2009type2cprotein pages 4-4, krzywinska2016phosphataseabi1and pages 2-4, umezawa2009type2cprotein pages 3-4)
ABA-receptor regulation In the absence of ABA, ABI1 restrains signaling by dephosphorylating SnRK2s. ABA-bound PYR/PYL/RCAR receptors bind and inhibit ABI1, releasing SnRK2 activity; receptor-overexpression evidence supports broader depletion/inactivation of clade-A PP2Cs. PYR1 inhibited ABI1-mediated SnRK2 inactivation only in the presence of ABA; in planta ABI1 complexes recovered 9 of 14 soluble receptor-family members. A 2024 multi-omics study analyzed RCAR6/RCAR10 overexpression with replicated phosphoproteomic, proteomic, and metabolomic measurements. Umezawa et al.; October 2009; 10.1073/pnas.0907095106; Joshi-Saha et al.; July 2011; 10.1093/mp/ssr055; Yoshida et al.; April 2024; 10.1111/tpj.16765 (umezawa2009type2cprotein pages 4-4, joshisaha2011abscisicacidsignal pages 6-7, yoshida2024integratingmultiomicsdata pages 2-3)
Structural mechanism ABI1 engages SnRK2.6 through complementary interfaces that position the kinase activation loop at the ABI1 catalytic center. Conversely, an ABA-bound PYL receptor occupies/occludes the PP2C substrate-binding and active-site region, explaining mutually exclusive receptor-versus-kinase recognition. A 2.6 Å SnRK2.6 kinase-domain structure, biochemical mapping, and computational modeling identified two ABI1–SnRK2.6 interfaces and their catalytic orientation. Xie et al.; 2 January 2012; 10.1074/jbc.M111.313106 (xie2012molecularmechanismfor pages 1-2)
Subcellular localization ABI1 is nucleocytoplasmic, with experimentally important nuclear action; interactions with SnRK2s occur in both nucleus and cytoplasm, and signaling can also involve plasma-membrane-associated contexts. ABA itself did not detectably relocalize ABI1 in the reported assay. GFP imaging, BiFC, deletion/mutation of ABI1’s C-terminal NLS, and rescue with a heterologous SV40 NLS showed that nuclear targeting is required for suppression of ABA-responsive transcription. SnRK2.6 and ABI1 are coexpressed in guard cells. Moes et al.; June 2008; 10.1111/j.1365-313X.2008.03454.x; Umezawa et al.; October 2009; 10.1073/pnas.0907095106 (moes2008nuclearlocalizationof pages 1-2, moes2008nuclearlocalizationof pages 6-7, moes2008nuclearlocalizationof pages 2-3, umezawa2009type2cprotein pages 2-3)
Dominant abi1-1 allele abi1-1 encodes ABI1 G180D in the catalytic domain. The substitution disrupts PYL–PP2C regulation, leaving the phosphatase refractory to ABA-receptor inhibition and able to continue suppressing SnRK2s; preferential nuclear accumulation also contributes to its dominant ABA-insensitive behavior. The mutant retained SnRK2-inactivating activity despite ABA plus PYR1. Localization/NLS experiments showed that nuclear targeting was necessary for strong mutant effects; wild-type and mutant proteins were not simply distinguished by higher maximal catalytic activity. Moes et al.; June 2008; 10.1111/j.1365-313X.2008.03454.x; Umezawa et al.; October 2009; 10.1073/pnas.0907095106 (umezawa2009type2cprotein pages 4-4, umezawa2009type2cprotein pages 2-3, moes2008nuclearlocalizationof pages 9-10, moes2008nuclearlocalizationof pages 10-11)
Physiological outputs By restraining SnRK2 signaling, ABI1 controls ABA-responsive transcription, germination, root growth, guard-cell/stomatal behavior, water loss, and salt-responsive root growth. These are pathway outputs rather than evidence that ABI1 directly dephosphorylates every downstream effector. abi1-expressing lines germinated at >90% in 10 µM ABA, whereas controls were fully inhibited by 1 µM ABA; at 100 µM ABA, root elongation was reduced by ~35% in abi1 lines versus >80% in NLS-deficient lines, and abi1 leaves lost about twice as much water. ABI1 also inhibited salt-activated SnRK2.4 in vitro and in vivo. Moes et al.; June 2008; 10.1111/j.1365-313X.2008.03454.x; Krzywińska et al.; June 2016; 10.1186/s12870-016-0817-1 (moes2008nuclearlocalizationof pages 5-6, krzywinska2016phosphataseabi1and pages 2-4)
2024 development BIK1 supplies an osmotic-stress route for releasing SnRK2.6 from ABI1/clade-A PP2C inhibition. BIK1 phosphorylates SnRK2.6 at Tyr163 and Tyr182; Tyr182 lies near the PP2C tryptophan lock and may weaken docking. This complements, rather than replaces, canonical ABA–PYL inhibition of ABI1. BIK1 reduced SnRK2.6–ABI1 interaction in yeast three-hybrid and split-luciferase assays, especially under 1 M mannitol, without detectable stable BIK1–ABI1 binding. Osmotic activation assays used 0.6 M mannitol and three biological replicates; BIK1 could overcome abi1-1-mediated inhibition. Li et al.; published online 21 October 2024; 10.1038/s44318-024-00277-0 (li2024osmoticsignalingreleases pages 1-2, li2024osmoticsignalingreleases pages 2-3, li2024osmoticsignalingreleases pages 10-12, li2024osmoticsignalingreleases pages 3-4)

