ArticleMolecular biology of the cell1997
Distinct endocytic responses of heteromeric and homomeric transforming growth factor beta receptors.
Article in Molecular biology of the cell, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Article
- TGF-β receptor I/II trafficking and signaling at primary cilia are inhibited by ceramide to attenuate cell migration and tumor metastasis.Science signaling · 2017Article
- Basolateral delivery of the type I transforming growth factor beta receptor is mediated by a dominant-acting cytoplasmic motif.Molecular biology of the cell · 2017Article
- Sorting nexin 9 differentiates ligand-activated Smad3 from Smad2 for nuclear import and transforming growth factor β signaling.Molecular biology of the cell · 2015Article
- Internalization of the TGF-β type I receptor into caveolin-1 and EEA1 double-positive early endosomes.Cell research · 2015Article
- Retromer maintains basolateral distribution of the type II TGF-β receptor via the recycling endosome.Molecular biology of the cell · 2013Article
- Coated pit-mediated endocytosis of the type I transforming growth factor-β (TGF-β) receptor depends on a di-leucine family signal and is not required for signaling.The Journal of biological chemistry · 2012Article
- Type II transforming growth factor-beta receptor recycling is dependent upon the clathrin adaptor protein Dab2.Molecular biology of the cell · 2010Article
- Disruption of the murine Ap2β1 gene causes nonsyndromic cleft palate.The Cleft palate-craniofacial journal : official publication of the American Cleft Palate-Craniofacial Association · 2010Article
- Transforming growth factor-beta 1 (TGF-beta1) induces angiogenesis through vascular endothelial growth factor (VEGF)-mediated apoptosis.Journal of cellular physiology · 2009Article
- Endocytosis of the type III transforming growth factor-beta (TGF-beta) receptor through the clathrin-independent/lipid raft pathway regulates TGF-beta signaling and receptor down-regulation.The Journal of biological chemistry · 2008Article
- A unique element in the cytoplasmic tail of the type II transforming growth factor-beta receptor controls basolateral delivery.Molecular biology of the cell · 2007Article
- Modulation of integrin-linked kinase (ILK) expression in human oesophageal squamous cell carcinoma cell lines by the EGF and TGFbeta1 growth factors.Cancer cell international · 2006Article
- Increased expression of integrin alphavbeta5 induces the myofibroblastic differentiation of dermal fibroblasts.The American journal of pathology · 2006Article
- Decreased expression of TGF-beta type II receptor in bronchial glands of smokers with COPD.Thorax · 2005Article
- Ligand-dependent and -independent transforming growth factor-beta receptor recycling regulated by clathrin-mediated endocytosis and Rab11.Molecular biology of the cell · 2004Article
- Differential trafficking of transforming growth factor-beta receptors and ligand in polarized epithelial cells.Molecular biology of the cell · 2004Article
- A novel transforming growth factor-beta receptor-interacting protein that is also a light chain of the motor protein dynein.Molecular biology of the cell · 2002Article
- Transforming growth factor-beta receptors interact with AP2 by direct binding to beta2 subunit.Molecular biology of the cell · 2002Article
- Internalization-dependent and -independent requirements for transforming growth factor beta receptor signaling via the Smad pathway.Molecular and cellular biology · 2002Article
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Authors and funding
4 authors.
Funding
Abstract
Transforming growth factor beta (TGF beta) family ligands initiate a cascade of events capable of modulating cellular growth and differentiation. The receptors responsible for transducing these cellular signals are referred to as the type I and type II TGF beta receptors. Ligand binding to the type II receptor results in the transphosphorylation and activation of the type I receptor. This heteromeric complex then propagates the signal(s) to downstream effectors. There is presently little data concerning the fate of TGF beta receptors after ligand binding, with conflicting reports indicating no change or decreasing cell surface receptor numbers. To address the fate of ligand-activated receptors, we have used our previously characterized chimeric receptors consisting of the ligand binding domain from the granulocyte/macrophage colony-stimulating factor alpha or beta receptor fused to the transmembrane and cytoplasmic domain of the type I or type II TGF beta receptor. This system not only provides the necessary sensitivity and specificity to address these types of questions but also permits the differentiation of endocytic responses to either homomeric or heteromeric intracellular TGF beta receptor oligomerization. Data are presented that show, within minutes of ligand binding, chimeric TGF beta receptors are internalized. However, although all the chimeric receptor combinations show similar internalization rates, receptor down-regulation occurs only after activation of heteromeric TGF beta receptors. These results indicate that effective receptor down-regulation requires cross-talk between the type I and type II TGF beta receptors and that TGF beta receptor heteromers and homomers show distinct trafficking behavior.
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