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Journal articles on the topic 'Transforming growth factor β receptor II'

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Published: 11 March 2023

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1

Anders, Robert A., Sandra L. Arline, Jules J. E. Doré, and Edward B. Leof. "Distinct Endocytic Responses of Heteromeric and Homomeric Transforming Growth Factor β Receptors." Molecular Biology of the Cell 8, no. 11 (November 1997): 2133–43. http://dx.doi.org/10.1091/mbc.8.11.2133.

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Transforming growth factor β (TGFβ) 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 TGFβ 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 TGFβ 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 α or β receptor fused to the transmembrane and cytoplasmic domain of the type I or type II TGFβ 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 TGFβ receptor oligomerization. Data are presented that show, within minutes of ligand binding, chimeric TGFβ receptors are internalized. However, although all the chimeric receptor combinations show similar internalization rates, receptor down-regulation occurs only after activation of heteromeric TGFβ receptors. These results indicate that effective receptor down-regulation requires cross-talk between the type I and type II TGFβ receptors and that TGFβ receptor heteromers and homomers show distinct trafficking behavior.

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2

Zhang, Wei, Yaxin Jiang, Qiang Wang, Xinyong Ma, Zeyu Xiao, Wei Zuo, Xiaohong Fang, and Ye-Guang Chen. "Single-molecule imaging reveals transforming growth factor-β-induced type II receptor dimerization." Proceedings of the National Academy of Sciences 106, no. 37 (August 31, 2009): 15679–83. http://dx.doi.org/10.1073/pnas.0908279106.

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Transforming growth factor-β (TGF-β) elicits its signals through two transmembrane serine/threonine kinase receptors, type II (TβRII) and type I receptors. It is generally believed that the initial receptor dimerization is an essential event for receptor activation. However, previous studies suggested that TGF-β signals by binding to the preexisting TβRII homodimer. Here, using single molecule microscopy to image green fluorescent protein (GFP)-labeled TβRII on the living cell surface, we demonstrated that the receptor could exist as monomers at the low expression level in resting cells and dimerize upon TGF-β stimulation. This work reveals a model in which the activation of serine-threonine kinase receptors is also accomplished via dimerization of monomers, suggesting that receptor dimerization is a general mechanism for ligand-induced receptor activation.

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3

Wicks, Stephen J., Stephen Lui, Nadia Abdel-Wahab, Roger M. Mason, and Andrew Chantry. "Inactivation of Smad-Transforming Growth Factor β Signaling by Ca2+-Calmodulin-Dependent Protein Kinase II." Molecular and Cellular Biology 20, no. 21 (November 1, 2000): 8103–11. http://dx.doi.org/10.1128/mcb.20.21.8103-8111.2000.

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ABSTRACT Members of the transforming growth factor β (TGF-β) family transduce signals through Smad proteins. Smad signaling can be regulated by the Ras/Erk/mitogen-activated protein pathway in response to receptor tyrosine kinase activation and the gamma interferon pathway and also by the functional interaction of Smad2 with Ca2+-calmodulin. Here we report that Smad–TGF-β-dependent transcriptional responses are prevented by expression of a constitutively activated Ca2+-calmodulin-dependent protein kinase II (Cam kinase II). Smad2 is a target substrate for Cam kinase II in vitro at serine-110, -240, and -260. Cam kinase II induces in vivo phosphorylation of Smad2 and Smad4 and, to a lesser extent, Smad3. A phosphopeptide antiserum raised against Smad2 phosphoserine-240 reacted with Smad2 in vivo when coexpressed with Cam kinase II and by activation of the platelet-derived growth factor receptor, the epidermal growth factor receptor, HER2 (c-erbB2), and the TGF-β receptor. Furthermore, Cam kinase II blocked nuclear accumulation of a Smad2 and induced Smad2-Smad4 hetero-oligomerization independently of TGF-β receptor activation, while preventing TGF-β-dependent Smad2-Smad3 interactions. These findings provide a novel cross-talk mechanism by which Ca2+-dependent kinases activated downstream of multiple growth factor receptors antagonize cell responses to TGF-β.

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4

Clarke, David C., Meredith L. Brown, Richard A. Erickson, Yigong Shi, and Xuedong Liu. "Transforming Growth Factor β Depletion Is the Primary Determinant of Smad Signaling Kinetics." Molecular and Cellular Biology 29, no. 9 (February 17, 2009): 2443–55. http://dx.doi.org/10.1128/mcb.01443-08.

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ABSTRACT A cell's decision to growth arrest, apoptose, or differentiate in response to transforming growth factor β (TGF-β) superfamily ligands depends on the ligand concentration. How cells sense the concentration of extracellular bioavailable TGF-β remains poorly understood. We therefore undertook a systematic quantitative analysis of how TGF-β ligand concentration is transduced into downstream phospho-Smad2 kinetics, and we found that the rate of TGF-β ligand depletion is the principal determinant of Smad signal duration. TGF-β depletion is caused by two mechanisms: (i) cellular uptake of TGF-β by a TGF-β type II receptor-dependent mechanism and (ii) reversible binding of TGF-β to the cell surface. Our results indicate that cells sense TGF-β dose by depleting TGF-β via constitutive TGF-β type II receptor trafficking processes. Our results also have implications for the role of the TGF-β type II receptor in disease, as tumor cells harboring TGF-β type II receptor mutations exhibit impaired TGF-β depletion, which may contribute to the overproduction of TGF-β and a consequently poor prognosis in cancer.

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5

Jacko, A. M., L. Nan, S. Li, J. Tan, J. Zhao, D. J. Kass, and Y. Zhao. "De-ubiquitinating enzyme, USP11, promotes transforming growth factor β-1 signaling through stabilization of transforming growth factor β receptor II." Cell Death & Disease 7, no. 11 (November 2016): e2474-e2474. http://dx.doi.org/10.1038/cddis.2016.371.

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6

HALL, Frederick L., Paul D. BENYA, Silvia R. PADILLA, Denise CARBONARO-HALL, Richard WILLIAMS, Sue BUCKLEY, and David WARBURTON. "Transforming growth factor-β type-II receptor signalling: intrinsic/associated casein kinase activity, receptor interactions and functional effects of blocking antibodies." Biochemical Journal 316, no. 1 (May 15, 1996): 303–10. http://dx.doi.org/10.1042/bj3160303.