Table: Evidence-based annotation of Arabidopsis ABI1, spanning identity, enzymology, substrates, pathway regulation, localization, mutant biology, physiological outputs, and a 2024 osmotic-signaling mechanism.

Molecular function and catalyzed reaction

ABI1 catalyzes hydrolytic removal of phosphate from phosphoserine/phosphothreonine residues:

phosphoprotein + H₂O → dephosphorylated protein + orthophosphate.

As a PP2C/PPM-family enzyme, catalysis is divalent-metal dependent, with Mg²⁺ supporting activity. Wild-type ABI1 and the dominant abi1-1/G180D protein reportedly have comparable phosphatase activity at optimal Mg²⁺; the mutant instead exhibits altered behavior under limiting Mg²⁺ and, more importantly, impaired regulation by ABA receptors. Thus abi1-1 should not simply be annotated as a constitutively more active catalytic enzyme. (moes2008nuclearlocalizationof pages 10-11)

Substrate specificity

The strongest direct-substrate evidence concerns SnRK2 kinases:

  1. ABA-responsive subclass-III SnRK2s: ABI1 physically associates with and dephosphorylates SnRK2.2/SRK2D, SnRK2.3/SRK2I, and SnRK2.6/OST1/SRK2E, thereby suppressing kinase activity and autophosphorylation. At least five ABA-responsive sites in SnRK2 activation loops were found to be PP2C-sensitive. (umezawa2009type2cprotein pages 4-4, xie2012molecularmechanismfor pages 1-2)
  2. SnRK2.4: purified ABI1 removed phosphorylation from activation-loop Ser158, which is required for kinase activity. ABI1 inhibited SnRK2.4 in vitro, in salt-treated protoplasts, and in Arabidopsis T87 cells; a clade-B PP2C control did not reproduce the effect. (krzywinska2016phosphataseabi1and pages 2-4)
  3. SnRK2.8: ABI1 also dephosphorylated and inhibited this group-2 kinase, indicating that its substrate range extends beyond the canonical ABA-activated subclass III. (krzywinska2016phosphataseabi1and pages 2-4)

