Homologue structure of the SLAC1 anion channel for closing stomata in leaves.
Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Combined Automated Annotation using Multiple IEA Methods
CO2 regulator SLAC1 and its homologues are essential for anion homeostasis in plant cells.
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SLAC1 localizes to the guard-cell plasma membrane and its loss causes over-accumulation of osmoregulatory anions in guard cells.
"The loss-of-function mutation in SLAC1 was accompanied by an over-accumulation of the osmoregulatory anions in guard cell protoplasts."
SLAC1 is required for plant guard cell S-type anion channel function in stomatal signalling.
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SLAC1 is required for S-type (but not R-type) anion currents in guard cells and for stomatal closure to many stimuli.
"Mutations in SLAC1 impair slow (S-type) anion channel currents that are activated by cytosolic Ca2+ and abscisic acid, but do not affect rapid (R-type) anion channel currents or Ca2+ channel function."
Activity of guard cell anion channel SLAC1 is controlled by drought-stress signaling kinase-phosphatase pair.
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SLAC1 is an anion channel activated by OST1 and inhibited by ABI1 in Xenopus oocytes.
"Our studies demonstrate that SLAC1 represents the slow, deactivating, weak voltage-dependent anion channel of guard cells controlled by phosphorylation/dephosphorylation."
A protein kinase-phosphatase pair interacts with an ion channel to regulate ABA signaling in plant guard cells.
Guard cell anion channel SLAC1 is regulated by CDPK protein kinases with distinct Ca2+ affinities.
A plasma membrane receptor kinase, GHR1, mediates abscisic acid- and hydrogen peroxide-regulated stomatal movement in Arabidopsis.
Nitrated cyclic GMP modulates guard cell signaling in Arabidopsis.
Calcium-dependent and -independent stomatal signaling network and compensatory feedback control of stomatal opening via Ca2+ sensitivity priming.
A molecular pathway for CO₂ response in Arabidopsis guard cells.
S-type Anion Channels SLAC1 and SLAH3 Function as Essential Negative Regulators of Inward K+ Channels and Stomatal Opening in Arabidopsis.
Coordinating the overall stomatal response of plants: Rapid leaf-to-leaf communication during light stress.
STRESS INDUCED FACTOR 2 Regulates Arabidopsis Stomatal Immunity through Phosphorylation of the Anion Channel SLAC1.
Homologue structure of the SLAC1 anion channel for closing stomata in leaves.
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SLAC1 protomers each form a five-helix anion pore gated by conserved Phe450; AtSLAC1 F450A gives large constitutive Cl- currents.
"removal of the phenyl group in HiTehA F262A or in the homologous AtSLAC1 F450A resulted in very large Cl− currents relative to wild-type levels"
Ozone-triggered rapid stomatal response involves the production of reactive oxygen species, and is controlled by SLAC1 and OST1.
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OST1 phosphorylates SLAC1 at Ser120, required for ozone-induced rapid stomatal closure.
"only S120 was a specific phosphorylation site for OST1"
The receptor-like pseudokinase GHR1 is required for stomatal closure.
Structure and activity of SLAC1 channels for stomatal signaling in leaves.
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Multisite phosphorylation of AtSLAC1 strongly enhances channel activity.
"We identified 14 phosphorylation sites in AtSLAC1 and showed nearly 330-fold channel-activity enhancement with 4 to 6 of these phosphorylated."
Structure of the Arabidopsis guard cell anion channel SLAC1 suggests activation mechanism by phosphorylation.
Cryo-EM structures of the plant anion channel SLAC1 from Arabidopsis thaliana suggest a combined activation model.
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Open and closed AtSLAC1 structures show that phosphorylation dissociates the intracellular domain to open the pore.
"Multiple phosphorylation of an intracellular domain (ICD) causes dissociation of ICD from the transmembrane domain."
SLAC1 UniProtKB/Swiss-Prot record (Guard cell S-type anion channel SLAC1)
OpenScientist hypothesis adjudication: SLAC1 inhibition of KAT1 and AKT2
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No independent lab has replicated SLAC1 inhibition of KAT1/AKT2 since Zhang et al. 2016. The report recommends GO:0019870 only as a cautious, caveated non-core addition (or declining it), with GO:0015459 potassium channel regulator activity as a more conservative fallback; it does not consider the inward-rectifier child GO:0070320, so the KAT1 refinement to that term is a curator decision. Its Laanemets 2013 and Zhang 2016 quotes were checked against the sources; the citation counts were not re-checked.
"single study, single lab, heterologous oocyte system, gain-of-function"
Mutations in the SLAC1 anion channel slow stomatal opening and severely reduce K+ uptake channel activity via enhanced cytosolic [Ca2+] and increased Ca2+ sensitivity of K+ uptake channels.
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Reduced inward potassium-channel activity in slac1 mutants can be restored by lowering cytosolic calcium, supporting compensatory feedback rather than simple loss of a direct inhibitor.
"reducing [Ca(2+)](cyt) to < 10 nM rapidly restored the activity of K(+)(in) channels in slac1 closer to wild-type levels."
MAP3Kinase-dependent SnRK2-kinase activation is required for abscisic acid signal transduction and rapid osmotic stress response.
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Upstream RAF-like MAP3Ks enable reactivation after PP2C dephosphorylation and permit downstream transcription-factor and SLAC1 activation.
"ABA-triggered SnRK2 activation, transcription factor phosphorylation and SLAC1 activation require these M3Ks in vitro and in plants."
A unique voltage sensor sensitizes the potassium channel AKT2 to phosphoregulation.
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AKT2 can switch between inward-rectifying and nonrectifying gating modes, limiting a gating-specific description of its inhibition.
"when nonphosphorylated AKT2 behaves as an inward-rectifying potassium channel"