ArticleThe Journal of biological chemistry2011
A molecular and structural mechanism for G protein-mediated microtubule destabilization.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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
11 citing papers in PubMed, 24 citations in OpenAlex.
- 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
- Activation of microtubule dynamics increases neuronal growth via the nerve growth factor (NGF)- and Gαs-mediated signaling pathways.The Journal of biological chemistry · 2015Article
- The taccalonolides and paclitaxel cause distinct effects on microtubule dynamics and aster formation.Molecular cancer · 2014Article
- Tubulin, actin and heterotrimeric G proteins: coordination of signaling and structure.Biochimica et biophysica acta · 2014Review
- Arborization of dendrites by developing neocortical neurons is dependent on primary cilia and type 3 adenylyl cyclase.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013Article
- Microtubule plus-ends within a mitotic cell are 'moving platforms' with anchoring, signalling and force-coupling roles.Open biology · 2012Review
- 3β-Methoxy-pregnenolone (MAP4343) as an innovative therapeutic approach for depressive disorders.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Non-canonical signaling and localizations of heterotrimeric G proteins.Cellular signalling · 2012Review
- Modeling the effects of drug binding on the dynamic instability of microtubules.Physical biology · 2011Article
- Antibody-DM1 conjugates as cancer therapeutics.Cancer letters · 2011Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
The heterotrimeric, G protein-coupled receptor-associated G protein, Gα(s), binds tubulin with nanomolar affinity and disrupts microtubules in cells and in vitro. Here we determine that the activated form of Gα(s) binds tubulin with a K(D) of 100 nm, stimulates tubulin GTPase, and promotes microtubule dynamic instability. Moreover, the data reveal that the α3-β5 region of Gα(s) is a functionally important motif in the Gα(s)-mediated microtubule destabilization. Indeed, peptides corresponding to that region of Gα(s) mimic Gα(s) protein in activating tubulin GTPase and increase microtubule dynamic instability. We have identified specific mutations in peptides or proteins that interfere with this process. The data allow for a model of the Gα(s)/tubulin interface in which Gα(s) binds to the microtubule plus-end and activates the intrinsic tubulin GTPase. This model illuminates both the role of tubulin as an "effector" (e.g. adenylyl cyclase) for Gα(s) and the role of Gα(s) as a GTPase activator for tubulin. Given the ability of Gα(s) to translocate intracellularly in response to agonist activation, Gα(s) may play a role in hormone- or neurotransmitter-induced regulation of cellular morphology.
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.