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Lentil seed aquaporins form a hetero-oligomer which is phosphorylated by a Mg2+-dependent and Ca2+-regulated kinase

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Názov:	Lentil seed aquaporins form a hetero-oligomer which is phosphorylated by a Mg2+-dependent and Ca2+-regulated kinase
Autori:	Harvengt, P, Vlerick, A, Fuks, B, Wattiez, R, Ruysschaert, Jean Marie, Homblé, Fabrice
Zdroj:	Biochemical Journal. 352:183-190
Informácie o vydavateľovi:	Portland Press Ltd., 2000.
Rok vydania:	2000
Predmety:	0301 basic medicine, Time Factors, Protein Conformation, Sequence Homology, Phosphotransferases -- chemistry, Cell Membrane -- metabolism, Medicinal, Protein Isoforms, Magnesium, Membrane Proteins -- metabolism, Phosphorylation, Plant Proteins, 0303 health sciences, Cross-Linking Reagents -- pharmacology, Blotting, Temperature, Fabaceae, Sciences bio-médicales et agricoles, Plants, Hydrogen-Ion Concentration, Plant Proteins -- metabolism, Amino Acid, Cross-Linking Reagents, Membrane Proteins -- chemistry, Electrophoresis, Polyacrylamide Gel, Drug, Western, Sequence Analysis, Plant Proteins -- chemistry, Protein Binding, Electrophoresis, Magnesium -- metabolism, Blotting, Western, Molecular Sequence Data, Aquaporins -- chemistry, Aquaporins, Protein Kinases -- chemistry, Dose-Response Relationship, 03 medical and health sciences, Fabaceae -- chemistry, Amino Acid Sequence, Ions, Polyacrylamide Gel, Plants, Medicinal, Dose-Response Relationship, Drug, Protein, Cell Membrane, Phosphotransferases, Membrane Proteins, Calcium -- metabolism, Autoradiography, Calcium
Popis:	In plants, aquaporins regulate the water flow through membranes during growth, development and stress responses. We have isolated two isoforms of the aquaporin family from the protein-storage vacuoles of lentil (Lens culinaris Med.) seeds. Chemical cross-linking experiments showed that both isoforms belong to the same oligomer in the membrane and are phosphorylated by a membrane-bound protein kinase. We assigned the kinase activity to a 52kDa protein that is magnesium-dependent and calcium-regulated.
Druh dokumentu:	Article
Popis súboru:	1 full-text file(s): application/pdf
Jazyk:	English
ISSN:	1470-8728 0264-6021
DOI:	10.1042/bj3520183
Prístupová URL adresa:	https://europepmc.org/articles/pmc1221445?pdf=render https://pubmed.ncbi.nlm.nih.gov/11062071 https://core.ac.uk/display/8857880 https://www.ncbi.nlm.nih.gov/pubmed/11062071 https://difusion.ulb.ac.be/vufind/Record/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/58319/Details https://www.cabdirect.org/cabdirect/abstract/20003023456 https://portlandpress.com/biochemj/article/352/1/183/38402/Lentil-seed-aquaporins-form-a-hetero-oligomer
Prístupové číslo:	edsair.doi.dedup.....cdf32aeb76b67e1fe8b245f929b8916f
Databáza:	OpenAIRE

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Abstrakt:	In plants, aquaporins regulate the water flow through membranes during growth, development and stress responses. We have isolated two isoforms of the aquaporin family from the protein-storage vacuoles of lentil (Lens culinaris Med.) seeds. Chemical cross-linking experiments showed that both isoforms belong to the same oligomer in the membrane and are phosphorylated by a membrane-bound protein kinase. We assigned the kinase activity to a 52kDa protein that is magnesium-dependent and calcium-regulated.
ISSN:	14708728 02646021
DOI:	10.1042/bj3520183