Arabidopsis Yak1 protein (AtYak1) is a dual specificity protein kinase

Handle URI:
http://hdl.handle.net/10754/579844
Title:
Arabidopsis Yak1 protein (AtYak1) is a dual specificity protein kinase
Authors:
Kim, Dongjin ( 0000-0003-4175-9817 ) ; Ntui, Valentine Otang; Zhang, Nianshu; Xiong, Liming ( 0000-0001-8099-0806 )
Abstract:
Yak1 is a member of dual-specificity Tyr phosphorylation-regulated kinases (DYRKs) that are evolutionarily conserved. The downstream targets of Yak1 and their functions are largely unknown. Here, a homologous protein AtYAK1 was identified in Arabidopsis thaliana and the phosphoprotein profiles of the wild type and an atyak1 mutant were compared on two-dimensional gel following Pro-Q Diamond phosphoprotein gel staining. Annexin1, Annexin2 and RBD were phosphorylated at serine/ threonine residues by the AtYak1 kinase. Annexin1, Annexin2 and Annexin4 were also phosphorylated at tyrosine residues. Our study demonstrated that AtYak1 is a dual specificity protein kinase in Arabidopsis that may regulate the phosphorylation status of the annexin family proteins.
KAUST Department:
Biological and Environmental Sciences and Engineering (BESE) Division; Center for Desert Agriculture
Citation:
Arabidopsis Yak1 protein (AtYak1) is a dual specificity protein kinase 2015 FEBS Letters
Publisher:
Wiley-Blackwell
Journal:
FEBS Letters
Issue Date:
9-Oct-2015
DOI:
10.1016/j.febslet.2015.09.025
Type:
Article
ISSN:
00145793
Additional Links:
http://linkinghub.elsevier.com/retrieve/pii/S0014579315008741
Appears in Collections:
Articles; Center for Desert Agriculture; Biological and Environmental Sciences and Engineering (BESE) Division

Full metadata record

DC FieldValue Language
dc.contributor.authorKim, Dongjinen
dc.contributor.authorNtui, Valentine Otangen
dc.contributor.authorZhang, Nianshuen
dc.contributor.authorXiong, Limingen
dc.date.accessioned2015-10-18T14:43:39Zen
dc.date.available2015-10-18T14:43:39Zen
dc.date.issued2015-10-09en
dc.identifier.citationArabidopsis Yak1 protein (AtYak1) is a dual specificity protein kinase 2015 FEBS Lettersen
dc.identifier.issn00145793en
dc.identifier.doi10.1016/j.febslet.2015.09.025en
dc.identifier.urihttp://hdl.handle.net/10754/579844en
dc.description.abstractYak1 is a member of dual-specificity Tyr phosphorylation-regulated kinases (DYRKs) that are evolutionarily conserved. The downstream targets of Yak1 and their functions are largely unknown. Here, a homologous protein AtYAK1 was identified in Arabidopsis thaliana and the phosphoprotein profiles of the wild type and an atyak1 mutant were compared on two-dimensional gel following Pro-Q Diamond phosphoprotein gel staining. Annexin1, Annexin2 and RBD were phosphorylated at serine/ threonine residues by the AtYak1 kinase. Annexin1, Annexin2 and Annexin4 were also phosphorylated at tyrosine residues. Our study demonstrated that AtYak1 is a dual specificity protein kinase in Arabidopsis that may regulate the phosphorylation status of the annexin family proteins.en
dc.language.isoenen
dc.publisherWiley-Blackwellen
dc.relation.urlhttp://linkinghub.elsevier.com/retrieve/pii/S0014579315008741en
dc.rightsNOTICE: this is the author’s version of a work that was accepted for publication in FEBS Letters. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in FEBS Letters, 9 October 2015. DOI: 10.1016/j.febslet.2015.09.025en
dc.subjectSerine / Threonine protein kinaseen
dc.subjectTyrosine protein kinaseen
dc.subjectDual specificity protein kinaseen
dc.subjectPhosphorylationen
dc.subjectPhosphopeptideen
dc.titleArabidopsis Yak1 protein (AtYak1) is a dual specificity protein kinaseen
dc.typeArticleen
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Divisionen
dc.contributor.departmentCenter for Desert Agricultureen
dc.identifier.journalFEBS Lettersen
dc.eprint.versionPost-printen
dc.contributor.institutionCambridge Systems Biology Centre, Department of Biochemistry, The Sanger Building, Tennis Court Road, Cambridge CB2 1GA, UKen
dc.contributor.affiliationKing Abdullah University of Science and Technology (KAUST)en
kaust.authorKim, Dongjinen
kaust.authorKim, Dongjinen
kaust.authorNtui, Valentine Otangen
kaust.authorNtui, Valentine Otangen
kaust.authorXiong, Limingen
All Items in KAUST are protected by copyright, with all rights reserved, unless otherwise indicated.