Activity against generic artificial phosphatase substrates did not predict the ability to inactivate SnRK2s. ABI1 specificity therefore depends on productive protein–protein docking and presentation of the kinase activation loop, not merely recognition of any phosphoserine/phosphothreonine. (umezawa2009type2cprotein pages 4-4)

Evidence also connects clade-A PP2Cs to SnRK1 and other kinases, but these broader findings should not automatically be treated as equally well-established ABI1-specific substrates. The direct physiological annotation should remain centered on SnRK2 dephosphorylation. (yoshida2024integratingmultiomicsdata pages 2-3)

Position in the core ABA-signaling pathway

Signal-off state

At low ABA, ABI1 binds activated or activatable SnRK2s and removes activation-loop phosphate. This both reverses kinase activation and stabilizes an inhibitory PP2C–SnRK2 complex. Consequently, phosphorylation of downstream ABA-response factors remains low. (umezawa2009type2cprotein pages 4-4, xie2012molecularmechanismfor pages 1-2)

Signal-on state

ABA binds a PYR/PYL/RCAR receptor, causing the receptor to engage ABI1 and occlude its substrate-binding/catalytic region. PYR1 experimentally inhibited ABI1-mediated SnRK2 inactivation in an ABA-dependent manner. In planta affinity purification of ABI1 recovered predominantly nine of the fourteen soluble PYR/PYL/RCAR family members, supporting extensive receptor connectivity. (umezawa2009type2cprotein pages 4-4, joshisaha2011abscisicacidsignal pages 6-7)

Released SnRK2.2/2.3/2.6 kinases can then phosphorylate ABA-responsive transcription factors and transport proteins. For SnRK2.6/OST1, relevant downstream outputs include ion channels such as SLAC1 and KAT1; these channels are downstream kinase substrates, not demonstrated direct ABI1 substrates in the evidence reviewed. (xie2012molecularmechanismfor pages 1-2)

Structural basis

Structural and biochemical analysis resolved the SnRK2.6 kinase domain at 2.6 Å and identified two ABI1–SnRK2.6 interfaces. These contacts orient the SnRK2.6 activation loop toward the ABI1 catalytic center, providing a physical explanation for efficient dephosphorylation. ABA-bound PYL receptors engage an overlapping PP2C surface and obstruct substrate entry, explaining why receptor and kinase binding are functionally antagonistic. (xie2012molecularmechanismfor pages 1-2)

Cellular localization

ABI1 is best described as nucleocytoplasmic, with functionally important nuclear activity. GFP and BiFC experiments detected ABI1 or ABI1–SnRK2 interactions in both nucleus and cytoplasm; ABI1 and SnRK2.6 are coexpressed in guard cells. Some evidence also places ABI1 in plasma-membrane-associated signaling contexts, but it is not an integral membrane protein. (umezawa2009type2cprotein pages 2-3, moes2008nuclearlocalizationof pages 1-2, moes2008nuclearlocalizationof pages 6-7)

A predicted C-terminal nuclear-localization signal is functionally important. Deleting or mutating it redistributed ABI1/abi1-1 toward the cytosol and abolished much of their capacity to suppress ABA-responsive transcription. Addition of a heterologous SV40 NLS restored nuclear localization and signaling inhibition, strongly supporting a causal requirement for nuclear targeting. ABA treatment itself did not detectably relocalize ABI1 in these experiments. (moes2008nuclearlocalizationof pages 7-9, moes2008nuclearlocalizationof pages 6-7, moes2008nuclearlocalizationof pages 2-3)

The dominant abi1-1 protein accumulates preferentially in nuclei relative to wild-type ABI1, which is distributed more evenly between nucleus and cytosol. Treatment with 50 µM MG132 enhanced wild-type ABI1 nuclear compartmentation without detectably increasing total ABI1 abundance, suggesting regulated trafficking or retention rather than simple stabilization. (moes2008nuclearlocalizationof pages 9-10)

