ReviewOncogene2001
Regulation of G proteins by covalent modification.
Review in Oncogene, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
70 citing papers in PubMed, 191 citations in OpenAlex.
- Long-Chain S-Acylation Is a Key Modulator During the Macrophage Inflammatory Response.Molecular & cellular proteomics : MCP · 2026Article
- Proteins required for stereocilia elongation during mammalian hair cell development ensure precise and steady heights during adult life.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Thermodynamic bounds on ultrasensitivity in covalent switching.Biophysical journal · 2023Article
- Phenotypic Diversity in GNAO1 Patients: A Comprehensive Overview of Variants and Phenotypes.Human mutation · 2023Review
- Mechanistic Understanding of the Palmitoylation of GPharmaceutics · 2022Article
- G protein-coupled receptor signaling: transducers and effectors.American journal of physiology. Cell physiology · 2022Review
- Local and substrate-specific S-palmitoylation determines subcellular localization of Gαo.Nature communications · 2022Article
- Gαi protein subunit: A step toward understanding its non-canonical mechanisms.Frontiers in cell and developmental biology · 2022Review
- Pediatric Encephalopathy: Clinical, Biochemical and Cellular Insights into the Role of Gln52 ofCells · 2021Article
- Fusion with Promiscuous GαInternational journal of molecular sciences · 2021Article
- Protein N-myristoylation: functions and mechanisms in control of innate immunity.Cellular & molecular immunology · 2021Review
- The Gαi protein subclass selectivity to the dopamine DCell communication and signaling : CCS · 2020Article
- Negative feedback-loop mechanisms regulating HOG- and pheromone-MAPK signaling in yeast.Current genetics · 2020Review
- Protein expression of prenyltransferase subunits in postmortem schizophrenia dorsolateral prefrontal cortex.Translational psychiatry · 2020Article
- Article
- Lipid Modifications in Cilia Biology.Journal of clinical medicine · 2019Review
- Deletion of the α subunit of the heterotrimeric Go protein impairs cerebellar cortical development in mice.Molecular brain · 2019Article
- Statins Perturb GMolecular pharmacology · 2019Article
- G protein subunit phosphorylation as a regulatory mechanism in heterotrimeric G protein signaling in mammals, yeast, and plants.The Biochemical journal · 2018Review
- Regulators of G protein signaling in cardiovascular function during pregnancy.Physiological genomics · 2018Review
10 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Heterotrimeric G protein alpha,beta, and gamma subunits are subject to several kinds of co- and post-translational covalent modifications. Among those relevant to G protein-coupled receptor signaling in normal cell function are lipid modifications and phosphorylation. N-myristoylation is a co-translational modification occurring for members of the G(i) family of Galpha subunits, while palmitoylation is a post-translational modification that occurs for these and most other Galpha subunits. One or both modifications are required for plasma membrane targeting and contribute to regulating strength of interaction with the Gbetagamma heterodimer, effectors, and regulators of G protein signaling (RGS proteins). Galpha subunits, including those with transforming activity, are often inactive when unable to be modified with lipids. The reversible nature of palmitoylation is intriguing in this regard, as it lends itself to a regulation integrated with the activation state of the G protein. Several Galpha subunits are substrates for phosphorylation by protein kinase C and at least one is a substrate for phosphorylation by the p21-activated protein kinase. Phosphorylation in both instances inhibits the interactions of these subunits with the Gbetagamma heterodimer and RGS proteins. Several Galpha subunits are also substrates for tyrosine phosphorylation. A Ggamma subunit is phosphorylated by protein kinase C, with the consequence that it interacts more tightly with a Galpha subunit but less well with an effector.
Indexed as
Identifiers
What OpenQuestion holds
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.