ArticleMolecular biology of the cell2001
Transforming growth factor beta receptor signaling and endocytosis are linked through a COOH terminal activation motif in the type I receptor.
Article in Molecular biology of the cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 48 citations in OpenAlex.
- Defining the clinical validity of genes reported to cause pulmonary arterial hypertension.Genetics in medicine : official journal of the American College of Medical Genetics · 2023Article
- Computational and Experimental Analyses for Pathogenicity Prediction ofJournal of clinical medicine · 2023Article
- Structural basis for ALK2/BMPR2 receptor complex signaling through kinase domain oligomerization.Nature communications · 2021Article
- BMPR1B gene in brachydactyly type 2-A family with de novo R486W mutation and a disease phenotype.Molecular genetics & genomic medicine · 2021Article
- Article
- New Player in Endosomal Trafficking: Differential Roles of Smad Anchor for Receptor Activation (SARA) Protein.Molecular and cellular biology · 2018Review
- Extracellular matrix-induced transforming growth factor-beta receptor signaling dynamics.Oncogene · 2010Article
- Extracellular matrix-induced gene expression in human breast cancer cells.Molecular cancer research : MCR · 2009Article
- Differential trafficking of transforming growth factor-beta receptors and ligand in polarized epithelial cells.Molecular biology of the cell · 2004Article
- Molecular and functional analysis identifies ALK-1 as the predominant cause of pulmonary hypertension related to hereditary haemorrhagic telangiectasia.Journal of medical genetics · 2003Article
- Cell-type-specific activation of PAK2 by transforming growth factor beta independent of Smad2 and Smad3.Molecular and cellular biology · 2003Article
- Mutations in bone morphogenetic protein receptor 1B cause brachydactyly type A2.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
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6 authors at 2 institutions in 1 country.
Funding
Abstract
Transforming growth factor beta (TGF-beta) coordinates a number of biological events important in normal and pathophysiological growth. In this study, deletion and substitution mutations were used to identify receptor motifs modulating TGF-beta receptor activity. Initial experiments indicated that a COOH-terminal sequence between amino acids 482-491 in the kinase domain of the type I receptor was required for ligand-induced receptor signaling and down-regulation. These 10 amino acids are highly conserved in mammalian, Xenopus, and Drosophila type I receptors. Although mutation or deletion of the region (referred to as the NANDOR BOX, for nonactivating non-down-regulating) abolishes TGF-beta-dependent mitogenesis, transcriptional activity, type I receptor phosphorylation, and down-regulation in mesenchymal cultures, adjacent mutations also within the kinase domain are without effect. Moreover, a kinase-defective type I receptor can functionally complement a mutant BOX expressing type I receptor, documenting that when the BOX mutant is activated, it has kinase activity. These results indicate that the sequence between 482 and 491 in the type I receptor provides a critical function regulating activation of the TGF-beta receptor complex.
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