Biological processes and physiological implementation

ABI1’s principal biological role is setting the activation threshold and termination rate of ABA/SnRK2 signaling. Its documented pathway outputs include:

Quantitatively, abi1-expressing lines germinated at >90% in 10 µM ABA, whereas control germination was fully inhibited by 1 µM ABA. At 100 µM ABA, root elongation was reduced by approximately 35% in abi1 lines but by >80% in NLS-deficient abi1 lines. Leaves expressing nuclear-localized abi1 lost approximately twice as much water as controls or NLS-deficient lines. These data demonstrate that nuclear phosphatase action has whole-plant consequences for ABA sensitivity and water balance. (moes2008nuclearlocalizationof pages 5-6)

The abi1-1 allele: mechanistic importance

The classic dominant allele abi1-1 encodes G180D in the PP2C catalytic-domain region. The substitution disrupts productive PYR/PYL–PP2C interaction, so ABA-bound receptors cannot efficiently inhibit the mutant phosphatase. abi1-1 therefore continues binding and suppressing SnRK2s in the presence of ABA, producing dominant ABA insensitivity. Preferential nuclear accumulation further strengthens suppression of transcriptional ABA outputs. (umezawa2009type2cprotein pages 4-4, umezawa2009type2cprotein pages 2-3, moes2008nuclearlocalizationof pages 9-10)

This distinction is important for annotation: loss-of-function ABI1 alleles support the conclusion that normal ABI1 is a negative ABA regulator, whereas abi1-1 is a receptor-refractory, hypermorphic signaling allele—not a conventional null and not necessarily an intrinsically faster enzyme. (alandes2013molecularandgenetic pages 29-32, moes2008nuclearlocalizationof pages 10-11)

Recent developments, 2023–2024

BIK1 provides an osmotic route around PP2C inhibition

A 2024 EMBO Journal study reported that the receptor-like cytoplasmic kinase BIK1 helps release SnRK2.6 from ABI1/clade-A PP2C inhibition during osmotic stress. BIK1 phosphorylates SnRK2.6 at Tyr163 and Tyr182; Tyr182 lies near the PP2C tryptophan “lock,” and phosphorylation is proposed to weaken PP2C docking. BIK1 reduced the SnRK2.6–ABI1 interaction, particularly under 1 M mannitol, but did not detectably form a stable complex with ABI1, indicating that it acts by modifying the kinase. (li2024osmoticsignalingreleases pages 10-12, li2024osmoticsignalingreleases pages 3-4)

Osmotic SnRK2 activation was tested with 0.6 M mannitol and phospho-S175 antibodies using three biological replicates. BIK1 could overcome inhibition by abi1-1, while bik1 mutants showed impaired SnRK2 activation, stress-gene expression, ABA accumulation, growth maintenance, and water-loss control. This updates the canonical model: PYL–ABA inhibition of ABI1 remains central, but osmotic signaling can additionally destabilize the PP2C–SnRK2 complex from the kinase side. Publication: 21 October 2024, DOI/URL: https://doi.org/10.1038/s44318-024-00277-0. (li2024osmoticsignalingreleases pages 1-2, li2024osmoticsignalingreleases pages 2-3)

Multi-omics places PP2C suppression within energy–stress integration

A 2024 phosphoproteomic/proteomic/metabolomic study of RCAR6/PYL12-overexpressing Arabidopsis found that receptor activation decreased levels of clade-A PP2C coreceptors and activated both SnRK2 and SnRK1-associated programs. The design included three biological replicates for Col-0 and RCAR6 under control conditions and three per line under drought; the RCAR10 control arm had only two replicates and was not emphasized statistically. The study broadens the interpretation of receptor–PP2C signaling toward coordinated water- and energy-saving metabolism, although it does not establish every observed phosphosite or metabolic change as an ABI1-specific effect. Publication: April 2024, DOI/URL: https://doi.org/10.1111/tpj.16765. (yoshida2024integratingmultiomicsdata pages 2-3)