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The transforming growth factor β (TGF-β) family of growth factors control proliferation, extracellular matrix synthesis and/ or differentiation in a wide variety of cells. However, the molecular mechanisms governing ligand binding, receptor oligomerization and signal transduction remain incompletely understood. In this study, we utilized a set of antibodies selective for the extracellular and intracellular domains of the TGF-β type-II receptor as probes to investigate the intrinsic kinase activity of this receptor and its physical association in multimeric complexes with type-I and type-III receptors. The type-II receptor immunoprecipitated from human osteosarcoma cells exhibited autophosphorylation and casein kinase activity that was markedly stimulated by polylysine yet was insensitive to heparin. Affinity cross-linking of 125I-TGF-β1 ligand to cellular receptors followed by specific immunoprecipitation demonstrated that type-II receptors form stable complexes with both type-I and type-III receptors expressed on the surfaces of both human osteosarcoma cells and rabbit chondrocytes. Pretreatment of the cultured cells with an antibody directed against a distinct extracellular segment of the type-II receptor (anti-TGF-β-IIR-NT) effectively blocked the 125I-TGF-β labelling of type-I receptors without preventing the affinity labelling of type-II or type-III receptors, indicating a selective disruption of the type-I/type-II hetero-oligomers. The anti-TGF-β-IIR-NT antibodies also blocked the TGF-β-dependent induction of the plasminogen activator inhibitor (PAI-1) promoter observed in mink lung epithelial cells. However, the same anti-TGF-β-IIR-NT antibodies did not prevent the characteristic inhibition of cellular proliferation by TGF-β1, as determined by [3H]thymidine incorporation into DNA. The selective perturbation of PAI-1 promoter induction versus cell-cycle-negative regulation suggests that strategic disruption of TGF-β type-I and -II receptor interactions can effectively alter specific cellular responses to TGF-β signalling.

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7

Bhowmick, Neil A., Roy Zent, Mayshan Ghiassi, Maureen McDonnell, and Harold L. Moses. "Integrin β1Signaling Is Necessary for Transforming Growth Factor-β Activation of p38MAPK and Epithelial Plasticity." Journal of Biological Chemistry 276, no. 50 (October 5, 2001): 46707–13. http://dx.doi.org/10.1074/jbc.m106176200.

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Transforming growth factor-β (TGF-β) can induce epithelial to mesenchymal transdifferentiation (EMT) in mammary epithelial cells. TGF-β-meditated EMT involves the stimulation of a number of signaling pathways by the sequential binding of the type II and type I serine/threonine kinase receptors, respectively. Integrins comprise a family of heterodimeric extracellular matrix receptors that mediate cell adhesion and intracellular signaling, hence making them crucial for EMT progression. In light of substantial evidence indicating TGF-β regulation of various β1integrins and their extracellular matrix ligands, we examined the cross-talk between the TGF-β and integrin signal transduction pathways. Using an inducible system for the expression of a cytoplasmically truncated dominant negative TGF-β type II receptor, we blocked TGF-β-mediated growth inhibition, transcriptional activation, and EMT progression. Dominant negative TGF-β type II receptor expression inhibited TGF-β signaling to the SMAD and AKT pathways, but did not block TGF-β-mediated p38MAPK activation. Interestingly, blocking integrin β1function inhibited TGF-β-mediated p38MAPK activation and EMT progression. Limiting p38MAPK activity through the expression of a dominant negative-p38MAPK also blocked TGF-β-mediated EMT. In summary, TGF-β-mediated p38MAPK activation is dependent on functional integrin β1, and p38MAPK activity is required but is not sufficient to induce EMT.

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8

Tsuchida, K., K. A. Lewis, L. S. Mathews, and W. W. Vale. "Molecular Characterization of Rat Transforming Growth Factor-β Type II Receptor." Biochemical and Biophysical Research Communications 191, no. 3 (March 1993): 790–95. http://dx.doi.org/10.1006/bbrc.1993.1286.

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9

Datta, Pran K., and Harold L. Moses. "STRAP and Smad7 Synergize in the Inhibition of Transforming Growth Factor β Signaling." Molecular and Cellular Biology 20, no. 9 (May 1, 2000): 3157–67. http://dx.doi.org/10.1128/mcb.20.9.3157-3167.2000.

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ABSTRACT Smad proteins play a key role in the intracellular signaling of the transforming growth factor β (TGF-β) superfamily of extracellular polypeptides that initiate signaling from the cell surface through serine/threonine kinase receptors. A subclass of Smad proteins, including Smad6 and Smad7, has been shown to function as intracellular antagonists of TGF-β family signaling. We have previously reported the identification of a WD40 repeat protein, STRAP, that associates with both type I and type II TGF-β receptors and that is involved in TGF-β signaling. Here we demonstrate that STRAP synergizes specifically with Smad7, but not with Smad6, in the inhibition of TGF-β-induced transcriptional responses. STRAP does not show cooperation with a C-terminal deletion mutant of Smad7 that does not bind with the receptor and consequently has no inhibitory activity. STRAP associates stably with Smad7, but not with the Smad7 mutant. STRAP recruits Smad7 to the activated type I receptor and forms a complex. Moreover, STRAP stabilizes the association between Smad7 and the activated receptor, thus assisting Smad7 in preventing Smad2 and Smad3 access to the receptor. STRAP interacts with Smad2 and Smad3 but does not cooperate functionally with these Smads to transactivate TGF-β-dependent transcription. The C terminus of STRAP is required for its phosphorylation in vivo, which is dependent on the TGF-β receptor kinases. Thus, we describe a mechanism to explain how STRAP and Smad7 function synergistically to block TGF-β-induced transcriptional activation.

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10

Fernandez, Tania, Stephanie Amoroso, Shellyann Sharpe, Gary M. Jones, Valery Bliskovski, Alexander Kovalchuk, Lalage M. Wakefield, Seong-Jin Kim, Michael Potter, and John J. Letterio. "Disruption of Transforming Growth Factor β Signaling by a Novel Ligand-dependent Mechanism." Journal of Experimental Medicine 195, no. 10 (May 13, 2002): 1247–55. http://dx.doi.org/10.1084/jem.20011521.

