ArticleThe Journal of biological chemistry2012
Phosphorylation by protein kinase Cα regulates RalB small GTPase protein activation, subcellular localization, and effector utilization.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
20 citing papers in PubMed, 36 citations in OpenAlex.
- Article
- RalB uncoupling from exocyst is required for endothelial Weibel-Palade body exocytosis.Molecular biology of the cell · 2025Article
- Article
- FAM3C in circulating tumor-derived extracellular vesicles promotes non-small cell lung cancer growth in secondary sites.Theranostics · 2023Article
- Review
- Article
- PHLPPing the balance: restoration of protein kinase C in cancer.The Biochemical journal · 2021Review
- Superoxide increases surface NKCC2 in the rat thick ascending limbs via PKC.American journal of physiology. Renal physiology · 2019Article
- Localization of RalB signaling at endomembrane compartments and its modulation by autophagy.Scientific reports · 2019Article
- RAL GTPases: Biology and Potential as Therapeutic Targets in Cancer.Pharmacological reviews · 2018Review
- Ral A, via activating the mitotic checkpoint, sensitizes cells lacking a functional Nf1 to apoptosis in the absence of protein kinase C.Oncotarget · 2016Article
- Ral-Arf6 crosstalk regulates Ral dependent exocyst trafficking and anchorage independent growth signalling.Cellular signalling · 2016Article
- Inhibition of Ral GTPases Using a Stapled Peptide Approach.The Journal of biological chemistry · 2016Article
- Divergent roles of CAAX motif-signaled posttranslational modifications in the regulation and subcellular localization of Ral GTPases.The Journal of biological chemistry · 2015Article
- Drugging the Ral GTPase.Small GTPases · 2015Article
- Ral small GTPase signaling and oncogenesis: More than just 15minutes of fame.Biochimica et biophysica acta · 2014Review
- Ral GTPase down-regulation stabilizes and reactivates p53 to inhibit malignant transformation.The Journal of biological chemistry · 2014Article
- Drugging the undruggable RAS: Mission possible?Nature reviews. Drug discovery · 2014Review
- Ral and Rheb GTPase activating proteins integrate mTOR and GTPase signaling in aging, autophagy, and tumor cell invasion.Molecular cell · 2014Article
- RabGAP22 is required for defense to the vascular pathogen Verticillium longisporum and contributes to stomata immunity.PloS one · 2014Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Ras-like (Ral) small GTPases are regulated downstream of Ras and the noncanonical Ral guanine nucleotide exchange factor (RalGEF) effector pathway. Despite RalA and RalB sharing 82% sequence identity and utilization of shared effector proteins, their roles in normal and neoplastic cell growth have been shown to be highly distinct. Here, we determined that RalB function is regulated by protein kinase Cα (PKCα) phosphorylation. We found that RalB phosphorylation on Ser-198 in the C-terminal membrane targeting sequence resulted in enhanced RalB endomembrane accumulation and decreased RalB association with its effector, the exocyst component Sec5. Additionally, RalB phosphorylation regulated vesicular trafficking and membrane fusion by regulating v- and t-SNARE interactions. RalB phosphorylation regulated vesicular traffic of α5-integrin to the cell surface and cell attachment to fibronectin. In summary, our data suggest that phosphorylation by PKCα is critical for RalB-mediated vesicle trafficking and exocytosis.
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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.