Reading protein modifications with interaction domains

By B. Seet, Ivan Dikic, Ming‐Ming Zhou, Tony Pawson. Nature reviews. Molecular cell biology, 2006

694 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/6be6b00447c8adc7fe431bf0f857d32235f5a9d5

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Citations in the corpus

Bub3 reads phosphorylated MELT repeats to promote spindle assembly checkpoint signaling (2013, background): “member of a family of protein domains involved in the recognition of phosphorylated sequence motifs, which includes, among others, the SH2, PTB, BRCT, FHA and polo-box domains (Seet et al., 2006; Pawson and Kofler, 2009).”
HATs and HDACs: from structure, function and regulation to novel strategies for therapy and prevention (2007, background): “In addition, chromodomains, plant homeodomain-linked (PHD) fingers and other modification-specific modules are present in HAT and HDAC complexes (reviewed in Seet et al., 2006; Kouzarides, 2007; Lee and Workman, 2007).”
The age of crosstalk: phosphorylation, ubiquitination, and beyond. (2007, background): “Phosphobinding domains of several types are known, with some specific for pSer/pThr (e.g., FHA, BRCT, and 14-3-3) and others for pTyr (e.g., SH2 and PTB) ( Seet et al., 2006 ).”
The Roles of Post-translational Modifications in the Context of Protein Interaction Networks (2015, background): “As many PTMs modulate the binding affinities between proteins by changing the electrostatic or structural properties of the involved interaction sites [29], PTMs and protein-protein interactions are frequently functionally connected.”
Conserved function of RNF4 family proteins in eukaryotes: targeting a ubiquitin ligase to SUMOylated proteins (2007, background): “Many ubiquitin E3 ligases exist with targeting motifs that recognize post-translational modifications (Seet et al, 2006), for example, the SH2 domain in cCbl for phosphorylated tyrosine (Joazeiro et al, 1999), and the Fbx2 subunit in an SCF complex for N-linked glycosylation (Yoshida et al, 2002).”
Decoding signalling networks by mass spectrometry-based proteomics (2010, background): “These phosphorylation events can create docking sites for the recruitment of downstream signalling effectors, which contain specific modification interaction domains, such as SH2 domains and PTB domains , which recognize phosphorylated Tyr residues in specific sequence context”
How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers (2007, background): “The emerging effector-mediated paradigm posits that histone PTMs are 'read' by protein modules termed effectors, facilitating meaningful downstream events via the recruitment or stabilization of module-associated chromatin-templated machiner”
Systematic discovery of in vivo phosphorylation networks. (2007, background): “These, in turn, can modify protein function by inducing conformational changes or by creating binding sites for protein interaction domains (for example, SH2 or BRCT) that selectively recognize phosphorylated linear motifs ( Seet et al., 2006 ).”
The role of chromatin during transcription. (2007, background): “Second, it is well accepted that protein modifications can be recognized by other proteins (reviewed in Seet et al., 2006).”
Early steps in the DNA base excision/single-strand interruption repair pathway in mammalian cells (2008, neutral): “[177].”