ArticleBiochimica et biophysica acta2008
Structural model of a complex between the heterotrimeric G protein, Gsalpha, and tubulin.
Article in Biochimica et biophysica acta, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 34 citations in OpenAlex.
- GαFrontiers in pharmacology · 2022Review
- Membrane-Associated α-Tubulin Is Less Acetylated in Postmortem Prefrontal Cortex from Depressed Subjects Relative to Controls: Cytoskeletal Dynamics, HDAC6, and Depression.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2020Article
- Disruption of lipid-raft localized GαNeuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2018Article
- Article
- Neurodegeneration and microtubule dynamics: death by a thousand cuts.Frontiers in cellular neuroscience · 2015Review
- Tubulin, actin and heterotrimeric G proteins: coordination of signaling and structure.Biochimica et biophysica acta · 2014Review
- Non-canonical signaling and localizations of heterotrimeric G proteins.Cellular signalling · 2012Review
- A molecular and structural mechanism for G protein-mediated microtubule destabilization.The Journal of biological chemistry · 2011Article
- Caveolin-1 and lipid microdomains regulate Gs trafficking and attenuate Gs/adenylyl cyclase signaling.Molecular pharmacology · 2009Article
- Cytosolic G{alpha}s acts as an intracellular messenger to increase microtubule dynamics and promote neurite outgrowth.The Journal of biological chemistry · 2009Article
- Heterotrimeric G-proteins interact directly with cytoskeletal components to modify microtubule-dependent cellular processes.Neuro-Signals · 2009Review
- The GTPase domain of Galphao contributes to the functional interaction of Galphao with the promyelocytic leukemia zinc finger protein.Cellular & molecular biology letters · 2009Article
- Submembraneous microtubule cytoskeleton: regulation of microtubule assembly by heterotrimeric Gproteins.The FEBS journal · 2008Review
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
A number of studies have demonstrated interplay between the cytoskeleton and G protein signaling. Many of these studies have determined a specific interaction between tubulin, the building block of microtubules, and G proteins. The alpha subunits of some heterotrimeric G proteins, including Gsalpha, have been shown to interact strongly with tubulin. Binding of Galpha to tubulin results in increased dynamicity of microtubules due to activation of GTPase of tubulin. Tubulin also activates Gsalpha via a direct transfer of GTP between these molecules. Structural insight into the interaction between tubulin and Gsalpha was required, and was determined, in this report, through biochemical and molecular docking techniques. Solid phase peptide arrays suggested that a portion of the amino terminus, alpha2-beta4 (the region between switch II and switch III) and alpha3-beta5 (just distal to the switch III region) domains of Gsalpha are important for interaction with tubulin. Molecular docking studies revealed the best-fit models based on the biochemical data, showing an interface between the two molecules that includes the adenylyl cyclase/Gbetagamma interaction regions of Gsalpha and the exchangeable nucleotide-binding site of tubulin. These structural models explain the ability of tubulin to facilitate GTP exchange on Galpha and the ability of Galpha to activate tubulin GTPase.
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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.