ArticleMolecular and cellular biology1993
Phosphorylation of the TAL1 oncoprotein by the extracellular-signal-regulated protein kinase ERK1.
Article in Molecular and cellular biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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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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Who cites it
26 citing papers in PubMed, 77 citations in OpenAlex.
- Transcription Factor TAL1 in Erythropoiesis.Advances in experimental medicine and biology · 2024Review
- Review
- GATA2 +9.5 enhancer: from principles of hematopoiesis to genetic diagnosis in precision medicine.Current opinion in hematology · 2020Review
- Review
- Interleukin-18 produced by bone marrow-derived stromal cells supports T-cell acute leukaemia progression.EMBO molecular medicine · 2014Article
- RapGEF2 is essential for embryonic hematopoiesis but dispensable for adult hematopoiesis.Blood · 2010Article
- Targeted therapy in T-cell malignancies: dysregulation of the cellular signaling pathways.Leukemia · 2010Review
- Novel membrane-targeted ERK1 and ERK2 chimeras which act as dominant negative, isotype-specific mitogen-activated protein kinase inhibitors of Ras-Raf-mediated transcriptional activation of c-fos in NIH 3T3 cells.Molecular and cellular biology · 1999Article
- Mitogen-activated protein kinase mediates erythropoietin-induced phosphorylation of the TAL1/SCL transcription factor in murine proerythroblasts.The Biochemical journal · 1999Article
- The SCL gene specifies haemangioblast development from early mesoderm.The EMBO journal · 1998Article
- Basal extracellular signal-regulated kinase activity modulates cell-cell and cell-matrix interactions.Molecular and cellular biology · 1998Article
- Review
- Insulin regulation of mitogen-activated protein kinase kinase (MEK), mitogen-activated protein kinase and casein kinase in the cell nucleus: a possible role in the regulation of gene expression.The Biochemical journal · 1997Article
- A structural basis for substrate specificities of protein Ser/Thr kinases: primary sequence preference of casein kinases I and II, NIMA, phosphorylase kinase, calmodulin-dependent kinase II, CDK5, and Erk1.Molecular and cellular biology · 1996Article
- The extracellular signal-regulated kinase pathway phosphorylates AML1, an acute myeloid leukemia gene product, and potentially regulates its transactivation ability.Molecular and cellular biology · 1996Article
- The pool of map kinase associated with microtubules is small but constitutively active.Molecular biology of the cell · 1996Article
- Effect of human papillomavirus type 16 oncogenes on MAP kinase activity.Journal of virology · 1995Article
- ERK phosphorylation potentiates Elk-1-mediated ternary complex formation and transactivation.The EMBO journal · 1995Article
- The E2A and tal-1 helix-loop-helix proteins associate in vivo and are modulated by Id proteins during interleukin 6-induced myeloid differentiation.Proceedings of the National Academy of Sciences of the United States of America · 1994Article
- Formation of in vivo complexes between the TAL1 and E2A polypeptides of leukemic T cells.Proceedings of the National Academy of Sciences of the United States of America · 1994Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Alteration of the TAL1 gene is the most common genetic lesion found in T-cell acute lymphoblastic leukemia. TAL1 encodes phosphoproteins, pp42TAL1 and pp22TAL1, that represent phosphorylated versions of the full-length (residues 1 to 331) and truncated (residues 176 to 331) TAL1 gene products, respectively. Both proteins contain the basic helix-loop-helix motif, a DNA-binding and protein dimerization motif common to several known transcriptional regulatory factors. We now report that serine residue 122 (S122) is a major phosphorylation site of pp42TAL1 in leukemic cell lines and transfected COS1 cells. In vivo phosphorylation of S122 is induced by epidermal growth factor with a rapid time course that parallels activation of the ERK/MAP2 protein kinases. Moreover, S122 is readily phosphorylated in vitro by the extracellular signal-regulated protein kinase ERK1. These data suggest that TAL1 residue S122 serves as an in vivo substrate for ERK/MAP2 kinases such as ERK1. Therefore, S122 phosphorylation may provide a mechanism whereby the properties of TAL1 polypeptides can be modulated by extracellular stimuli.
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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 OpenQuestion graph.