scholarly journals NM23-H1 Tumor Suppressor Physically Interacts with Serine-Threonine Kinase Receptor-associated Protein, a Transforming Growth Factor-β (TGF-β) Receptor-interacting Protein, and Negatively Regulates TGF-β Signaling

2007 ◽  
Vol 282 (16) ◽  
pp. 12075-12096 ◽  
Author(s):  
Hyun-A Seong ◽  
Haiyoung Jung ◽  
Hyunjung Ha
Keyword(s):  
Growth Factor ◽  
Tumor Suppressor ◽  
Transforming Growth Factor ◽  
Protein A ◽  
Transforming Growth Factor Β ◽  
Serine Threonine Kinase ◽  
Interacting Protein ◽  
Receptor Associated Protein ◽  
Threonine Kinase ◽  
Β Receptor

Reversible ubiquitination regulates the Smad/TGF-β signalling pathway

2006 ◽  
Vol 34 (5) ◽  
pp. 761-763 ◽  
Author(s):  
S.J. Wicks ◽  
T. Grocott ◽  
K. Haros ◽  
M. Maillard ◽  
P. ten Dijke ◽  
...  
Keyword(s):  
Transforming Growth Factor ◽  
Transforming Growth Factor Β ◽  
Type I ◽  
Serine Threonine Kinase ◽  
Full Spectrum ◽  
Threonine Kinase ◽  
Pathological Conditions ◽  
C Terminus ◽  
Β Receptor ◽  
Fine Tune

TGF-β (transforming growth factor-β) signals through serine/threonine kinase receptors and intracellular Smad transcription factors. An important regulatory step involves specific ubiquitination by Smurfs (Smad–ubiquitin regulatory factors), members of the HECT (homologous to E6-associated protein C-terminus) ubiquitin ligase family, which mediate the proteasomal degradation of Smads and/or receptors. Recently, we have defined a novel interaction between Smads and UCH37 (ubiquitin C-terminal hydrolase 37), a DUB (de-ubiquitinating enzyme) that could potentially counteract Smurf-mediated ubiquitination. We have demonstrated specific interactions between UCH37 and inhibitory Smad7, as well as weaker associations with Smad2 and Smad3. Importantly, Smad7 can act as an adaptor able to recruit UCH37 to the type I TGF-β receptor. Consequently, UCH37 dramatically up-regulates TGF-β-dependent gene expression by de-ubiquitinating and stabilizing the type I TGF-β receptor. Our findings suggest that competing effects of ubiquitin ligases and DUBs in complex with Smad7 can serve to fine-tune responses to TGF-βs under various physiological and pathological conditions. Studies are currently under way using activity-based HA (haemagglutinin)-tagged ubiquitin probes to identify the full spectrum of DUBs that impact on Smad/TGF-β signalling activity.

scholarly journals Transforming Growth Factor-β Receptor-associated Protein 1 Is a Smad4 Chaperone

2001 ◽  
Vol 276 (22) ◽  
pp. 19495-19502 ◽  
Author(s):  
Jens U. Wurthner ◽  
David B. Frank ◽  
Angelina Felici ◽  
Harry M. Green ◽  
Zhouhong Cao ◽  
...  
Keyword(s):  
Growth Factor ◽  
Transforming Growth Factor ◽  
Transforming Growth Factor Β ◽  
Receptor Associated Protein ◽  
Β Receptor

scholarly journals Single-molecule imaging reveals transforming growth factor-β-induced type II receptor dimerization

2009 ◽  
Vol 106 (37) ◽  
pp. 15679-15683 ◽  
Author(s):  
Wei Zhang ◽  
Yaxin Jiang ◽  
Qiang Wang ◽  
Xinyong Ma ◽  
Zeyu Xiao ◽  
...  
Keyword(s):  
Growth Factor ◽  
Single Molecule ◽  
Transforming Growth Factor ◽  
Transforming Growth Factor Β ◽  
Receptor Activation ◽  
General Mechanism ◽  
Type Ii ◽  
Serine Threonine Kinase ◽  
Receptor Dimerization ◽  
Threonine Kinase

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.

A Transforming Growth Factor-β Receptor–Interacting Protein Frequently Mutated in Human Ovarian Cancer

2005 ◽  
Vol 65 (15) ◽  
pp. 6526-6533 ◽  
Author(s):  
Wei Ding ◽  
Qian Tang ◽  
Virginia Espina ◽  
Lance A. Liotta ◽  
David T. Mauger ◽  
...  
Keyword(s):  
Ovarian Cancer ◽  
Growth Factor ◽  
Transforming Growth Factor ◽  
Transforming Growth Factor Β ◽  
Human Ovarian Cancer ◽  
Interacting Protein ◽  
Β Receptor

scholarly journals The Type III Transforming Growth Factor-β Receptor as a Novel Tumor Suppressor Gene in Prostate Cancer

2007 ◽  
Vol 67 (3) ◽  
pp. 1090-1098 ◽  
Author(s):  
Ryan S. Turley ◽  
Elizabeth C. Finger ◽  
Nadine Hempel ◽  
Tam How ◽  
Timothy A. Fields ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Growth Factor ◽  
Tumor Suppressor ◽  
Tumor Suppressor Gene ◽  
Transforming Growth Factor ◽  
Transforming Growth Factor Β ◽  
Suppressor Gene ◽  
Type Iii ◽  
Β Receptor
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