ArticleMolecular and cellular biology2002
Identification of Akt association and oligomerization domains of the Akt kinase coactivator TCL1.
Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 92 citations in OpenAlex.
- TCL1A mediates DNA methylation defects in recurrent hydatidiform mole with NLRP7 pathogenic variants.Nature communications · 2026Article
- Exosomal mRNA Cargo are biomarkers of tumor and immune cell populations in pediatric osteosarcoma.Translational oncology · 2024Article
- TCL1A+ B cells predict prognosis in triple-negative breast cancer through integrative analysis of single-cell and bulk transcriptomic data.Open life sciences · 2023Article
- AktAR and Akt-STOPS: Genetically Encodable Molecular Tools to Visualize and Perturb Akt Kinase Activity at Different Subcellular Locations in Living Cells.Current protocols · 2022Article
- Multidimensional single-cell analysis of human peripheral blood reveals characteristic features of the immune system landscape in aging and frailty.Nature aging · 2022Article
- Rare t(X;14)(q28;q32) translocation reveals link between MTCP1 and chronic lymphocytic leukemia.Nature communications · 2021Article
- Review
- Review
- Autophagy as a modulator of cell death machinery.Cell death & disease · 2020Review
- Control of Akt activity and substrate phosphorylation in cells.IUBMB life · 2020Review
- The TCL1 function revisited focusing on metabolic requirements of stemness.Cell cycle (Georgetown, Tex.) · 2019Review
- Article
- T-Cell Leukemia/Lymphoma 1 (TCL1): An Oncogene Regulating Multiple Signaling Pathways.Frontiers in oncology · 2018Article
- ROR1 can interact with TCL1 and enhance leukemogenesis in Eμ-TCL1 transgenic mice.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Protooncogene TCL1b functions as an Akt kinase co-activator that exhibits oncogenic potency in vivo.Oncogenesis · 2013Article
- Article
- Aromatase inhibitors, estrogens and musculoskeletal pain: estrogen-dependent T-cell leukemia 1A (TCL1A) gene-mediated regulation of cytokine expression.Breast cancer research : BCR · 2012Article
- Article
- Recent development of anticancer therapeutics targeting Akt.Recent patents on anti-cancer drug discovery · 2011Review
- Epstein-Barr virus nuclear protein 3C domains necessary for lymphoblastoid cell growth: interaction with RBP-Jkappa regulates TCL1.Journal of virology · 2009Article
Corrections and comments
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Authors and funding
9 authors at 6 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Serine/threonine kinase Akt/protein kinase B, the cellular homologue of the transforming viral oncogene v-Akt, plays a central role in the regulation of cell survival and proliferation. We have previously demonstrated that the proto-oncogene TCL1 is an Akt kinase coactivator. TCL1 binds to Akt and mediates the formation of oligomeric TCL1-Akt high-molecular-weight protein complexes in vivo. Within these protein complexes, Akt is preferentially phosphorylated and activated. The MTCP1/TCL1/TCL1b oncogene activation is the hallmark of human T-cell prolymphocytic leukemia (T-PLL), a form of adult leukemia. In the present study, using a PCR-generated random TCL1 library combined with a yeast two-hybrid screening detecting loss of interaction, we identified D16 and I74 as amino acid residues mediating the association of TCL1 with Akt. Based on molecular modeling, we determined that the beta C-sheet of TCL1 is essential for TCL1 homodimerization. Studies with mammalian overexpression systems demonstrated that both Akt association and oligomerization domains of TCL1 are distinct functional domains. In vitro kinase assays and overexpression experiments in mammalian cells demonstrated that both TCL1-Akt interaction and oligomerization of TCL1 were required for TCL1-induced Akt activation and substrate phosphorylation. Assays for mitochondrial permeability transition, nuclear translocation, and cell recovery demonstrated that both Akt association and homodimerization of TCL1 are similarly needed for the full function of TCL1 as an Akt kinase coactivator in vivo. The results demonstrate the structural basis of TCL1-induced activation of Akt, which causes human T-PLL.
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Registered trials
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