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dc.contributor.author Mikami, Koji
dc.contributor.author Saavedra, Laura
dc.contributor.author Hiwatashi, Yuji
dc.contributor.author Uji, Toshiki
dc.contributor.author Hasebe, Mitsuyasu
dc.contributor.author Sommarin, Marianne
dc.date.accessioned 2013-09-26T21:44:19Z
dc.date.available 2013-09-26T21:44:19Z
dc.date.issued 2010-07
dc.identifier.citation Mikami , K , Saavedra , L , Hiwatashi , Y , Uji , T , Hasebe , M & Sommarin , M 2010 , ' A dibasic amino acid pair conserved in the activation loop directs plasma membrane localization and is necessary for activity of plant type I/II phosphatidylinositol phosphate kinase ' Plant Physiology , vol 153 , no. 3 , pp. 1004-15 . DOI: 10.1104/pp.109.152686 en
dc.identifier.issn 0032-0889
dc.identifier.other PURE: 3202119
dc.identifier.other PURE UUID: 1763ba6e-851e-492c-9c04-5d503a55e932
dc.identifier.other PubMed: 20427464
dc.identifier.other Scopus: 77954305924
dc.identifier.other PubMedCentral: PMC2899925
dc.identifier.other handle.net: 2160/12176
dc.identifier.uri http://hdl.handle.net/2160/12176
dc.description.abstract Phosphatidylinositol phosphate kinase (PIPK) is an enzyme involved in the regulation of cellular levels of phosphoinositides involved in various physiological processes, such as cytoskeletal organization, ion channel activation, and vesicle trafficking. In animals, research has focused on the modes of activation and function of PIPKs, providing an understanding of the importance of plasma membrane localization. However, it still remains unclear how this issue is regulated in plant PIPKs. Here, we demonstrate that the carboxyl-terminal catalytic domain, which contains the activation loop, is sufficient for plasma membrane localization of PpPIPK1, a type I/II B PIPK from the moss Physcomitrella patens. The importance of the carboxyl-terminal catalytic domain for plasma membrane localization was confirmed with Arabidopsis (Arabidopsis thaliana) AtPIP5K1. Our findings, in which substitution of a conserved dibasic amino acid pair in the activation loop of PpPIPK1 completely prevented plasma membrane targeting and abolished enzymatic activity, demonstrate its critical role in these processes. Placing our results in the context of studies of eukaryotic PIPKs led us to conclude that the function of the dibasic amino acid pair in the activation loop in type I/II PIPKs is plant specific. en
dc.format.extent 12 en
dc.language.iso eng
dc.relation.ispartof Plant Physiology en
dc.rights en
dc.subject Amino Acid Sequence en
dc.subject Amino Acids, Diamino en
dc.subject Animals en
dc.subject Arabidopsis en
dc.subject Bryopsida en
dc.subject Catalytic Domain en
dc.subject Cell Membrane en
dc.subject Conserved Sequence en
dc.subject Enzyme Activation en
dc.subject Molecular Sequence Data en
dc.subject Onions en
dc.subject Phosphatidic Acids en
dc.subject Phosphotransferases (Alcohol Group Acceptor) en
dc.subject Protein Transport en
dc.subject Protoplasts en
dc.subject Structure-Activity Relationship en
dc.subject Subcellular Fractions en
dc.title A dibasic amino acid pair conserved in the activation loop directs plasma membrane localization and is necessary for activity of plant type I/II phosphatidylinositol phosphate kinase en
dc.type /dk/atira/pure/researchoutput/researchoutputtypes/contributiontojournal/article en
dc.identifier.doi https://doi.org/10.1104/pp.109.152686
dc.contributor.institution Department of Biological, Environmental and Rural Sciences en
dc.description.status Peer reviewed en


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