ArticleThe Journal of biological chemistry2009
Phosphorylation-induced conformational changes in Rap1b: allosteric effects on switch domains and effector loop.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 46 citations in OpenAlex.
- EPSD 2.0: An Updated Database of Protein Phosphorylation Sites Across Eukaryotic Species.Genomics, proteomics & bioinformatics · 2025Article
- A Comparison of White and Yellow Seminal Plasma Phosphoproteomes Obtained from Turkey (International journal of molecular sciences · 2024Article
- Host Cell Rap1b mediates cAMP-dependent invasion by Trypanosoma cruzi.PLoS neglected tropical diseases · 2023Article
- Soluble cyclase-mediated nuclear cAMP synthesis is sufficient for cell proliferation.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Serotonin and serotonin reuptake inhibitors alter placental aromatase.The Journal of steroid biochemistry and molecular biology · 2019Article
- Attenuation of amyloid-β generation by atypical protein kinase C-mediated phosphorylation of engulfment adaptor PTB domain containing 1 threonine 35.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
- Volatile anesthetics affect macrophage phagocytosis.PloS one · 2019Article
- Cyclase-associated protein 1 (CAP1) is a prenyl-binding partner of Rap1 GTPase.The Journal of biological chemistry · 2018Article
- Same but not alike: Structure, flexibility and energetics of domains in multi-domain proteins are influenced by the presence of other domains.PLoS computational biology · 2018Article
- Phosphorylation of FE65 at threonine 579 by GSK3β stimulates amyloid precursor protein processing.Scientific reports · 2017Article
- Phosphorylation of Rap1 by cAMP-dependent Protein Kinase (PKA) Creates a Binding Site for KSR to Sustain ERK Activation by cAMP.The Journal of biological chemistry · 2017Article
- Host Epac1 is required for cAMP-mediated invasion by Trypanosoma cruzi.Molecular and biochemical parasitology · 2017Article
- Intrinsic K-Ras dynamics: A novel molecular dynamics data analysis method shows causality between residue pair motions.Scientific reports · 2016Article
- ARD1-mediated Hsp70 acetylation balances stress-induced protein refolding and degradation.Nature communications · 2016Article
- Single-residue posttranslational modification sites at the N-terminus, C-terminus or in-between: To be or not to be exposed for enzyme access.Proteomics · 2015Article
- RASA3 is a critical inhibitor of RAP1-dependent platelet activation.The Journal of clinical investigation · 2015Article
- Article
- CK2 phosphorylation of human centrins 1 and 2 regulates their binding to the DNA repair protein XPC, the centrosomal protein Sfi1 and the phototransduction protein transducin β.FEBS open bio · 2014Article
- Protein kinase A-dependent phosphorylation of Rap1 regulates its membrane localization and cell migration.The Journal of biological chemistry · 2013Article
- Disruption of RAB40AL function leads to Martin--Probst syndrome, a rare X-linked multisystem neurodevelopmental human disorder.Journal of medical genetics · 2012Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
Rap1b has been implicated in the transduction of the cAMP mitogenic response. Agonists that increase intracellular cAMP rapidly activate (i.e. GTP binding) and phosphorylate Rap1b on Ser(179) at its C terminus. cAMP-dependent protein kinase (PKA)-mediated phosphorylation of Rap1b is required for cAMP-dependent mitogenesis, tumorigenesis, and inhibition of AKT activity. However, the role of phosphorylation still remains unknown. In this study, we utilized amide hydrogen/deuterium exchange mass spectroscopy (DXMS) to assess potential conformational changes and/or mobility induced by phosphorylation. We report here DXMS data comparing exchange rates for PKA-phosphorylated (Rap1-P) and S179D phosphomimetic (Rap1-D) Rap1b proteins. Rap1-P and Rap1-D behaved exactly the same, revealing an increased exchange rate in discrete regions along the protein; these regions include a domain around the phosphorylation site and unexpectedly the two switch loops. Thus, local effects induced by Ser(179) phosphorylation communicate allosterically with distal domains involved in effector interaction. These results provide a mechanistic explanation for the differential effects of Rap1 phosphorylation by PKA on effector protein interaction.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.