Applications and translational relevance

ABI1 is chiefly implemented as a research and engineering control point rather than as a commercial standalone product. Current applications include:

  1. Chemical screening: the ABA–PYL–PP2C interface provides a structurally defined target for ABA agonists or antagonists intended to manipulate drought responses and stomatal behavior. The receptor’s occupation of ABI1’s active-site region supplies a direct assayable mechanism. (umezawa2009type2cprotein pages 4-4, xie2012molecularmechanismfor pages 1-2)
  2. Synthetic and crop signaling design: altering receptor abundance or PP2C sensitivity can shift the threshold of ABA responses. However, because ABI1 affects germination, roots, transcription, stomata, and growth, constitutive inhibition is likely to impose growth–stress trade-offs; tissue-specific or inducible modulation is more defensible than blanket suppression. (yoshida2024integratingmultiomicsdata pages 2-3, moes2008nuclearlocalizationof pages 5-6)
  3. Stress-pathway dissection: abi1-1 is a powerful genetic reagent for separating PYL-dependent ABA release from alternative mechanisms such as BIK1-mediated osmotic release of SnRK2s. (li2024osmoticsignalingreleases pages 1-2, li2024osmoticsignalingreleases pages 2-3)

Expert interpretation and annotation confidence

The convergent genetic, biochemical, localization, and structural evidence makes the core annotation high confidence: ABI1 is a nucleocytoplasmic clade-A PP2C that directly dephosphorylates SnRK2 activation loops and functions as an ABA-pathway brake. The most defensible primary substrates are SnRK2 kinases, especially SnRK2.2/2.3/2.6 and SnRK2.4. Broad physiological traits should be annotated as downstream consequences rather than evidence of direct substrate recognition. (umezawa2009type2cprotein pages 4-4, krzywinska2016phosphataseabi1and pages 2-4, xie2012molecularmechanismfor pages 1-2)

The latest research does not overturn this model. Instead, it shows that the ABI1–SnRK2 switch is embedded in a larger, spatially and environmentally regulated network: receptors inhibit ABI1 from the phosphatase side, whereas osmotic signaling can weaken the same complex by modifying SnRK2.6. (li2024osmoticsignalingreleases pages 1-2, li2024osmoticsignalingreleases pages 10-12)

Key references

References

  1. (krzywinska2016phosphataseabi1and pages 2-4): Ewa Krzywińska, Maria Bucholc, Anna Kulik, Arkadiusz Ciesielski, Małgorzata Lichocka, Janusz Dębski, Agnieszka Ludwików, Michał Dadlez, Pedro L. Rodriguez, and Grażyna Dobrowolska. Phosphatase abi1 and okadaic acid-sensitive phosphoprotein phosphatases inhibit salt stress-activated snrk2.4 kinase. BMC Plant Biology, Jun 2016. URL: https://doi.org/10.1186/s12870-016-0817-1, doi:10.1186/s12870-016-0817-1. This article has 64 citations and is from a peer-reviewed journal.

  2. (umezawa2009type2cprotein pages 4-4): Taishi Umezawa, Naoyuki Sugiyama, Masahide Mizoguchi, Shimpei Hayashi, Fumiyoshi Myouga, Kazuko Yamaguchi-Shinozaki, Yasushi Ishihama, Takashi Hirayama, and Kazuo Shinozaki. Type 2c protein phosphatases directly regulate abscisic acid-activated protein kinases in arabidopsis. Proceedings of the National Academy of Sciences, 106:17588-17593, Oct 2009. URL: https://doi.org/10.1073/pnas.0907095106, doi:10.1073/pnas.0907095106. This article has 1336 citations and is from a highest quality peer-reviewed journal.