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Transforming growth factor (TGF)-β is the prototype in a family of secreted proteins that act in autocrine and paracrine pathways to regulate cell development and function. Normal cells typically coexpress TGF-β receptors and one or more isoforms of TGF-β, thus the synthesis and secretion of TGF-β as an inactive latent complex is considered an essential step in regula-ting the activity of this pathway. To determine whether intracellular activation of TGF-β results in TGF-β ligand–receptor interactions within the cell, we studied pristane-induced plasma cell tumors (PCTs). We now demonstrate that active TGF-β1 in the PCT binds to intracellular TGF-β type II receptor (TβRII). Disruption of the expression of TGF-β1 by antisense TGF-β1 mRNA restores localization of TβRII at the PCT cell surface, indicating a ligand-induced impediment in receptor trafficking. We also show that retroviral expression of a truncated, dominant-negative TβRII (dnTβRII) effectively competes for intracellular binding of active ligand in the PCT and restores cell surface expression of the endogenous TβRII. Analysis of TGF-β receptor–activated Smad2 suggests the intracellular ligand–receptor complex is not capable of signaling. These data are the first to demonstrate the formation of an intracellular TGF-β–receptor complex, and define a novel mechanism for modulating the TGF-β signaling pathway.

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11

Zheng, Shuhui, Hang Zhou, Zhuohui Chen, Yongyong Li, Taifeng Zhou, Chengjie Lian, Bo Gao, Peiqiang Su, and Caixia Xu. "Type III Transforming Growth Factor-β Receptor RNA Interference Enhances Transforming Growth Factor β3-Induced Chondrogenesis Signaling in Human Mesenchymal Stem Cells." Stem Cells International 2018 (August 8, 2018): 1–11. http://dx.doi.org/10.1155/2018/4180857.

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The type III transforming growth factor-β (TGF-β) receptor (TβRIII), a coreceptor of the TGF-β superfamily, is known to bind TGF-βs and regulate TGF-β signaling. However, the regulatory roles of TβRIII in TGF-β-induced mesenchymal stem cell (MSC) chondrogenesis have not been explored. The present study examined the effect of TβRIII RNA interference (RNAi) on TGF-β3-induced human MSC (hMSC) chondrogenesis and possible signal mechanisms. A lentiviral expression vector containing TβRIII small interfering RNA (siRNA) (SiTβRIII) or a control siRNA (SiNC) gene was constructed and infected into hMSCs. The cells were cultured in chondrogenic medium containing TGF-β3 or control medium. TβRIII RNAi significantly enhanced TGF-β3-induced chondrogenic differentiation of hMSCs, the ratio of type II (TβRII) to type I (TβRI) TGF-β receptors, and phosphorylation levels of Smad2/3 as compared with cells infected with SiNC. An inhibitor of the TGF-β signal, SB431542, not only inhibited TβRIII RNAi-stimulated TGF-β3-mediated Smad2/3 phosphorylation but also inhibited the effects of TβRIII RNAi on TGF-β3-induced chondrogenic differentiation. These results demonstrate that TβRIII RNAi enhances TGF-β3-induced chondrogenic differentiation in hMSCs by activating TGF-β/Smad2/3 signaling. The finding points to the possibility of modifying MSCs by TβRIII knockdown as a potent future strategy for cell-based cartilage tissue engineering.

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12

Matoba, H., S. Sugano, N. Yamaguchi, and Y. Miyachi. "Expression of Transforming Growth Factor-β1and Transforming Growth Factor-β Type-II Receptor mRNA in Papillary Thyroid Carcinoma." Hormone and Metabolic Research 30, no. 10 (October 1998): 624–28. http://dx.doi.org/10.1055/s-2007-978946.

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13

Penheiter, Sumedha G., Raman Deep Singh, Claire E. Repellin, Mark C. Wilkes, Maryanne Edens, Philip H. Howe, Richard E. Pagano, and Edward B. Leof. "Type II Transforming Growth Factor-β Receptor Recycling Is Dependent upon the Clathrin Adaptor Protein Dab2." Molecular Biology of the Cell 21, no. 22 (November 15, 2010): 4009–19. http://dx.doi.org/10.1091/mbc.e09-12-1019.

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Transforming growth factor (TGF)-β family proteins form heteromeric complexes with transmembrane serine/threonine kinases referred to as type I and type II receptors. Ligand binding initiates a signaling cascade that generates a variety of cell type-specific phenotypes. Whereas numerous studies have investigated the regulatory activities controlling TGF-β signaling, there is relatively little information addressing the endocytic and trafficking itinerary of TGF-β receptor subunits. In the current study we have investigated the role of the clathrin-associated sorting protein Disabled-2 (Dab2) in TGF-β receptor endocytosis. Although small interfering RNA-mediated Dab2 knockdown had no affect on the internalization of various clathrin-dependent (i.e., TGF-β, low-density lipoprotein, or transferrin) or -independent (i.e., LacCer) cargo, TGF-β receptor recycling was abrogated. Loss of Dab2 resulted in enlarged early endosomal antigen 1-positive endosomes, reflecting the inability of cargo to traffic from the early endosome to the endosomal recycling compartment and, as documented previously, diminished Smad2 phosphorylation. The results support a model whereby Dab2 acts as a multifunctional adaptor in mesenchymal cells required for TGF-β receptor recycling as well as Smad2 phosphorylation.

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14

Rebbapragada, A., H. Benchabane, J. L. Wrana, A. J. Celeste, and L. Attisano. "Myostatin Signals through a Transforming Growth Factor β-Like Signaling Pathway To Block Adipogenesis." Molecular and Cellular Biology 23, no. 20 (October 15, 2003): 7230–42. http://dx.doi.org/10.1128/mcb.23.20.7230-7242.2003.

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ABSTRACT Myostatin, a transforming growth factor β (TGF-β) family member, is a potent negative regulator of skeletal muscle growth. In this study we characterized the myostatin signal transduction pathway and examined its effect on bone morphogenetic protein (BMP)-induced adipogenesis. While both BMP7 and BMP2 activated transcription from the BMP-responsive I-BRE-Lux reporter and induced adipogenic differentiation, myostatin inhibited BMP7- but not BMP2-mediated responses. To dissect the molecular mechanism of this antagonism, we characterized the myostatin signal transduction pathway. We showed that myostatin binds the type II Ser/Thr kinase receptor. ActRIIB, and then partners with a type I receptor, either activin receptor-like kinase 4 (ALK4 or ActRIB) or ALK5 (TβRI), to induce phosphorylation of Smad2/Smad3 and activate a TGF-β-like signaling pathway. We demonstrated that myostatin prevents BMP7 but not BMP2 binding to its receptors and that BMP7-induced heteromeric receptor complex formation is blocked by competition for the common type II receptor, ActRIIB. Thus, our results reveal a strikingly specific antagonism of BMP7-mediated processes by myostatin and suggest that myostatin is an important regulator of adipogenesis.

