ArticleThe Journal of biological chemistry2009
A PH domain in the Arf GTPase-activating protein (GAP) ARAP1 binds phosphatidylinositol 3,4,5-trisphosphate and regulates Arf GAP activity independently of recruitment to the plasma membranes.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 33 citations in OpenAlex.
- Article
- In vitro reconstitution reveals phosphoinositides as cargo-release factors and activators of the ARF6 GAP ADAP1.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Role of Protein Kinase CK2 in Aberrant Lipid Metabolism in Cancer.Pharmaceuticals (Basel, Switzerland) · 2020Review
- AGAP2: Modulating TGFβ1-Signaling in the Regulation of Liver Fibrosis.International journal of molecular sciences · 2020Review
- ARF GTPases and their GEFs and GAPs: concepts and challenges.Molecular biology of the cell · 2019Review
- Arf GAPs as Regulators of the Actin Cytoskeleton-An Update.International journal of molecular sciences · 2019Review
- Polyphosphoinositide-Binding Domains: Insights from Peripheral Membrane and Lipid-Transfer Proteins.Advances in experimental medicine and biology · 2019Review
- ARAP1 Bridges Actin Dynamics and AP-3-Dependent Membrane Traffic in Bone-Digesting Osteoclasts.iScience · 2018Article
- Identification of genes required for eye development by high-throughput screening of mouse knockouts.Communications biology · 2018Article
- Arap1 Deficiency Causes Photoreceptor Degeneration in Mice.Investigative ophthalmology & visual science · 2017Article
- PIP3-binding proteins promote age-dependent protein aggregation and limit survival in C. elegans.Oncotarget · 2016Article
- Polyphosphoinositide binding domains: Key to inositol lipid biology.Biochimica et biophysica acta · 2015Review
- The Arf6 GTPase-activating proteins ARAP2 and ACAP1 define distinct endosomal compartments that regulate integrin α5β1 traffic.The Journal of biological chemistry · 2014Article
- Mammalian phosphatidylinositol 4-kinases as modulators of membrane trafficking and lipid signaling networks.Progress in lipid research · 2013Review
- Phosphatidylinositol-3,4,5-trisphosphate: tool of choice for class I PI 3-kinases.BioEssays : news and reviews in molecular, cellular and developmental biology · 2013Review
- The Arf GAP AGAP2 interacts with β-arrestin2 and regulates β2-adrenergic receptor recycling and ERK activation.The Biochemical journal · 2013Article
- ARAP2 signals through Arf6 and Rac1 to control focal adhesion morphology.The Journal of biological chemistry · 2013Article
- ARAP1 regulates the ring size of circular dorsal ruffles through Arf1 and Arf5.Molecular biology of the cell · 2012Article
- Phosphatidylinositol-4-phosphate 5-kinase and GEP100/Brag2 protein mediate antiangiogenic signaling by semaphorin 3E-plexin-D1 through Arf6 protein.The Journal of biological chemistry · 2011Article
- A screen for novel phosphoinositide 3-kinase effector proteins.Molecular & cellular proteomics : MCP · 2011Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
ARAP1 is a phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P(3))-dependent Arf GTPase-activating protein (GAP) with five PH domains that regulates endocytic trafficking of the epidermal growth factor receptor (EGFR). Two tandem PH domains are immediately N-terminal of the Arf GAP domain, and one of these fits the consensus sequence for PtdIns(3,4,5)P(3) binding. Here, we tested the hypothesis that PtdIns(3,4,5)P(3)-dependent recruitment mediated by the first PH domain of ARAP1 regulates the in vivo and in vitro function of ARAP1. We found that PH1 of ARAP1 specifically bound to PtdIns(3,4,5)P(3), but with relatively low affinity (approximately 1.6 microm), and the PH domains did not mediate PtdIns(3,4,5)P(3)-dependent recruitment to membranes in cells. However, PtdIns(3,4,5)P(3) binding to the PH domain stimulated GAP activity and was required for in vivo function of ARAP1 as a regulator of endocytic trafficking of the EGFR. Based on these results, we propose a variation on the model for the function of phosphoinositide-binding PH domains. In our model, ARAP1 is recruited to membranes independently of PtdIns(3,4,5)P(3), the subsequent production of which triggers enzymatic activity.
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