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AHA1, activator of heat shock 90kDa protein ATPase homolog 1

Encodes a plasma membrane proton ATPase. Mutants have a reduced ability to close their stomata in response to drought and are affected in stomatal but not seed responsiveness to ABA. (from NCBI)
Top mentioned proteins: ATPase, Hsp90, fibrillin-1, CAN, ACID
Papers on AHA1
Dynamics and environmental responses of PATROL1 in Arabidopsis subsidiary cells.
Hasezawa et al., Kashiwa, Japan. In Plant Cell Physiol, Apr 2014
In this work, we studied the dynamic behavior and environmental responses of PATROL1, which has been identified as a translocation factor of the plasma membrane proton pump ATPase (PM H(+)-ATPase) AHA1 in guard cells and subsidiary cells in Arabidopsis thaliana.
Expression of a translationally fused TAP-tagged plasma membrane proton pump in Arabidopsis thaliana.
Sussman et al., Madison, United States. In Biochemistry, Feb 2014
The Arabidopsis thaliana plasma membrane proton ATPase genes, AHA1 and AHA2, are the two most highly expressed isoforms of an 11 gene family and are collectively essential for embryo development.
Co-immunoprecipitation-based identification of putative BAX INHIBITOR-1-interacting proteins involved in cell death regulation and plant-powdery mildew interactions.
Hückelhoven et al., Freising, Germany. In Mol Plant Pathol, Oct 2013
Five selected candidate proteins, a RIBOPHORIN II (RPN2) family protein, VACUOLAR ATP SYNTHASE SUBUNIT A (VHA-A), cytochrome P450 83A1 (CYP83A1), H(+) -ATPASE 1 (AHA1) and PROHIBITIN 2 (PHB2), were further investigated with regard to their role in BI-1-associated processes.
Haem oxygenase modifies salinity tolerance in Arabidopsis by controlling K⁺ retention via regulation of the plasma membrane H⁺-ATPase and by altering SOS1 transcript levels in roots.
Shabala et al., Hobart, Australia. In J Exp Bot, 2013
The gene expression analysis after 12h and 24h of salt stress revealed high expression levels of H(+)-ATPases (AHA1/2/3) and Na(+)/H(+) antiporter [salt overly sensitive1 (SOS1)] transcripts in the plasma membrane of HO overexpressors.
Stabilization of polyplexes via polymer crosslinking for efficient siRNA delivery.
Wagner et al., München, Germany. In Eur J Pharm Sci, 2013
Downregulation of endogenous AHA1 mRNA (85% knockdown compared to control) by crosslinked HD-O/AHA1-siRNA particles was detected by quantitative real-time PCR.
A Munc13-like protein in Arabidopsis mediates H+-ATPase translocation that is essential for stomatal responses.
Iba et al., Fukuoka, Japan. In Nat Commun, 2012
Here we describe the isolation of an Arabidopsis gene, PATROL1, that controls the translocation of a major H(+)-ATPase, AHA1, to the plasma membrane.
Modulation of the cochaperone AHA1 regulates heat-shock protein 90 and endothelial NO synthase activation by vascular endothelial growth factor.
Gratton et al., Montréal, Canada. In Arterioscler Thromb Vasc Biol, 2012
Our study is designed to determine whether modulation of the activator of Hsp90 ATPase 1 (AHA1) regulates the function of Hsp90 in ECs.
Dynamic tyrosine phosphorylation modulates cycling of the HSP90-P50(CDC37)-AHA1 chaperone machine.
Neckers et al., Bethesda, United States. In Mol Cell, 2012
Hsp90 phosphorylation on tyrosine313 promotes recruitment of AHA1, which stimulates Hsp90 ATPase activity, furthering the chaperoning process.
Characterization of the interaction of Aha1 with components of the Hsp90 chaperone machine and client proteins.
Matts et al., Stillwater, United States. In Biochim Biophys Acta, 2012
The interaction of Aha1 with Hsp90 and its co-chaperones in rabbit reticulocyte lysate (RRL) and in HeLa cell extracts, was characterized.
The effect of a genetically reduced plasma membrane protonmotive force on vegetative growth of Arabidopsis.
