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Scansite 2.0: proteome-wide prediction of cell signaling interactions using short sequence motifs
TLDR
Scansite identifies short protein sequence motifs that are recognized by modular signaling domains, phosphorylated by protein Ser/Thr- or Tyr-kinases or mediate specific interactions with protein or phospholipid ligands, allowing segments of biological pathways to be constructed in silico. Expand
MDC1 Directly Binds Phosphorylated Histone H2AX to Regulate Cellular Responses to DNA Double-Strand Breaks
TLDR
It is shown that MDC1/NFBD1-gammaH2AX complex formation regulates H2AX phosphorylation and is required for normal radioresistance and efficient accumulation of DNA-damage-response proteins on damaged chromatin. Expand
RNF8 Transduces the DNA-Damage Signal via Histone Ubiquitylation and Checkpoint Protein Assembly
TLDR
This study implicates RNF8 as a novel DNA-damage-responsive protein that integrates protein phosphorylation and ubiquitylation signaling and plays a critical role in the cellular response to genotoxic stress. Expand
The Structural Basis for 14-3-3:Phosphopeptide Binding Specificity
TLDR
It is shown that the 14-3-3 dimer binds tightly to single molecules containing tandem repeats of phosphoserine motifs, implicating bidentate association as a signaling mechanism with molecules such as Raf, BAD, and Cbl. Expand
Proteomic Screen Finds pSer/pThr-Binding Domain Localizing Plk1 to Mitotic Substrates
TLDR
This finding reveals how Plk1 can localize to specific sites within cells in response to Cdk phosphorylation at those sites and provides a structural mechanism for targeting the PlK1 kinase domain to its substrates. Expand
Polo-like kinase-1 is activated by aurora A to promote checkpoint recovery
TLDR
It is demonstrated that the initial activation of PLK1 is a primary function of aurora A, and that Bora/aurora-A-dependent phosphorylation is a prerequisite for PLK 1 to promote mitotic entry after a checkpoint-dependent arrest. Expand
The Molecular Basis for Phosphodependent Substrate Targeting and Regulation of Plks by the Polo-Box Domain
TLDR
Mutations that specifically disrupt phosphodependent interactions abolish cell-cycle-dependent localization and provide compelling phenotypic evidence that PBD-phospholigand binding is necessary for proper mitotic progression. Expand
TAZ, a Transcriptional Modulator of Mesenchymal Stem Cell Differentiation
TLDR
It is reported that a 14-3-3–binding protein, TAZ (transcriptional coactivator with PDZ-binding motif), coactivates Runx2- dependent gene transcription while repressing PPARγ-dependent gene transcription, indicating that TAZ functions as a molecular rheostat that modulates MSC differentiation. Expand
TAZ: a novel transcriptional co‐activator regulated by interactions with 14‐3‐3 and PDZ domain proteins
TLDR
TAZ may link events at the plasma membrane and cytoskeleton to nuclear transcription in a manner that can be regulated by 14‐3‐3, and is identified as a novel transcriptional co‐activator with PDZ‐binding motif. Expand
The mTOR-Regulated Phosphoproteome Reveals a Mechanism of mTORC1-Mediated Inhibition of Growth Factor Signaling
TLDR
It is found that the phosphorylation response to insulin is largely mTOR dependent and that mTOR exhibits a unique preference for proline, hydrophobic, and aromatic residues at the +1 position. Expand
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