| http://purl.uniprot.org/citations/29453559 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/29453559 | http://www.w3.org/2000/01/rdf-schema#comment | "Plant vacuolar H+-transporting inorganic pyrophosphatase (V-PPase; EC 3.6.1.1) is a crucial enzyme that exists on the tonoplast to maintain pH homeostasis across the vacuolar membrane. This enzyme generates proton gradient between cytosol and vacuolar lumen by hydrolysis of a metabolic byproduct, pyrophosphate (PP i ). The regulation of V-PPase at protein level has drawn attentions of many workers for decades, but its mechanism is still unclear. In this work, we show that AVP1, the V-PPase from Arabidopsis thaliana, is a target protein for regulatory 14-3-3 proteins at the vacuolar membrane, and all twelve 14-3-3 isoforms were analyzed for their association with AVP1. In the presence of 14-3-3ν, -µ, -ο, and -ι, both enzymatic activities and its associated proton pumping of AVP1 were increased. Among these 14-3-3 proteins, 14-3-3 µ shows the highest stimulation on coupling efficiency. Furthermore, 14-3-3ν, -µ, -ο, and -ι exerted protection of AVP1 against the inhibition of suicidal substrate PP i at high concentration. Moreover, the thermal profile revealed the presence of 14-3-3ο improves the structural stability of AVP1 against high temperature deterioration. Additionally, the 14-3-3 proteins mitigate the inhibition of Na+ to AVP1. Besides, the binding sites/motifs of AVP1 were identified for each 14-3-3 protein. Taken together, a working model was proposed to elucidate the association of 14-3-3 proteins with AVP1 for stimulation of its enzymatic activity."xsd:string |
| http://purl.uniprot.org/citations/29453559 | http://purl.org/dc/terms/identifier | "doi:10.1007/s00232-018-0020-4"xsd:string |
| http://purl.uniprot.org/citations/29453559 | http://purl.uniprot.org/core/author | "Pan Y.J."xsd:string |
| http://purl.uniprot.org/citations/29453559 | http://purl.uniprot.org/core/author | "Lee C.H."xsd:string |
| http://purl.uniprot.org/citations/29453559 | http://purl.uniprot.org/core/author | "Liao Y.Y."xsd:string |
| http://purl.uniprot.org/citations/29453559 | http://purl.uniprot.org/core/author | "Pan R.L."xsd:string |
| http://purl.uniprot.org/citations/29453559 | http://purl.uniprot.org/core/author | "Lin W.H."xsd:string |
| http://purl.uniprot.org/citations/29453559 | http://purl.uniprot.org/core/author | "Liu T.Y."xsd:string |
| http://purl.uniprot.org/citations/29453559 | http://purl.uniprot.org/core/author | "Huang Y.F."xsd:string |
| http://purl.uniprot.org/citations/29453559 | http://purl.uniprot.org/core/author | "Hsu Y.D."xsd:string |
| http://purl.uniprot.org/citations/29453559 | http://purl.uniprot.org/core/author | "Huang L.K."xsd:string |
| http://purl.uniprot.org/citations/29453559 | http://purl.uniprot.org/core/date | "2018"xsd:gYear |
| http://purl.uniprot.org/citations/29453559 | http://purl.uniprot.org/core/name | "J Membr Biol"xsd:string |
| http://purl.uniprot.org/citations/29453559 | http://purl.uniprot.org/core/pages | "263-276"xsd:string |
| http://purl.uniprot.org/citations/29453559 | http://purl.uniprot.org/core/title | "Regulation of H+-pyrophosphatase by 14-3-3 Proteins from Arabidopsis thaliana."xsd:string |
| http://purl.uniprot.org/citations/29453559 | http://purl.uniprot.org/core/volume | "251"xsd:string |
| http://purl.uniprot.org/citations/29453559 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/29453559 |
| http://purl.uniprot.org/citations/29453559 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/29453559 |
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| http://purl.uniprot.org/uniprot/#_P31414-mappedCitation-29453559 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/29453559 |
| http://purl.uniprot.org/uniprot/A8MQH1 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/29453559 |
| http://purl.uniprot.org/uniprot/P31414 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/29453559 |