ArticleThe Journal of biological chemistry2013
Protein kinase A-dependent phosphorylation of Rap1 regulates its membrane localization and cell migration.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 60 citations in OpenAlex.
- A negative feedback loop between small GTPase Rap1 and mammalian tumor suppressor homologue KrsB regulates cell-substrate adhesion inMolecular biology of the cell · 2025Article
- Review
- From disorder comes function: Regulation of small GTPase function by intrinsically disordered lipidated membrane anchor.Current opinion in structural biology · 2024Review
- Differential Lipid Binding Specificities of RAP1A and RAP1B are Encoded by the Amino Acid Sequence of the Membrane Anchors.Journal of the American Chemical Society · 2024Article
- CRISPR/Cas9 mediated Y-chromosome elimination affects human cells transcriptome.Cell & bioscience · 2024Article
- Deciphering transcriptome patterns in porcine mesenchymal stem cells promoting phenotypic maintenance and differentiation by key driver genes.Frontiers in cell and developmental biology · 2024Article
- Signalling of Adrenoceptors: Canonical Pathways and New Paradigms.Handbook of experimental pharmacology · 2024Review
- CAP1 (cyclase-associated protein 1) mediates the cyclic AMP signals that activate Rap1 in stimulating matrix adhesion of colon cancer cells.Cellular signalling · 2023Article
- Host Cell Rap1b mediates cAMP-dependent invasion by Trypanosoma cruzi.PLoS neglected tropical diseases · 2023Article
- Phostensin enables lymphocyte integrin activation and population of peripheral lymphoid organs.The Journal of experimental medicine · 2022Article
- Avian Hepatitis E Virus ORF2 Protein Interacts with Rap1b to Induce Cytoskeleton Rearrangement That Facilitates Virus Internalization.Microbiology spectrum · 2022Article
- PP2Acα promotes macrophage accumulation and activation to exacerbate tubular cell death and kidney fibrosis through activating Rap1 and TNFα production.Cell death and differentiation · 2021Article
- Temporal pattern and synergy influence activity of ERK signaling pathways during L-LTP induction.eLife · 2021Article
- Review
- Review
- Akt3 induces oxidative stress and DNA damage by activating the NADPH oxidase via phosphorylation of p47Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Protein kinase A inhibitor proteins (PKIs) divert GPCR-Gαs-cAMP signaling toward EPAC and ERK activation and are involved in tumor growth.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020Article
- Myelin-associated glycoprotein inhibits neurite outgrowth through inactivation of the small GTPase Rap1.FEBS letters · 2020Article
- The road to ERK activation: Do neurons take alternate routes?Cellular signalling · 2020Review
- NOX2-Derived Reactive Oxygen Species in Cancer.Oxidative medicine and cellular longevity · 2020Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
The small G protein Rap1 can mediate "inside-out signaling" by recruiting effectors to the plasma membrane that signal to pathways involved in cell adhesion and cell migration. This action relies on the membrane association of Rap1, which is dictated by post-translational prenylation as well as by a stretch of basic residues within its carboxyl terminus. One feature of this stretch of acidic residues is that it lies adjacent to a functional phosphorylation site for the cAMP-dependent protein kinase PKA. This phosphorylation has two effects on Rap1 action. One, it decreases the level of Rap1 activity as measured by GTP loading and the coupling of Rap1 to RapL, a Rap1 effector that couples Rap1 GTP loading to integrin activation. Two, it destabilizes the membrane localization of Rap1, promoting its translocation into the cytoplasm. These two actions, decreased GTP loading and decreased membrane localization, are related, as the translocation of Rap1-GTP into the cytoplasm is associated with its increased GTP hydrolysis and inactivation. The consequences of this phosphorylation in Rap1-dependent cell adhesion and cell migration were also examined. Active Rap1 mutants that lack this phosphorylation site had a minimal effect on cell adhesion but strongly reduced cell migration, when compared with an active Rap1 mutant that retained the phosphorylation site. This suggests that optimal cell migration is associated with cycles of Rap1 activation, membrane egress, and inactivation, and requires the regulated phosphorylation of Rap1 by PKA.
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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.