  3. (xie2012molecularmechanismfor pages 1-2): Tian Xie, Ruobing Ren, Yuan-yuan Zhang, Yuxuan Pang, Chuangye Yan, Xinqi Gong, Yuan He, Wenqi Li, Di Miao, Qi Hao, Haiteng Deng, Zhixin Wang, Jia-Wei Wu, and Nieng Yan. Molecular mechanism for inhibition of a critical component in the arabidopsis thaliana abscisic acid signal transduction pathways, snrk2.6, by protein phosphatase abi1. Journal of Biological Chemistry, 287(1):794-802, Jan 2012. URL: https://doi.org/10.1074/jbc.m111.313106, doi:10.1074/jbc.m111.313106. This article has 87 citations and is from a domain leading peer-reviewed journal.

  4. (umezawa2009type2cprotein pages 3-4): Taishi Umezawa, Naoyuki Sugiyama, Masahide Mizoguchi, Shimpei Hayashi, Fumiyoshi Myouga, Kazuko Yamaguchi-Shinozaki, Yasushi Ishihama, Takashi Hirayama, and Kazuo Shinozaki. Type 2c protein phosphatases directly regulate abscisic acid-activated protein kinases in arabidopsis. Proceedings of the National Academy of Sciences, 106:17588-17593, Oct 2009. URL: https://doi.org/10.1073/pnas.0907095106, doi:10.1073/pnas.0907095106. This article has 1336 citations and is from a highest quality peer-reviewed journal.

  5. (moes2008nuclearlocalizationof pages 10-11): Danièle Moes, Axel Himmelbach, Arthur Korte, Georg Haberer, and Erwin Grill. Nuclear localization of the mutant protein phosphatase abi1 is required for insensitivity towards aba responses in arabidopsis. The Plant journal : for cell and molecular biology, 54 5:806-19, Jun 2008. URL: https://doi.org/10.1111/j.1365-313x.2008.03454.x, doi:10.1111/j.1365-313x.2008.03454.x. This article has 126 citations.

  6. (joshisaha2011abscisicacidsignal pages 6-7): Archana Joshi-Saha, Christiane Valon, and Jeffrey Leung. Abscisic acid signal off the starting block. Molecular plant, 4 4:562-80, Jul 2011. URL: https://doi.org/10.1093/mp/ssr055, doi:10.1093/mp/ssr055. This article has 144 citations and is from a highest quality peer-reviewed journal.

  7. (yoshida2024integratingmultiomicsdata pages 2-3): Takuya Yoshida, Julia Mergner, Zhenyu Yang, Jinghui Liu, Bernhard Kuster, Alisdair R. Fernie, and Erwin Grill. Integrating multi-omics data reveals energy and stress signaling activated by abscisic acid in arabidopsis. The Plant journal : for cell and molecular biology, 119:1112-1133, Apr 2024. URL: https://doi.org/10.1111/tpj.16765, doi:10.1111/tpj.16765. This article has 13 citations.

  8. (moes2008nuclearlocalizationof pages 1-2): Danièle Moes, Axel Himmelbach, Arthur Korte, Georg Haberer, and Erwin Grill. Nuclear localization of the mutant protein phosphatase abi1 is required for insensitivity towards aba responses in arabidopsis. The Plant journal : for cell and molecular biology, 54 5:806-19, Jun 2008. URL: https://doi.org/10.1111/j.1365-313x.2008.03454.x, doi:10.1111/j.1365-313x.2008.03454.x. This article has 126 citations.

  9. (moes2008nuclearlocalizationof pages 6-7): Danièle Moes, Axel Himmelbach, Arthur Korte, Georg Haberer, and Erwin Grill. Nuclear localization of the mutant protein phosphatase abi1 is required for insensitivity towards aba responses in arabidopsis. The Plant journal : for cell and molecular biology, 54 5:806-19, Jun 2008. URL: https://doi.org/10.1111/j.1365-313x.2008.03454.x, doi:10.1111/j.1365-313x.2008.03454.x. This article has 126 citations.

