Two maize Kip-related proteins differentially interact with, inhibit and are phosphorylated by cyclin D–cyclin-dependent kinase complexes
| Autor: | Silvia K. Godínez-Palma, Elpidio García-Ramírez, Omar G. Rosas-Bringas, Jorge Zamora-Zaragoza, Fernando R. Rosas-Bringas, Jorge M. Vázquez-Ramos |
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| Rok vydání: | 2017 |
| Předmět: |
0106 biological sciences
0301 basic medicine CDKs Physiology Cyclin D Plant Developmental Biology Plant Science Zea mays 01 natural sciences law.invention Cyclins D 03 medical and health sciences Gene Expression Regulation Plant Cyclin-dependent kinase law Phosphorylation Kinase activity Kinase inhibition Cyclin-Dependent Kinase Inhibitor Proteins Plant Proteins biology Kinase KRP phosphorylation food and beverages ICK/KRPs Cyclin-Dependent Kinases 030104 developmental biology Biochemistry biology.protein Cyclin-dependent kinase complex Recombinant DNA Research Paper 010606 plant biology & botany Cyclin-dependent kinase inhibitor protein |
| Zdroj: | Journal of Experimental Botany, 68(7), 1585-1597 Journal of Experimental Botany 68 (2017) 7 Journal of Experimental Botany |
| ISSN: | 1460-2431 0022-0957 |
| DOI: | 10.1093/jxb/erx054 |
| Popis: | Highlight Maize Kip-related proteins can be differentially phosphorylated by different cyclin D–cyclin-dependent kinase complexes and this influences their performance as cyclin-dependent kinase inhibitors. 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. |
| Databáze: | OpenAIRE |
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