ArticleThe Biochemical journal2006
The Dbs PH domain contributes independently to membrane targeting and regulation of guanine nucleotide-exchange activity.
Article in The Biochemical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
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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.
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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
29 citing papers in PubMed, 50 citations in OpenAlex.
- Rho Small GTPase Family in Androgen-Regulated Prostate Cancer Progression and Metastasis.Cancers · 2025Review
- The RhoGEF protein Plekhg5 self-associates via its PH domain to regulate apical cell constriction.Molecular biology of the cell · 2024Article
- New Mechanisms Underlying Oncogenesis in Dbl Family Rho Guanine Nucleotide Exchange Factors.Molecular pharmacology · 2024Review
- Role of RhoG as a regulator of cellular functions: integrating insights on immune cell activation, migration, and functions.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2023Review
- Article
- Identification of potent and novel inhibitors against RAC1: a Rho family GTPase.In silico pharmacology · 2022Article
- Article
- Structural Insights into the Regulation Mechanism of Small GTPases by GEFs.Molecules (Basel, Switzerland) · 2019Review
- DBS is activated by EPHB2/SRC signaling-mediated tyrosine phosphorylation in HEK293 cells.Molecular and cellular biochemistry · 2019Article
- Involvement of the protein kinase Akt2 in insulin-stimulated Rac1 activation leading to glucose uptake in mouse skeletal muscle.PloS one · 2019Article
- The RhoGEF protein Plekhg5 regulates apical constriction of bottle cells during gastrulation.Development (Cambridge, England) · 2018Article
- ARHGEF39 promotes gastric cancer cell proliferation and migration via Akt signaling pathway.Molecular and cellular biochemistry · 2018Article
- The Tiam1 guanine nucleotide exchange factor is auto-inhibited by its pleckstrin homology coiled-coil extension domain.The Journal of biological chemistry · 2017Article
- Novel Coronin7 interactions with Cdc42 and N-WASP regulate actin organization and Golgi morphology.Scientific reports · 2016Article
- Phosphatidylinositol 3-phosphates-at the interface between cell signalling and membrane traffic.The EMBO journal · 2016Review
- Article
- Crossroads of PI3K and Rac pathways.Small GTPases · 2015Review
- Superoxide inhibits guanine nucleotide exchange factor (GEF) action on Ras, but not on Rho, through desensitization of Ras to GEF.Biochemistry · 2014Article
- Gene expression within the extended amygdala of 5 pairs of rat lines selectively bred for high or low ethanol consumption.Alcohol (Fayetteville, N.Y.) · 2013Article
- Biochemical and cellular implications of a dual lipase-GEF function of phospholipase D2 (PLD2).Journal of leukocyte biology · 2012Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Dbl family GEFs (guanine nucleotide-exchange factors) for the Rho GTPases almost invariably contain a PH (pleckstrin homology) domain adjacent to their DH (Dbl homology) domain. The DH domain is responsible for GEF activity, and the PH domain plays a regulatory role that remains poorly understood. We demonstrated previously that Dbl family PH domains bind phosphoinositides with low affinity and cannot function as independent membrane targeting modules. In the present study, we show that dimerization of a Dbs (Dbl's big sister) DH/PH domain fragment is sufficient to drive it to the plasma membrane through a mechanism involving PH domain-phosphoinositide interactions. Thus, the Dbs PH domain could play a significant role in membrane targeting if it co-operates with other domains in the protein. We also show that mutations that prevent phosphoinositide binding by the Dbs PH domain significantly impair cellular GEF activity even in chimaeric proteins that are robustly membrane targeted by farnesylation or by the PH domain of phospholipase C-delta1. This finding argues that the Dbs PH domain plays a regulatory role that is independent of its ability to aid membrane targeting. Thus, we suggest that the PH domain plays dual roles, contributing independently to membrane localization of Dbs (as part of a multi-domain interaction) and allosteric regulation of the DH domain.
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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 Socratic graph.