Sussman et al., Madison, United States. In Plant Physiol, 2012
In Arabidopsis (Arabidopsis thaliana), this gradient is generated by the plasma membrane proton pump encoded by a family of 11 genes (abbreviated as AHA, for Arabidopsis H(+)-ATPase), of which AHA1 and AHA2 are the two most predominantly expressed in seedlings and adult plants.
Phosphosite mapping of P-type plasma membrane H+-ATPase in homologous and heterologous environments.
Palmgren et al., Frederiksberg, Denmark. In J Biol Chem, 2012
After a mass spectrometric analysis of the resulting peptides we could identify 10 different phosphorylation sites in plasma membrane H(+)-ATPases AHA1, AHA2, AHA3, and AHA4/11, five of which have not been reported before, bringing the total number of phosphosites up to 11, which is substantially higher than reported so far for any other P-type ATPase.
The co-chaperone Hch1 regulates Hsp90 function differently than its homologue Aha1 and confers sensitivity to yeast to the Hsp90 inhibitor NVP-AUY922.
LaPointe et al., Edmonton, Canada. In Plos One, 2011
Deletion of HCH1, but not AHA1, mitigates the temperature sensitive phenotype and high sensitivity to Hsp90 inhibitor drugs observed in Saccharomyces cerevisiae that express either of these two Hsp90 variants.
Δ9-THC increases endogenous AHA1 expression in rat cerebellum and may modulate CB1 receptor function during chronic use.
Winsauer et al., New Orleans, United States. In J Neurochem, 2011
Six proteins were found to significantly differ among the four treatment groups, with Δ9-THC and ovariectomy (OVX) decreasing the mitochondrial proteins, pyruvate carboxylase and NADH dehydrogenase, whereas the levels of putative cytosolic molecular chaperones NM23B, translationally controlled tumor protein, DJ-1 and activator of heat-shock 90kDa protein ATPase homolog 1 (AHA1) were increased.
The activation of the Arabidopsis P-ATPase 1 by the brassinosteroid receptor BRI1 is independent of threonine 948 phosphorylation.
Harter et al., Tübingen, Germany. In Plant Signal Behav, 2011
Here, we show that BRI1 also associates with a mutant version of the Arabidopsis P-ATPase 1 (AHA1) characterized by an exchange of a well-known regulatory threonine for a non-phosphorylatable residue in the auto-inhibitory C-terminal domain.
Hsp90 cochaperone Aha1 is a negative regulator of the Saccharomyces MAL activator and acts early in the chaperone activation pathway.
Michels et al., New York City, United States. In J Biol Chem, 2010
an interaction between Aha1 and residues near the C terminus of Mal63
Biological and structural basis for Aha1 regulation of Hsp90 ATPase activity in maintaining proteostasis in the human disease cystic fibrosis.
Balch et al., Los Angeles, United States. In Mol Biol Cell, 2010
Data propose a model for Aha1 in the Hsp90 ATPase cycle where Aha1 regulates dwell time of Hsp90, and suggest Aha1 activity integrates chaperone function with client folding energetics by modulating ATPase sensitive dimer structural transitions.
Asymmetric activation of the hsp90 dimer by its cochaperone aha1.
Buchner et al., Garching bei München, Germany. In Mol Cell, 2010
For maximum activation of Hsp90, the two domains of Aha1 bind to sites in the middle and N-terminal domains of Hsp90 in a sequential manner.
Investigating the functions of the RIN4 protein complex during plant innate immune responses.
Coaker et al., Davis, United States. In Plant Signal Behav, 2009
However, the molecular mechanisms by which RIN4 controls multiple immune responses have remained elusive. in our recently published study, we purified components of the RIN4 protein complex from A. thaliana and identified several novel RIN4-associated proteins.1 we found that one class of RIN4-associated proteins, the plasma membrane H(+)-ATPases AHA1 and AHA2, play a crucial role in resisting pathogen invasion.
Genes and proteins governing the cellular sensitivity to HSP90 inhibitors: a mechanistic perspective.
Workman et al., United Kingdom. In Curr Cancer Drug Targets, 2003
Important determinants of response include: 1) Dependence upon key HSP90 client proteins such as ERBB2, steroid hormone receptors and AKT/PKB; 2) Levels of HSP90 family members and co-chaperones, such as HSP70 and AHA1; and 3) expression of various cell cycle and apoptotic regulators.
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