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15

Doré, Jules J. E., Diying Yao, Maryanne Edens, Nandor Garamszegi, Elizabeth L. Sholl, and Edward B. Leof. "Mechanisms of Transforming Growth Factor-β Receptor Endocytosis and Intracellular Sorting Differ between Fibroblasts and Epithelial Cells." Molecular Biology of the Cell 12, no. 3 (March 2001): 675–84. http://dx.doi.org/10.1091/mbc.12.3.675.

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Transforming growth factor-βs (TGF-β) are multifunctional proteins capable of either stimulating or inhibiting mitosis, depending on the cell type. These diverse cellular responses are caused by stimulating a single receptor complex composed of type I and type II receptors. Using a chimeric receptor model where the granulocyte/monocyte colony-stimulating factor receptor ligand binding domains are fused to the transmembrane and cytoplasmic signaling domains of the TGF-β type I and II receptors, we wished to describe the role(s) of specific amino acid residues in regulating ligand-mediated endocytosis and signaling in fibroblasts and epithelial cells. Specific point mutations were introduced at Y182, T200, and Y249 of the type I receptor and K277 and P525 of the type II receptor. Mutation of either Y182 or Y249, residues within two putative consensus tyrosine-based internalization motifs, had no effect on endocytosis or signaling. This is in contrast to mutation of T200 to valine, which resulted in ablation of signaling in both cell types, while only abolishing receptor down-regulation in fibroblasts. Moreover, in the absence of ligand, both fibroblasts and epithelial cells constitutively internalize and recycle the TGF-β receptor complex back to the plasma membrane. The data indicate fundamental differences between mesenchymal and epithelial cells in endocytic sorting and suggest that ligand binding diverts heteromeric receptors from the default recycling pool to a pathway mediating receptor down-regulation and signaling.

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16

Song, Kyung, Hui Wang, Tracy L. Krebs, Seong-Jin Kim, and David Danielpour. "Androgenic Control of Transforming Growth Factor-β Signaling in Prostate Epithelial Cells through Transcriptional Suppression of Transforming Growth Factor-β Receptor II." Cancer Research 68, no. 19 (September 30, 2008): 8173–82. http://dx.doi.org/10.1158/0008-5472.can-08-2290.

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17

MIYAJIMA, AKIRA, TOMOHIKO ASANO, and MASAMICHI HAYAKAWA. "CAPTOPRIL RESTORES TRANSFORMING GROWTH FACTOR-β TYPE II RECEPTOR AND SENSITIVITY TO TRANSFORMING GROWTH FACTOR-β IN MURINE RENAL CELL CANCER CELLS." Journal of Urology 165, no. 2 (February 2001): 616–20. http://dx.doi.org/10.1097/00005392-200102000-00083.

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18

Kim, Jae-Hwan, Phillip J. Wilder, Jingwen Hou, Tamara Nowling, and Angie Rizzino. "Activation of the Murine Type II Transforming Growth Factor-β Receptor Gene." Journal of Biological Chemistry 277, no. 20 (March 13, 2002): 17520–30. http://dx.doi.org/10.1074/jbc.m110434200.

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19

Griswold-Prenner, Irene, Craig Kamibayashi, E. Miko Maruoka, Marc C. Mumby, and Rik Derynck. "Physical and Functional Interactions between Type I Transforming Growth Factor β Receptors and Bα, a WD-40 Repeat Subunit of Phosphatase 2A." Molecular and Cellular Biology 18, no. 11 (November 1, 1998): 6595–604. http://dx.doi.org/10.1128/mcb.18.11.6595.

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ABSTRACT We have previously shown that a WD-40 repeat protein, TRIP-1, associates with the type II transforming growth factor β (TGF-β) receptor. In this report, we show that another WD-40 repeat protein, the Bα subunit of protein phosphatase 2A, associates with the cytoplasmic domain of type I TGF-β receptors. This association depends on the kinase activity of the type I receptor, is increased by coexpression of the type II receptor, which is known to phosphorylate and activate the type I receptor, and allows the type I receptor to phosphorylate Bα. Furthermore, Bα enhances the growth inhibition activity of TGF-β in a receptor-dependent manner. Because Bα has been characterized as a regulator of phosphatase 2A activity, our observations suggest possible functional interactions between the TGF-β receptor complex and the regulation of protein phosphatase 2A.

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20

Vincent, F., M. Nagashima, S. Takenoshita, M. A. Khan, A. Gemma, K. Hagiwara, and W. P. Bennett. "Mutation analysis of the transforming growth factor-β type II receptor in human cell lines resistant to growth inhibition by transforming growth factor-β." Oncogene 15, no. 1 (July 1997): 117–22. http://dx.doi.org/10.1038/sj.onc.1201166.

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21

Togni, Claudio, Emanuel Rom, Isabel Burghardt, Patrick Roth, Elisabeth J. Rushing, Michael Weller, and Dorothee Gramatzki. "Prognostic Relevance of Transforming Growth Factor-β Receptor Expression and Signaling in Glioblastoma, Isocitrate Dehydrogenase-Wildtype." Journal of Neuropathology & Experimental Neurology 81, no. 3 (February 22, 2022): 225–35. http://dx.doi.org/10.1093/jnen/nlac007.