  10. (moes2008nuclearlocalizationof pages 2-3): Danièle Moes, Axel Himmelbach, Arthur Korte, Georg Haberer, and Erwin Grill. Nuclear localization of the mutant protein phosphatase abi1 is required for insensitivity towards aba responses in arabidopsis. The Plant journal : for cell and molecular biology, 54 5:806-19, Jun 2008. URL: https://doi.org/10.1111/j.1365-313x.2008.03454.x, doi:10.1111/j.1365-313x.2008.03454.x. This article has 126 citations.

  11. (umezawa2009type2cprotein pages 2-3): Taishi Umezawa, Naoyuki Sugiyama, Masahide Mizoguchi, Shimpei Hayashi, Fumiyoshi Myouga, Kazuko Yamaguchi-Shinozaki, Yasushi Ishihama, Takashi Hirayama, and Kazuo Shinozaki. Type 2c protein phosphatases directly regulate abscisic acid-activated protein kinases in arabidopsis. Proceedings of the National Academy of Sciences, 106:17588-17593, Oct 2009. URL: https://doi.org/10.1073/pnas.0907095106, doi:10.1073/pnas.0907095106. This article has 1336 citations and is from a highest quality peer-reviewed journal.

  12. (moes2008nuclearlocalizationof pages 9-10): Danièle Moes, Axel Himmelbach, Arthur Korte, Georg Haberer, and Erwin Grill. Nuclear localization of the mutant protein phosphatase abi1 is required for insensitivity towards aba responses in arabidopsis. The Plant journal : for cell and molecular biology, 54 5:806-19, Jun 2008. URL: https://doi.org/10.1111/j.1365-313x.2008.03454.x, doi:10.1111/j.1365-313x.2008.03454.x. This article has 126 citations.

  13. (moes2008nuclearlocalizationof pages 5-6): Danièle Moes, Axel Himmelbach, Arthur Korte, Georg Haberer, and Erwin Grill. Nuclear localization of the mutant protein phosphatase abi1 is required for insensitivity towards aba responses in arabidopsis. The Plant journal : for cell and molecular biology, 54 5:806-19, Jun 2008. URL: https://doi.org/10.1111/j.1365-313x.2008.03454.x, doi:10.1111/j.1365-313x.2008.03454.x. This article has 126 citations.

  14. (li2024osmoticsignalingreleases pages 1-2): Guo-Jun Li, Kong Chen, Shujing Sun, and Yang Zhao. Osmotic signaling releases pp2c-mediated inhibition of arabidopsis snrk2s via the receptor-like cytoplasmic kinase bik1. The EMBO Journal, 43:6076-6103, Oct 2024. URL: https://doi.org/10.1038/s44318-024-00277-0, doi:10.1038/s44318-024-00277-0. This article has 44 citations.

  15. (li2024osmoticsignalingreleases pages 2-3): Guo-Jun Li, Kong Chen, Shujing Sun, and Yang Zhao. Osmotic signaling releases pp2c-mediated inhibition of arabidopsis snrk2s via the receptor-like cytoplasmic kinase bik1. The EMBO Journal, 43:6076-6103, Oct 2024. URL: https://doi.org/10.1038/s44318-024-00277-0, doi:10.1038/s44318-024-00277-0. This article has 44 citations.

  16. (li2024osmoticsignalingreleases pages 10-12): Guo-Jun Li, Kong Chen, Shujing Sun, and Yang Zhao. Osmotic signaling releases pp2c-mediated inhibition of arabidopsis snrk2s via the receptor-like cytoplasmic kinase bik1. The EMBO Journal, 43:6076-6103, Oct 2024. URL: https://doi.org/10.1038/s44318-024-00277-0, doi:10.1038/s44318-024-00277-0. This article has 44 citations.

