ArticleProceedings of the National Academy of Sciences of the United States of America2006
A retrovirus-based protein complementation assay screen reveals functional AKT1-binding partners.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed, 96 citations in OpenAlex.
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- Alpha-actinin-4 is essential for maintaining normal trophoblast proliferation and differentiation during early pregnancy.Reproductive biology and endocrinology : RB&E · 2021Article
- Detection of genes mutations in cerebrospinal fluid circulating tumor DNA from neoplastic meningitis patients using next generation sequencing.BMC cancer · 2020Article
- α-Actinin-4 Promotes the Progression of Prostate Cancer Through the Akt/GSK-3β/β-Catenin Signaling Pathway.Frontiers in cell and developmental biology · 2020Article
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- Elevated TRIP13 drives the AKT/mTOR pathway to induce the progression of hepatocellular carcinoma via interacting with ACTN4.Journal of experimental & clinical cancer research : CR · 2019Article
- Synergistic Ensemble of Optogenetic Actuators and Dynamic Indicators in Cell Biology.Molecules and cells · 2018Review
- ACTN4 regulates the stability of RIPK1 in melanoma.Oncogene · 2018Article
- Surveying the landscape of optogenetic methods for detection of protein-protein interactions.Wiley interdisciplinary reviews. Systems biology and medicine · 2018Review
- Recent Advances in Substrate Identification of Protein Kinases in Plants and Their Role in Stress Management.Current genomics · 2017Review
- Genome-wide identification of histone H2A and histone variant H2A.Z-interacting proteins by bPPI-seq.Cell research · 2017Article
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Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We developed a retrovirus-based protein-fragment complementation assay (RePCA) screen to identify protein-protein interactions in mammalian cells. In RePCA, bait protein is fused to one fragment of a rationally dissected fluorescent protein, such as GFP, intensely fluorescent protein, or red fluorescent protein. The second, complementary fragment of the fluorescent protein is fused to an endogenous protein by in-frame exon traps in the enhanced retroviral mutagen vector. An interaction between bait and host protein (prey) places the two parts of the fluorescent molecule in proximity, resulting in reconstitution of fluorescence. By using RePCA, we identified a series of 24 potential interaction partners or substrates of the serine/threonine protein kinase AKT1. We confirm that alpha-actinin 4 (ACTN4) interacts physically and functionally with AKT1. siRNA-mediated ACTN4 silencing down-regulates AKT phosphorylation, blocks AKT translocation to the membrane, increases p27(Kip1) levels, and inhibits cell proliferation. Thus, ACTN4 is a critical regulator of AKT1 localization and function.
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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.