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Abstract The transforming growth factor (TGF)-β signaling pathway has been recognized as a major factor in promoting the aggressive behavior of glioblastoma, isocitrate dehydrogenase-wildtype. However, there is little knowledge about the expression of TGF-β receptors in glioblastoma. Here, we studied the expression patterns of TGF-β receptor II (TGFβRII), type I receptors activin receptor-like kinase (ALK)-5, and ALK-1, as well as of the transcriptional regulators inhibitor of differentiation (Id) 2, Id3, and Id4 in human glioblastoma. The expression of TGFβRII, ALK-5, and ALK-1 varied greatly, with TGFβRII and ALK-5 being the most abundant and ALK-1 being the least expressed receptor. None of the 3 receptors was preferentially expressed by tumor vasculature as opposed to the tumor bulk, indicating tumor bulk-governed mechanisms of TGF-β signaling with regard to glioblastoma-associated angiogenesis. A positive correlation was found between ALK-1 and Id2, suggesting that Id2, broadly expressed in the tumor cells, is a downstream target of this receptor-dependent pathway. Furthermore, there was a trend for high expression of ALK-5 or Id2 to be associated with inferior overall survival. Hence, we propose that ALK-5 may be used for patient stratification in future anti-TGF-β treatment trials and that Id2 might be a potential target for anti-TGF-β interventions.

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22

Penheiter, Sumedha G., Hugh Mitchell, Nandor Garamszegi, Maryanne Edens, Jules J. E. Doré,, and Edward B. Leof. "Internalization-Dependent and -Independent Requirements for Transforming Growth Factor β Receptor Signaling via the Smad Pathway." Molecular and Cellular Biology 22, no. 13 (July 1, 2002): 4750–59. http://dx.doi.org/10.1128/mcb.22.13.4750-4759.2002.

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ABSTRACT Members of the transforming growth factor β (TGF-β) family of proteins signal through cell surface transmembrane serine/threonine protein kinases known as type I and type II receptors. The TGF-β signal is extended through phosphorylation of receptor-associated Smad proteins by the type I receptor. Although numerous investigations have established the sequence of events in TGF-β receptor (TGF-βR) activation, none have examined the role of the endocytic pathway in initiation and/or maintenance of the signaling response. In this study we investigated whether TGF-βR internalization modulates type I receptor activation, the formation of a functional receptor/Smad/SARA complex, Smad2/3 phosphorylation or nuclear translocation, and TGF-β-dependent reporter gene activity. Our data provide evidence that, whereas type I receptor phosphorylation and association of SARA and Smad2 with the TGF-βR complex take place independently of clathrin lattice formation, Smad2 or Smad3 activation and downstream signaling only occur after endocytic vesicle formation. Thus, TGF-βR endocytosis is not simply a way to dampen the signaling response but instead is required to propagate signaling via the Smad pathway.

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23

Mitchell, Hugh, Amit Choudhury, Richard E. Pagano, and Edward B. Leof. "Ligand-dependent and -independent Transforming Growth Factor-β Receptor Recycling Regulated by Clathrin-mediated Endocytosis and Rab11." Molecular Biology of the Cell 15, no. 9 (September 2004): 4166–78. http://dx.doi.org/10.1091/mbc.e04-03-0245.

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Proteins in the transforming growth factor-β (TGF-β) family recognize transmembrane serine/threonine kinases known as type I and type II receptors. Binding of TGF-β to receptors results in receptor down-regulation and signaling. Whereas previous work has focused on activities controlling TGF-β signaling, more recent studies have begun to address the trafficking properties of TGF-β receptors. In this report, it is shown that receptors undergo recycling both in the presence and absence of ligand activation, with the rates of internalization and recycling being unaffected by ligand binding. Recycling occurs as receptors are most likely internalized through clathrin-coated pits, and then returned to the plasma membrane via a rab11-dependent, rab4-independent mechanism. Together, the results suggest a mechanism wherein activated TGF-β receptors are directed to a distinct endocytic pathway for down-regulation and clathrin-dependent degradation after one or more rounds of recycling.

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24

Murphy, S. J., J. J. E. Doré, M. Edens, R. J. Coffey, J. A. Barnard, H. Mitchell, M. Wilkes, and E. B. Leof. "Differential Trafficking of Transforming Growth Factor-β Receptors and Ligand in Polarized Epithelial Cells." Molecular Biology of the Cell 15, no. 6 (June 2004): 2853–62. http://dx.doi.org/10.1091/mbc.e04-02-0097.

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Epithelial cells in vivo form tight cell-cell associations that spatially separate distinct apical and basolateral domains. These domains provide discrete cellular processes essential for proper tissue and organ development. Using confocal imaging and selective plasma membrane domain activation, the type I and type II transforming growth factor-β (TGFβ) receptors were found to be localized specifically at the basolateral surfaces of polarized Madin-Darby canine kidney (MDCK) cells. Receptors concentrated predominantly at the lateral sites of cell-cell contact, adjacent to the gap junctional complex. Cytoplasmic domain truncations for each receptor resulted in the loss of specific lateral domain targeting and dispersion to both the apical and basal domains. Whereas receptors concentrate basolaterally in regions of direct cell-cell contact in nonpolarized MDCK cell monolayers, receptor staining was absent from areas of noncell contact. In contrast to the defined basolateral polarity observed for the TGFβ receptor complex, TGFβ ligand secretion was found to be from the apical surfaces. Confocal imaging of MDCK cells with an antibody to TGFβ1 confirmed a predominant apical localization, with a stark absence at the basal membrane. These findings indicate that cell adhesion regulates the localization of TGFβ receptors in polarized epithelial cultures and that the response to TGFβ is dependent upon the spatial distribution and secretion of TGFβ receptors and ligand, respectively.

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Song, H., J. Papadimitriou, C. Drachenberg, M. R. Weir, and C. Wei. "Increase Transforming Growth Factor-Beta and its Receptors in Human Renal Tissue with Rejection." Microscopy and Microanalysis 6, S2 (August 2000): 614–15. http://dx.doi.org/10.1017/s143192760003556x.

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Transforming growth factor-bate (TGF-β) is a growth-relating peptide that has been shown to enhance collagen production in vivo and in vitro. TGF-β isoforms include TGF-β 1, β2 and β3. TGF-β receptors subtypes include type I (TGFβRI) and type II (TGFβRII) receptors. Overproduction of TGF-β can lead to real damage.Renal graft rejection is major problem after kidney transplantation with severe renal damage. We hypothesized that renal tissue level of TGF-β may increase in renal rejection after kidney transplantation. Therefore, the current study was designed to determine the TGF-β 1 isoform and its receptor TGFβRI in human renal tissue with rejection by immunohistochemical staining (IHCS) and compared with normal human renal tissue. The results of IHCS was evaluated by IHCS staining density scores (0, no staining; 1, minimal staining; 2, mild staining; 3, moderate staining; and 4, strong staining). The positive staining area (+%) in entire section was also determined. The sections treated with preabsorbed blocking peptide or nonimmune rabbit serum demonstrated no immunoperoxidase activity.

