Regulation of the Minichromosome Maintenance Protein 3 (MCM3) Chromatin Binding by the Prolyl Isomerase Pin1
| Autor: | Marat Meleshin, Miroslav Malesevic, Michael Schumann, Cordelia Schiene-Fischer, Erik Hinze, S. Mathea, Wolfgang Haehnel, Mike Schutkowski |
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| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Proline Protein subunit S Phase WW domain 03 medical and health sciences Minichromosome maintenance Structural Biology Prolyl isomerase Humans Phosphorylation Molecular Biology Binding Sites biology Chemistry Chromatin binding Minichromosome Maintenance Complex Component 3 Helicase Chromatin Cell biology NIMA-Interacting Peptidylprolyl Isomerase 030104 developmental biology Gene Expression Regulation Mutation biology.protein PIN1 HeLa Cells Protein Binding |
| Zdroj: | Journal of Molecular Biology. 430:5169-5181 |
| ISSN: | 0022-2836 |
| DOI: | 10.1016/j.jmb.2018.10.002 |
| Popis: | Human Pin1 is a peptidyl prolyl cis/trans isomerase with a unique preference for phosphorylated Ser/Thr-Pro substrate motifs. Here we report that MCM3 (minichromosome maintenance complex component 3) is a novel target of Pin1. MCM3 interacts directly with the WW domain of Pin1. Proline-directed phosphorylation of MCM3 at S112 and T722 are crucial for the interaction with Pin1. MCM3 as a subunit of the minichromosome maintenance heterocomplex MCM2-7 is part of the pre-replication complex responsible for replication licensing and is implicated in the formation of the replicative helicase during progression of replication. Our data suggest that Pin1 coordinates phosphorylation-dependently MCM3 loading onto chromatin and its unloading from chromatin, thereby mediating S phase control. |
| Databáze: | OpenAIRE |
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