Linear motif atlas for phosphorylation-dependent signaling.
|Abstract||Systematic and quantitative analysis of protein phosphorylation is revealing dynamic regulatory networks underlying cellular responses to environmental cues. However, matching these sites to the kinases that phosphorylate them and the phosphorylation-dependent binding domains that may subsequently bind to them remains a challenge. NetPhorest is an atlas of consensus sequence motifs that covers 179 kinases and 104 phosphorylation-dependent binding ... [truncated at 450 characters in length]|
|Author||Miller, Martin Lee; Jensen, Lars Juhl; Diella, Francesca; et al|
|Subject||14-3-3 Proteins Amino Acid Motifs Animals BRCA1 Protein Consensus Sequence Databases, Protein Humans Phosphorylation Phosphotransferases Phosphotyrosine Protein Binding Signal Transduction src Homology Domains chemistry chemistry chemistry metabolism|
Out of the box binding determines specificity of SH2 domain interaction.
|Abstract||SH2 domains are phosphotyrosine specific interaction modules with largely overlapping sequence specificities. A recent structure by Bae et al. revealed that SH2 domain specificity can be mediated by secondary binding sites located outside the phosphotyrosine binding pocket.|
|Author||Müller, Susanne; Knapp, Stefan;|
|Subject||Binding Sites Mutation Phosphotyrosine Protein Binding Signal Transduction src Homology Domains genetics chemistry genetics metabolism|
SH2 domains: modulators of nonreceptor tyrosine kinase activity.
|Abstract||The Src homology 2 (SH2) domain is a sequence-specific phosphotyrosine-binding module present in many signaling molecules. In cytoplasmic tyrosine kinases, the SH2 domain is located N-terminally to the catalytic kinase domain (SH1) where it mediates cellular localization, substrate recruitment, and regulation of kinase activity. Initially, structural studies established a role of the SH2 domain stabilizing the inactive state of Src family members ... [truncated at 450 characters in length]|
|Author||Filippakopoulos, Panagis; Müller, Susanne; Knapp, Stefan;|
|Subject||Disease Enzyme Activation Enzyme Stability Humans Mutation Protein-Tyrosine Kinases src Homology Domains genetics chemistry genetics metabolism|
Structural basis for c-KIT inhibition by the suppressor of cytokine signaling 6 (SOCS6) ubiquitin ligase.
|Abstract||The c-KIT receptor tyrosine kinase mediates the cellular response to stem cell factor (SCF). Whereas c-KIT activity is important for the proliferation of hematopoietic cells, melanocytes and germ cells, uncontrolled c-KIT activity contributes to the growth of diverse human tumors. Suppressor of cytokine signaling 6 (SOCS6) is a member of the SOCS family of E3 ubiquitin ligases that can interact with c-KIT and suppress c-KIT-dependent pathways. He ... [truncated at 450 characters in length]|
|Author||Zadjali, Fahad; Pike, Ashley C W; Vesterlund, Mattias; et al|
|Subject||Amino Acid Sequence HEK293 Cells Humans Models, Molecular Molecular Sequence Data Phosphopeptides Protein Tyrosine Phosphatase, Non-Receptor Type 11 Proto-Oncogene Proteins c-kit Signal Transduction Stem Cell Factor Substrate Specificity Suppressor of Cytokine Signaling Proteins Ubiquitination src Homology Domains metabolism chemistry metabolism antagonists and inhibitors metabolism metabolism chemistry metabolism|