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Isoe, Shiro, Hirofumi Naganuma, Shin Nakano, Atsushi Sasaki, Eiji Satoh, Mitsuyasu Nagasaka, Shuichiro Maeda, and Hideaki Nukui. "Resistance to growth inhibition by transforming growth factor—β in malignant glioma cells with functional receptors." Journal of Neurosurgery 88, no. 3 (March 1998): 529–34. http://dx.doi.org/10.3171/jns.1998.88.3.0529.

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Object. The aim of this study was to investigate the mechanism by which malignant glioma cells escape from growth inhibition mediated by transforming growth factor-β (TGF-β), a ubiquitous cytokine that inhibits cell proliferation by causing growth arrest in the G1 phase of the cell cycle. Methods. The authors measured the response of eight malignant glioma cell lines to the growth-inhibiting activity of TGF-β in vitro and the expression of TGF-β Types I and II receptors in malignant glioma cells. The effect of TGF-β on the expression of a p27Kip1 cyclin-dependent kinase inhibitor was also investigated to assess the downstream signal transmission from TGF-β receptors. All malignant glioma cell lines were insensitive to growth inhibition by TGF-β1 and TGF-β2. Analyses of TGF-β receptors by means of affinity labeling in which 125I-TGF-β1 was used showed that six glioma lines had both TGF-β Types I and II receptors on their cell surfaces, whereas two lines had very small amounts of TGF-β Type I and/or Type II receptors. Northern blot analysis showed that all tumor lines expressed variable levels of messenger RNAs for both TGF-β Types I and II receptors. Flow cytometric analyses revealed that treatment of malignant glioma cells with TGF-β1 significantly downregulated the expression of p27Kip1 protein in all malignant glioma cell lines except one. Conclusions. The authors suggest that most malignant glioma cells express TGF-β Types I and II receptors, which can transmit some signals downstream and that the loss of response to TGF-β growth inhibition may not be caused by an abnormality of the TGF-β receptors.

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MOSEDALE, David E., and David J. GRAINGER. "An antibody present in normal human serum inhibits the binding of cytokines to their receptors in an in vitro system." Biochemical Journal 343, no. 1 (September 24, 1999): 125–33. http://dx.doi.org/10.1042/bj3430125.

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The presence of active transforming growth factor-β (TGF-β) in serum has not been widely accepted. In particular, although at least five studies have concluded that active TGF-β is present in normal human plasma and serum, assays that use the extracellular domain of the TGF-β type II receptor as a capture agent have given contradictory results. We show that there is an antagonist present in normal human serum which inhibits the binding of active TGF-β to the extracellular domain of the TGF-β type II receptor when it is coated on the well of an ELISA plate. This antagonist activity is due to a pool of immunoglobulins of the G2, D and M classes. Moreover, we show that this same pool of immunoglobulins also recognizes the extracellular domain of the platelet-derived growth factor α-receptor, insulin-like growth factor-1 receptor and interleukin-3 receptor, by serial transfer of serum over the different receptors. In addition, the same immunoglobulin pool inhibits the binding of platelet-derived growth factor-AA to its receptor, in an analogous way to the inhibition of binding of TGF-β to its type II receptor. Circumstantial evidence suggests that the pool of immunoglobulins is recognizing a carbohydrate residue that is attached to the protein when it is synthesized by the mouse myeloma cell line, NSO, in which it is made. If the cytokine receptors are similarly glycosylated in vivo, then the presence of these antibodies in normal human serum may modulate physiological cytokine signalling.

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Bira, Yanjmaa, Kenji Tani, Yasuhiko Nishioka, Junya Miyata, Keiko Sato, Akihito Hayashi, Yutaka Nakaya, and Saburo Sone. "Transforming growth factor β stimulates rheumatoid synovial fibroblasts via the type II receptor." Modern Rheumatology 15, no. 2 (April 2005): 108–13. http://dx.doi.org/10.3109/s10165-004-0378-2.

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29

Brattain, Michael G., Sanford D. Markowitz, and James K. V. Willson. "The type II transforming growth factor-β receptor as a tumor-suppressor gene." Current Opinion in ONCOLOGY 8, no. 1 (January 1996): 49–53. http://dx.doi.org/10.1097/00001622-199601000-00009.

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Wang, DanHui, LuZhe Sun, Elizabeth Zborowska, James K. V. Willson, Jiangen Gong, Janaki Verraraghavan, and Michael G. Brattain. "Control of Type II Transforming Growth Factor-β Receptor Expression by Integrin Ligation." Journal of Biological Chemistry 274, no. 18 (April 30, 1999): 12840–47. http://dx.doi.org/10.1074/jbc.274.18.12840.

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31

Goetschy, Jean-Francois, Odile Letourneur, Nico Cerletti, and Michel A. Horisberger. "The Unglycosylated Extracellular Domain of Type-II Receptor for Transforming Growth Factor-β." European Journal of Biochemistry 241, no. 2 (October 1996): 355–62. http://dx.doi.org/10.1111/j.1432-1033.1996.00355.x.

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32

Agarwal, Rajiv, Senthuran Siva, Stephen R. Dunn, and Kumar Sharma. "Add-on angiotensin II receptor blockade lowers urinary transforming growth factor-β levels." American Journal of Kidney Diseases 39, no. 3 (March 2002): 486–92. http://dx.doi.org/10.1053/ajkd.2002.31392.

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33

Li, Min, Changgong Li, Yi-hsin Liu, Yiming Xing, Lingyan Hu, Zea Borok, Kenny Y. C. Kwong, and Parviz Minoo. "Mesodermal Deletion of Transforming Growth Factor-β Receptor II Disrupts Lung Epithelial Morphogenesis." Journal of Biological Chemistry 283, no. 52 (November 6, 2008): 36257–64. http://dx.doi.org/10.1074/jbc.m806786200.

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34

Jakowlew, Sonia B., Terry W. Moody, Liang You, and Jennifer M. Mariano. "Reduction in transforming growth factor-β type II receptor in mouse lung carcinogenesis." Molecular Carcinogenesis 22, no. 1 (May 1998): 46–56. http://dx.doi.org/10.1002/(sici)1098-2744(199805)22:1<46::aid-mc6>3.0.co;2-j.

