Pin1 acts as a negative regulator of the G2/M transition by interacting with the Aurora-A–Bora complex
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Summary
The results found that Aurora A can interact with and phosphorylate Pin1 at Ser16, which suppresses the G2/M function of Pin1 by disrupting its binding ability and mitotic entry, and shows that phosphorylation of Bora at Ser274 and Ser278 is crucial for binding of Pin 1.
- Type
- article
- Published
- 2013-11-01
- Cited by
- 39
- References
- 35
- OpenAlex
- https://openalex.org/W23970419
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:3189263
Keywords
Humanities, Art
References
- The mitotic serine/threonine kinase Aurora2/AIK is regulated by phosphorylation and degradation
- Mechanisms of p34cdc2 regulation
- Peptidyl-prolyl cis–trans isomerase Pin1 in ageing, cancer and Alzheimer disease
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- Two Mitosis-Specific Antibodies, MPM-2 and Phospho-Histone H3 (Ser28), Allow Rapid and Precise Determination of Mitotic Activity
- Critical Role of WW Domain Phosphorylation in Regulating Phosphoserine Binding Activity and Pin1 Function*
- The peptidyl-prolyl isomerase Pin1 regulates cytokinesis through Cep55.
- Selective inactivation of parvulin-like peptidyl-prolyl cis/trans isomerases by juglone.
- Mitotic activation of the kinase Aurora-A requires its binding partner Bora.
- The cell cycle: a review of regulation, deregulation and therapeutic targets in cancer
- The prolyl isomerase PIN1: a pivotal new twist in phosphorylation signalling and disease
- Plk1- and β-TrCP–dependent degradation of Bora controls mitotic progression
- Phosphorylation network dynamics in the control of cell cycle transitions
- Requirement of the prolyl isomerase Pin1 for the replication checkpoint.
- Polo-like kinase-1 is activated by aurora A to promote checkpoint recovery
- The mitotic peptidyl‐prolyl isomerase, Pin1, interacts with Cdc25 and Plx1
- The APC/C recruits cyclin B1–Cdk1–Cks in prometaphase before D box recognition to control mitotic exit
- Aurora-A site specificity: a study with synthetic peptide substrates.
- Function of WW domains as phosphoserine- or phosphothreonine-binding modules.
- Bora and the Kinase Aurora A Cooperatively Activate the Kinase Plk1 and Control Mitotic Entry
Cited by
- COT phosphorylates prolyl‐isomerase Pin1 to promote tumorigenesis in breast cancer
- Landscape of Pin1 in the cell cycle
- Pin1: Intimate involvement with the regulatory protein kinase networks in the global phosphorylation landscape.
- Cross-Talk between AURKA and Plk1 in Mitotic Entry and Spindle Assembly
- Pin1, the Master Orchestrator of Bone Cell Differentiation
- The isomerase PIN1 controls numerous cancer-driving pathways and is a unique drug target
- Physiological and Pathogenic Roles of Prolyl Isomerase Pin1 in Metabolic Regulations via Multiple Signal Transduction Pathway Modulations
- Grb7 Protein Stability Modulated by Pin1 in Association with Cell Cycle Progression
- PIN1 in breast development and cancer: a clinical perspective
- Understanding the role of PIN1 in hepatocellular carcinoma
- Dynamic regulation of Pin1 expression and function during zebrafish development
- Metformin disrupts malignant behavior of oral squamous cell carcinoma via a novel signaling involving Late SV40 factor/Aurora-A
- Structure and function of the human parvulins Pin1 and Par14/17
- Multivalent Interactions with Fbw7 and Pin1 Facilitate Recognition of c-Jun by the SCFFbw7 Ubiquitin Ligase.
- Pin1 Modulation in Physiological Status and Neurodegeneration. Any Contribution to the Pathogenesis of Type 3 Diabetes?
- Prolyl isomerase Pin1: a promoter of cancer and a target for therapy
- Gears-In-Motion: The Interplay of WW and PPIase Domains in Pin1
- Development of Pin1 inhibitors and their potential as therapeutic agents.
- A Guide to PIN1 Function and Mutations Across Cancers
- Prolyl isomerization of FAAP20 catalyzed by PIN1 regulates the Fanconi anemia pathway
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