gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 25 Jan 2016.

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, CAN, fibrillin-1, ACID
Papers on AHA1
The role of plasma membrane H(+) -ATPase in jasmonate-induced ion fluxes and stomatal closure in Arabidopsis thaliana.
Shen et al., Beijing, China. In Plant J, Aug 2015
Here, we recorded the transmembrane ion fluxes of H(+) , Ca(2+) and K(+) in guard cells of wild-type (Col-0) Arabidopsis, the CORONATINE INSENSITIVE1 (COI1) mutant coi1-1 and the PM H(+) -ATPase mutants aha1-6 and aha1-7, using a non-invasive micro-test technique.
An Arabidopsis Plasma Membrane Proton ATPase Modulates JA Signaling and Is Exploited by the Pseudomonas syringae Effector Protein AvrB for Stomatal Invasion.
Zhou et al., Beijing, China. In Plant Cell, Jul 2015
Here, we show that the Pseudomonas syringae type III effector protein AvrB induces stomatal opening and enhances bacterial virulence in a manner dependent on RPM1-INTERACTING4 (RIN4), which promotes stomatal opening by positively regulating the Arabidopsis plasma membrane H(+)-ATPase (AHA1), which is presumed to directly regulate guard cell turgor pressure.
Phosphorylation of the Plant Immune Regulator RPM1-INTERACTING PROTEIN4 Enhances Plant Plasma Membrane H⁺-ATPase Activity and Inhibits Flagellin-Triggered Immune Responses in Arabidopsis.
Coaker et al., Norwich, United Kingdom. In Plant Cell, Jul 2015
The plasma membrane H(+)-ATPase AHA1 is highly expressed in guard cells, and its activation can induce stomatal opening.
Phytosulfokine Regulates Growth in Arabidopsis through a Response Module at the Plasma Membrane That Includes CYCLIC NUCLEOTIDE-GATED CHANNEL17, H+-ATPase, and BAK1.
Sauter et al., Tübingen, Germany. In Plant Cell, Jun 2015
While PSKR1 does not interact directly with CNGC17, it interacts with the plasma membrane-localized H(+)-ATPases AHA1 and AHA2 and with the BRI-associated receptor kinase 1 (BAK1).
Rapid regulation of the plasma membrane H⁺-ATPase activity is essential to salinity tolerance in two halophyte species, Atriplex lentiformis and Chenopodium quinoa.
Shabala et al., Nanjing, China. In Ann Bot, Feb 2015
METHODS: The kinetics of salt-induced net H(+), Na(+) and K(+) fluxes, membrane potential and AHA1/2/3 expression changes in the roots of two halophyte species, Atriplex lentiformis (saltbush) and Chenopodium quinoa (quinoa), were compared with data obtained from Arabidopsis thaliana roots.
Receptor kinase-mediated control of primary active proton pumping at the plasma membrane.
Palmgren et al., Frederiksberg, Denmark. In Plant J, 2014
Here we show that the major plasma membrane proton pumps in Arabidopsis, AHA1 and AHA2, interact directly in vitro and in planta with PSY1R, a receptor kinase of the plasma membrane that serves as a receptor for the peptide growth hormone PSY1.
Hormonal status and age differentially affect tolerance to the disruptive effects of delta-9-tetrahydrocannabinol (Δ(9)-THC) on learning in female rats.
Sutton et al., New Orleans, United States. In Front Pharmacol, 2014
Hippocampal protein expression of CB1R, AHA1 (a co-chaperone of CB1R) and HSP90β (a molecular chaperone modulated by AHA-1) was affected more by OVX than chronic Δ(9)-THC; striatal protein expression was not consistently affected by either manipulation.
Mutation of essential Hsp90 co-chaperones SGT1 or CNS1 renders yeast hypersensitive to overexpression of other co-chaperones.
Langworthy et al., Moscow, United States. In Curr Genet, 2014
However, overexpression of SBA1, PPT1, AHA1 or HCH1 caused varying levels of growth defects in an sgt1-K360E strain.
Protozoan HSP90-heterocomplex: molecular interaction network and biological significance.
Angel et al., Buenos Aires, Argentina. In Curr Protein Pept Sci, 2014
The HSP90-heterocomplex is also named the HSP90/HSP70 cycle because different co-chaperones (HIP, HSP40, HOP, p23, AHA1, immunophilins, PP5) participate in this complex by assembling sequentially, from the early to the mature complex.
Dynamics and environmental responses of PATROL1 in Arabidopsis subsidiary cells.
Hasezawa et al., Kashiwa, Japan. In Plant Cell Physiol, 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, 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, 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.
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.
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 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.
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.
share on facebooktweetadd +1mail to friends