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35

Sokol, Jonathan P., and William P. Schiemann. "Cystatin C Antagonizes Transforming Growth Factor β Signaling in Normal and Cancer Cells." Molecular Cancer Research 2, no. 3 (March 1, 2004): 183–95. http://dx.doi.org/10.1158/1541-7786.183.2.3.

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Abstract Cystatin C (CystC) is a secreted cysteine protease inhibitor that regulates bone resorption, neutrophil chemotaxis, and tissue inflammation, as well as resistance to bacterial and viral infections. CystC is ubiquitously expressed and present in most bodily fluids where it inhibits the activities of cathepsins, a family of cysteine proteases that can promote cancer cell invasion and metastasis. Transforming growth factor β (TGF-β) is a multifunctional cytokine endowed with both tumor-suppressing and tumor-promoting activities. We show herein that TGF-β treatment up-regulated CystC transcript and protein in murine 3T3-L1 fibroblasts. Moreover, CystC mRNA expression was down-regulated in ∼50% of human malignancies, particularly cancers of the stomach, uterus, colon, and kidney. Overexpression of CystC in human HT1080 fibrosarcoma cells antagonized their invasion through synthetic basement membranes in part via a cathepsin-dependent pathway. Independent of effects on cathepsin activity, CystC also reduced HT1080 cell gene expression stimulated by TGF-β. Invasion of 3T3-L1 cells occurred through both cathepsin- and TGF-β-dependent pathways. Both pathways were blocked by CystC, but only the TGF-β-dependent pathway was blocked by a CystC mutant (i.e., Δ14CystC) that is impaired in its ability to inhibit cathepsin activity. Moreover, CystC and Δ14CystC both inhibited 3T3-L1 cell gene expression stimulated by TGF-β. We further show that CystC antagonized TGF-β binding to its cell surface receptors, doing so by interacting physically with the TGF-β type II receptor and antagonizing its binding of TGF-β. Collectively, our findings have identified CystC as a novel TGF-β receptor antagonist, as well as a novel CystC-mediated feedback loop that inhibits TGF-β signaling.

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Tian, Ya Chung, and Aled Owain Phillips. "Interaction between the Transforming Growth Factor-β Type II Receptor/Smad Pathway and β-Catenin during Transforming Growth Factor-β1-Mediated Adherens Junction Disassembly." American Journal of Pathology 160, no. 5 (May 2002): 1619–28. http://dx.doi.org/10.1016/s0002-9440(10)61109-1.

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37

Zhao, Yun, and Stephen L. Young. "Requirement of Transforming Growth Factor-β (TGF-β) Type II Receptor for TGF-β-induced Proliferation and Growth Inhibition." Journal of Biological Chemistry 271, no. 5 (February 1996): 2369–72. http://dx.doi.org/10.1074/jbc.271.5.2369.

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38

Wehrenberg, Uwe, Jürgen Giebel, and Gabriele M. Rune. "Possible involvement of transforming growth factor-β1 and transforming growth factor-β receptor type II during luteinization in the marmoset ovary." Tissue and Cell 30, no. 3 (June 1998): 360–67. http://dx.doi.org/10.1016/s0040-8166(98)80049-9.

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39

Yao, Diying, Marcelo Ehrlich, Yoav I. Henis, and Edward B. Leof. "Transforming Growth Factor-β Receptors Interact with AP2 by Direct Binding to β2 Subunit." Molecular Biology of the Cell 13, no. 11 (November 2002): 4001–12. http://dx.doi.org/10.1091/mbc.02-07-0104.

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Transforming growth factor-β (TGF-β) superfamily members regulate a wide range of biological processes by binding to two transmembrane serine/threonine kinase receptors, type I and type II. We have previously shown that the internalization of these receptors is inhibited by K+ depletion, cytosol acidification, or hypertonic medium, suggesting the involvement of clathrin-coated pits. However, the involvement of the clathrin-associated adaptor complex AP2 and the identity of the AP2 subunit that binds the receptors were not known. Herein, we have studied these issues by combining studies on intact cells with in vitro assays. Using fluorescence photobleaching recovery to measure the lateral mobility of the receptors on live cells (untreated or treated to alter their coated pit structure), we demonstrated that their mobility is restricted by interactions with coated pits. These interactions were transient and mediated through the receptors' cytoplasmic tails. To measure direct binding of the receptors to specific AP2 subunits, we used yeast two-hybrid screens and in vitro biochemical assays. In contrast to most other plasma membrane receptors that bind to AP2 via the μ2 subunit, AP2/TGF-β receptor binding was mediated by a direct interaction between the β2-adaptin N-terminal trunk domain and the cytoplasmic tails of the receptors; no binding was observed to the μ2, α, or ς2 subunits of AP2 or to μ1 of AP1. The data uniquely demonstrate both in vivo and in vitro the ability of β2-adaptin to directly couple TGF-β receptors to AP2 and to clathrin-coated pits, providing the first in vivo evidence for interactions of a transmembrane receptor with β2-adaptin.

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40

Suszko, Magdalena I., and Teresa K. Woodruff. "Cell-specificity of transforming growth factor-β response is dictated by receptor bioavailability." Journal of Molecular Endocrinology 36, no. 3 (June 2006): 591–600. http://dx.doi.org/10.1677/jme.1.01936.

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Members of the transforming growth factor-β (TGFβ) family control diverse cellular responses including differentiation, proliferation, controlled cell death and migration. The response of a cell to an individual ligand is highly restricted yet the signaling pathways for TGFβ, activin and bone morphogenic proteins share a limited number of receptors and activate similar intracellular cytoplasmic co-regulators, Smads. A central question in the study of this family of ligands is how cells titrate and integrate each TGFβ-like signal in order to respond in a cell- and ligand-specific manner. This study uses the pituitary gonadotrope cell line, LβT2, as a model to delineate the relative contribution of TGFβ and activin ligands to follicle-stimulating hormone (FSH) biosynthesis. It was found that pituitary gonadotrope cells do not express the TGFβ type II (TβRII) receptor and are therefore not responsive to the TGFβ ligand. Transfection of the receptor restores TGFβ signaling capabilities and the TGFβ-mediated stimulation of FSHβ gene transcription in LβT2 cells. Consequently, we evaluated the presence of the TβRII in the adult mouse pituitary. TβRII does not co-localize with FSH-producing cells; however it is detected on the cell surface of prolactin- and growth hormone-positive cells. Taken together, these results suggest that the bioavailability of the TGFβ-specific receptor rather than TGFβ dictates pituitary gonadotrope selectivity to activin, which is necessary to maintain normal reproductive function. It is likely that the ligand-restricted mechanisms employed by the gonadotrope are present in other cells, which could explain the distinct control of many cellular processes by members of the TGFβ superfamily.