  17. (li2024osmoticsignalingreleases pages 3-4): Guo-Jun Li, Kong Chen, Shujing Sun, and Yang Zhao. Osmotic signaling releases pp2c-mediated inhibition of arabidopsis snrk2s via the receptor-like cytoplasmic kinase bik1. The EMBO Journal, 43:6076-6103, Oct 2024. URL: https://doi.org/10.1038/s44318-024-00277-0, doi:10.1038/s44318-024-00277-0. This article has 44 citations.

  18. (moes2008nuclearlocalizationof pages 7-9): Danièle Moes, Axel Himmelbach, Arthur Korte, Georg Haberer, and Erwin Grill. Nuclear localization of the mutant protein phosphatase abi1 is required for insensitivity towards aba responses in arabidopsis. The Plant journal : for cell and molecular biology, 54 5:806-19, Jun 2008. URL: https://doi.org/10.1111/j.1365-313x.2008.03454.x, doi:10.1111/j.1365-313x.2008.03454.x. This article has 126 citations.

  19. (alandes2013molecularandgenetic pages 29-32): Regina Antoni Alandes. Molecular and genetic analyses of the pp2c-aba receptor interaction in the abscisic acid signaling pathway. ArXiv, Jun 2013. URL: https://doi.org/10.4995/thesis/10251/29756, doi:10.4995/thesis/10251/29756. This article has 0 citations.

Artifacts

Citations

  1. xie2012molecularmechanismfor pages 1-2
  2. moes2008nuclearlocalizationof pages 10-11
  3. yoshida2024integratingmultiomicsdata pages 2-3
  4. moes2008nuclearlocalizationof pages 9-10
  5. moes2008nuclearlocalizationof pages 6-7
  6. moes2008nuclearlocalizationof pages 5-6
  7. moes2008nuclearlocalizationof pages 7-9
  8. li2024osmoticsignalingreleases pages 1-2
  9. joshisaha2011abscisicacidsignal pages 6-7
  10. moes2008nuclearlocalizationof pages 1-2
  11. moes2008nuclearlocalizationof pages 2-3
  12. li2024osmoticsignalingreleases pages 2-3
  13. li2024osmoticsignalingreleases pages 10-12
  14. li2024osmoticsignalingreleases pages 3-4
  15. alandes2013molecularandgenetic pages 29-32
  16. 10.1186/s12870-016-0817-1
  17. 10.1073/pnas.0907095106
  18. 10.1111/j.1365-313X.2008.03454.x
  19. 10.1093/mp/ssr055
  20. 10.1111/tpj.16765
  21. 10.1074/jbc.M111.313106
  22. 10.1038/s44318-024-00277-0
  23. s
  24. https://doi.org/10.1186/s12870-016-0817-1
  25. https://doi.org/10.1073/pnas.0907095106
  26. https://doi.org/10.1111/j.1365-313x.2008.03454.x
  27. https://doi.org/10.1093/mp/ssr055
  28. https://doi.org/10.1111/tpj.16765
  29. https://doi.org/10.1074/jbc.m111.313106
  30. https://doi.org/10.1038/s44318-024-00277-0
  31. https://doi.org/10.1038/s44318-024-00277-0.
  32. https://doi.org/10.1111/tpj.16765.
  33. https://doi.org/10.1073/pnas.0907095106.
  34. https://doi.org/10.1074/jbc.M111.313106.
  35. https://doi.org/10.1111/j.1365-313X.2008.03454.x.
  36. https://doi.org/10.1186/s12870-016-0817-1.
  37. https://doi.org/10.1186/s12870-016-0817-1,
  38. https://doi.org/10.1073/pnas.0907095106,
  39. https://doi.org/10.1074/jbc.m111.313106,
  40. https://doi.org/10.1111/j.1365-313x.2008.03454.x,
  41. https://doi.org/10.1093/mp/ssr055,
  42. https://doi.org/10.1111/tpj.16765,
  43. https://doi.org/10.1038/s44318-024-00277-0,
  44. https://doi.org/10.4995/thesis/10251/29756,