Structural Analysis of the Protein Phosphatase 1 Docking Motif: Molecular Description of Binding Specificities Identifies Interacting Proteins
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TLDR
Structural elements that mediate the binding specificity of PP1 interacting proteins are determined, and a refined consensus sequence for high-affinity PP1 ligands is proposed, and this pattern is predicted and experimentally confirmed several previously unknown PP1 interactors.About:
This article is published in Chemistry & Biology.The article was published on 2006-01-01 and is currently open access. It has received 112 citations till now. The article focuses on the topics: Docking (molecular) & Binding site.read more
Citations
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Serine/Threonine Phosphatases: Mechanism through Structure
TL;DR: Biochemical and structural investigations that advance the mechanistic understanding of the three major classes of PSPs are discussed, with a focus on PP2A.
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The extended PP1 toolkit: designed to create specificity
TL;DR: Novel insights offer perspectives for the therapeutic targeting of PP1 by interfering with the binding of PIPs or substrates.
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The ULK1 complex: Sensing nutrient signals for autophagy activation
TL;DR: The Atg1/ULK1 complex plays a central role in starvation-induced autophagy, integrating signals from upstream sensors such as MTOR and AMPK and transducing them to the downstreamautophagy pathway, and examples of potential ULK1-independent autophapy have emerged, indicating that under certain specific contexts, the ULK 1 complex might be dispensable for autophagic activation.
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Emerging roles of nuclear protein phosphatases
TL;DR: Recent findings that define the role of nuclear protein phosphatases in controlling transforming growth factor-β and bone-morphogenetic protein (BMP) signalling, the DNA-damage response, RNA processing, cell-cycle progression and gene transcription are discussed.
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Docking Motif-Guided Mapping of the Interactome of Protein Phosphatase-1
Annick Hendrickx,Monique Beullens,Hugo Ceulemans,Tom Den Abt,Aleyde Van Eynde,Emilia Nicolaescu,Bart Lesage,Mathieu Bollen +7 more
TL;DR: A global analysis of the validated RVxf-based PP1 interactome provided insights into the conserved features of the RVxF motif but also led to the discovery of additional common PP1 binding elements, described as the "SILK" and "MyPhoNE" motifs that contribute to the design of PP1 interaction networks.
References
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