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41

Bollard, Catherine M., Claudia Rössig, M. Julia Calonge, M. Helen Huls, Hans-Joachim Wagner, Joan Massague, Malcolm K. Brenner, Helen E. Heslop, and Cliona M. Rooney. "Adapting a transforming growth factor β–related tumor protection strategy to enhance antitumor immunity." Blood 99, no. 9 (May 1, 2002): 3179–87. http://dx.doi.org/10.1182/blood.v99.9.3179.

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Abstract Transforming growth factor β (TGF-β), a pleiotropic cytokine that regulates cell growth and differentiation, is secreted by many human tumors and markedly inhibits tumor-specific cellular immunity. Tumors can avoid the differentiating and apoptotic effects of TGF-β by expressing a nonfunctional TGF-β receptor. We have determined whether this immune evasion strategy can be manipulated to shield tumor-specific cytotoxic T lymphocytes (CTLs) from the inhibitory effects of tumor-derived TGF-β. As our model we used Epstein-Barr virus (EBV)–specific CTLs that are infused as treatment for EBV-positive Hodgkin disease but that are vulnerable to the TGF-β produced by this tumor. CTLs were transduced with a retrovirus vector expressing the dominant-negative TGF-β type II receptor HATGF-βRII-Δcyt. HATGF-βRII-Δcyt– but not green fluorescence protein (eGFP)–transduced CTLs was resistant to the antiproliferative and anticytotoxic effects of exogenous TGF-β. Additionally, receptor-transduced cells continued to secrete cytokines in response to antigenic stimulation. TGF-β receptor ligation results in phosphorylation of Smad2, and this pathway was disrupted in HATGF-βRII-Δcyt–transduced CTLs, confirming blockade of the signal transduction pathway. Long-term expression of TGF-βRII-Δcyt did not affect CTL function, phenotype, or growth characteristics. Tumor-specific CTLs expressing HATGF-βRII-Δcyt should have a selective functional and survival advantage over unmodified CTLs in the presence of TGF-β–secreting tumors and may be of value in treatment of these diseases.

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42

Takarada, Masanori. "Functional Analysis of Transforming Growth Factor-.BETA. type II Dominant Negative Receptor." JOURNAL OF THE STOMATOLOGICAL SOCIETY,JAPAN 63, no. 2 (1996): 375–86. http://dx.doi.org/10.5357/koubyou.63.375.

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43

Buck, Miriam B., Peter Fritz, Juergen Dippon, Gerhard Zugmaier, and Cornelius Knabbe. "Prognostic Significance of Transforming Growth Factor β Receptor II in Estrogen Receptor-Negative Breast Cancer Patients." Clinical Cancer Research 10, no. 2 (January 15, 2004): 491–98. http://dx.doi.org/10.1158/1078-0432.ccr-0320-03.

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44

Cheng, Nikki, Anna Chytil, Yu Shyr, Alison Joly, and Harold L. Moses. "Enhanced Hepatocyte Growth Factor Signaling by Type II Transforming Growth Factor-β Receptor Knockout Fibroblasts Promotes Mammary Tumorigenesis." Cancer Research 67, no. 10 (May 10, 2007): 4869–77. http://dx.doi.org/10.1158/0008-5472.can-06-3381.

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45

Chowdhury, Sanjib. "Epigenetic Targeting of Transforming Growth Factor β Receptor II and Implications for Cancer Therapy." Molecular and Cellular Pharmacology 1, no. 1 (February 10, 2009): 57–70. http://dx.doi.org/10.4255/mcpharmacol.09.07.

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46

Miwa, Shohei, Masahiro Yokota, Yoshifumi Ueyama, Katsuya Maeda, Yosuke Ogoshi, Noriyoshi Seki, Naoki Ogawa, et al. "Discovery of Selective Transforming Growth Factor β Type II Receptor Inhibitors as Antifibrosis Agents." ACS Medicinal Chemistry Letters 12, no. 5 (April 21, 2021): 745–51. http://dx.doi.org/10.1021/acsmedchemlett.0c00679.

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47

Lin, Herbert Y., Aristidis Moustakas, Petra Knaus, Rebecca G. Wells, Yoav I. Henis, and Harvey F. Lodish. "The Soluble Exoplasmic Domain of the Type II Transforming Growth Factor (TGF)-β Receptor." Journal of Biological Chemistry 270, no. 6 (February 10, 1995): 2747–54. http://dx.doi.org/10.1074/jbc.270.6.2747.

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48

Zheng, Huaien, Junru Wang, Victor E. Koteliansky, Philip J. Gotwals, and Martin Hauer–Jensen. "Recombinant soluble transforming growth factor β type II receptor ameliorates radiation enteropathy in mice." Gastroenterology 119, no. 5 (November 2000): 1286–96. http://dx.doi.org/10.1053/gast.2000.19282.

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49

Yamashita, Satoshi, Satoru Takahashi, Nathalie McDonell, Naoko Watanabe, Tohru Niwa, Kosuke Hosoya, Yoshimi Tsujino, Tomoyuki Shirai, and Toshikazu Ushijima. "Methylation Silencing of Transforming Growth Factor-β Receptor Type II in Rat Prostate Cancers." Cancer Research 68, no. 7 (April 1, 2008): 2112–21. http://dx.doi.org/10.1158/0008-5472.can-07-5282.

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50

Izumoto, Shuichi, Norio Arita, Takanori Ohnishi, Shoju Hiraga, Takuyu Taki, Naohiro Tomita, Masayuki Ohue, and Toru Hayakawa. "Microsatellite instability and mutated type II transforming growth factor-β receptor gene in gliomas." Cancer Letters 112, no. 2 (January 1997): 251–56. http://dx.doi.org/10.1016/s0304-3835(96)04583-1.

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