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231224s2017 xx |||||o 00| ||eng c |
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|a 10.1093/jxb/erx054
|2 doi
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|a pubmed24n0901.xml
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|a (DE-627)NLM270578625
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|a (NLM)28369656
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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|a Godínez-Palma, Silvia K
|e verfasserin
|4 aut
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|a Two maize Kip-related proteins differentially interact with, inhibit and are phosphorylated by cyclin D-cyclin-dependent kinase complexes
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|c 2017
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
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|2 rdamedia
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|a ƒa Online-Ressource
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|2 rdacarrier
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|a Date Completed 18.07.2018
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|a Date Revised 13.11.2018
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|a published: Print
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|a Citation Status MEDLINE
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|a © The Author 2017. Published by Oxford University Press on behalf of the Society for Experimental Biology.
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|a The family of maize Kip-related proteins (KRPs) has been studied and a nomenclature based on the relationship to rice KRP genes is proposed. Expression studies of KRP genes indicate that all are expressed at 24 h of seed germination but expression is differential in the different tissues of maize plantlets. Recombinant KRP1;1 and KRP4;2 proteins, members of different KRP classes, were used to study association to and inhibitory activity on different maize cyclin D (CycD)-cyclin-dependent kinase (CDK) complexes. Kinase activity in CycD2;2-CDK, CycD4;2-CDK, and CycD5;3-CDK complexes was inhibited by both KRPs; however, only KRP1;1 inhibited activity in the CycD6;1-CDK complex, not KRP4;2. Whereas KRP1;1 associated with either CycD2;2 or CycD6;1, and to cyclin-dependent kinase A (CDKA) recombinant proteins, forming ternary complexes, KRP4;2 bound CDKA and CycD2;2 but did not bind CycD6;1, establishing a differential association capacity. All CycD-CDK complexes included here phosphorylated both the retinoblastoma-related (RBR) protein and the two KRPs; interestingly, while KRP4;2 phosphorylated by the CycD2;2-CDK complex increased its inhibitory capacity, when phosphorylated by the CycD6;1-CDK complex the inhibitory capacity was reduced or eliminated. Evidence suggests that the phosphorylated residues in KRP4;2 may be different for every kinase, and this would influence its performance as a cyclin-CDK inhibitor
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a CDKs
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|a ICK/KRPs
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|a KRP phosphorylation
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|a Zea mays.
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|a cyclins D
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|a kinase inhibition
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|a Cyclin D
|2 NLM
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|a Cyclin-Dependent Kinase Inhibitor Proteins
|2 NLM
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|a Plant Proteins
|2 NLM
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|a Cyclin-Dependent Kinases
|2 NLM
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| 650 |
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|a EC 2.7.11.22
|2 NLM
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| 700 |
1 |
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|a Rosas-Bringas, Fernando R
|e verfasserin
|4 aut
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|a Rosas-Bringas, Omar G
|e verfasserin
|4 aut
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| 700 |
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|a García-Ramírez, Elpidio
|e verfasserin
|4 aut
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| 700 |
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|a Zamora-Zaragoza, Jorge
|e verfasserin
|4 aut
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| 700 |
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|a Vázquez-Ramos, Jorge M
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Journal of experimental botany
|d 1985
|g 68(2017), 7 vom: 01. März, Seite 1585-1597
|w (DE-627)NLM098182706
|x 1460-2431
|7 nnns
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| 773 |
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|g volume:68
|g year:2017
|g number:7
|g day:01
|g month:03
|g pages:1585-1597
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|u http://dx.doi.org/10.1093/jxb/erx054
|3 Volltext
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|d 68
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|h 1585-1597
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