ArticlePloS one2014
Tyrosine phosphorylation within the intrinsically disordered cytosolic domains of the B-cell receptor: an NMR-based structural analysis.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- The pathogen-encoded signalling receptor Tir exploits host-like intrinsic disorder for infection.Communications biology · 2024Article
- Metallic trace elements in marine sponges living in a semi-enclosed tropical lagoon.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2024Article
- Unambiguous Tracking of Protein Phosphorylation by Fast High-Resolution FOSY NMR*.Angewandte Chemie (International ed. in English) · 2021Article
- RUNX2 Phosphorylation by Tyrosine Kinase ABL Promotes Breast Cancer Invasion.Frontiers in oncology · 2021Article
- Biotin proximity tagging favours unfolded proteins and enables the study of intrinsically disordered regions.Communications biology · 2020Article
- Random coil chemical shifts for serine, threonine and tyrosine phosphorylation over a broad pH range.Journal of biomolecular NMR · 2019Article
- Generation of the configurational ensemble of an intrinsically disordered protein from unbiased molecular dynamics simulation.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- The Structural and Functional Diversity of Intrinsically Disordered Regions in Transmembrane Proteins.The Journal of membrane biology · 2019Review
- AMPK and AKT protein kinases hierarchically phosphorylate the N-terminus of the FOXO1 transcription factor, modulating interactions with 14-3-3 proteins.The Journal of biological chemistry · 2019Article
- Review
- The immunobiology of ubiquitin-dependent B cell receptor functions.Molecular immunology · 2018Review
- An efficient combination of BEST and NUS methods in multidimensional NMR spectroscopy for high throughput analysis of proteins.RSC advances · 2018Article
- Functions of intrinsic disorder in transmembrane proteins.Cellular and molecular life sciences : CMLS · 2017Review
- Effect of Phosphorylation on a Human-like Osteopontin Peptide.Biophysical journal · 2017Article
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5 authors.
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Abstract
Intrinsically disordered proteins are found extensively in cell signaling pathways where they often are targets of posttranslational modifications e.g. phosphorylation. Such modifications can sometimes induce or disrupt secondary structure elements present in the modified protein. CD79a and CD79b are membrane-spanning, signal-transducing components of the B-cell receptor. The cytosolic domains of these proteins are intrinsically disordered and each has an immunoreceptor tyrosine-based activation motif (ITAM). When an antigen binds to the receptor, conserved tyrosines located in the ITAMs are phosphorylated which initiate further downstream signaling. Here we use NMR spectroscopy to examine the secondary structure propensity of the cytosolic domains of CD79a and CD79b in vitro before and after phosphorylation. The phosphorylation patterns are identified through analysis of changes of backbone chemical shifts found for the affected tyrosines and neighboring residues. The number of the phosphorylated sites is confirmed by mass spectrometry. The secondary structure propensities are calculated using the method of intrinsic referencing, where the reference random coil chemical shifts are measured for the same protein under denaturing conditions. Our analysis revealed that CD79a and CD79b both have an overall propensity for α-helical structure that is greatest in the C-terminal region of the ITAM. Phosphorylation of CD79a caused a decrease in helical propensity in the C-terminal ITAM region. For CD79b, the opposite was observed and phosphorylation resulted in an increase of helical propensity in the C-terminal part.
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