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  • 1
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    Structural basis of Smad2 recognition by the Smad anchor for receptor activation (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-12-30
    Description: The Smad proteins mediate transforming growth factor-beta (TGFbeta) signaling from the transmembrane serine-threonine receptor kinases to the nucleus. The Smad anchor for receptor activation (SARA) recruits Smad2 to the TGFbeta receptors for phosphorylation. The crystal structure of a Smad2 MH2 domain in complex with the Smad-binding domain (SBD) of SARA has been determined at 2.2 angstrom resolution. SARA SBD, in an extended conformation comprising a rigid coil, an alpha helix, and a beta strand, interacts with the beta sheet and the three-helix bundle of Smad2. Recognition between the SARA rigid coil and the Smad2 beta sheet is essential for specificity, whereas interactions between the SARA beta strand and the Smad2 three-helix bundle contribute significantly to binding affinity. Comparison of the structures between Smad2 and a comediator Smad suggests a model for how receptor-regulated Smads are recognized by the type I receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wu, G -- Chen, Y G -- Ozdamar, B -- Gyuricza, C A -- Chong, P A -- Wrana, J L -- Massague, J -- Shi, Y -- CA85171/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2000 Jan 7;287(5450):92-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Princeton University, Lewis Thomas Laboratory, Princeton, NJ 08544, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10615055" target="_blank"〉PubMed〈/a〉
    Keywords: *Activin Receptors, Type I ; Amino Acid Sequence ; Binding Sites ; Carrier Proteins/*chemistry/*metabolism ; Crystallography, X-Ray ; DNA-Binding Proteins/*chemistry/genetics/*metabolism ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Phosphorylation ; Point Mutation ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein-Serine-Threonine Kinases/chemistry/genetics/metabolism ; Receptors, Transforming Growth Factor beta/chemistry/genetics/metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; Signal Transduction ; Smad2 Protein ; Trans-Activators/*chemistry/genetics/*metabolism ; Zinc Fingers
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Regulation of cell polarity and protrusion formation by targeting RhoA for degradation (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-12-06
    Description: The Rho family of small guanosine triphosphatases regulates actin cytoskeleton dynamics that underlie cellular functions such as cell shape changes, migration, and polarity. We found that Smurf1, a HECT domain E3 ubiquitin ligase, regulated cell polarity and protrusive activity and was required to maintain the transformed morphology and motility of a tumor cell. Atypical protein kinase C zeta (PKCzeta), an effector of the Cdc42/Rac1-PAR6 polarity complex, recruited Smurf1 to cellular protrusions, where it controlled the local level of RhoA. Smurf1 thus links the polarity complex to degradation of RhoA in lamellipodia and filopodia to prevent RhoA signaling during dynamic membrane movements.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Hong-Rui -- Zhang, Yue -- Ozdamar, Barish -- Ogunjimi, Abiodun A -- Alexandrova, Evguenia -- Thomsen, Gerald H -- Wrana, Jeffrey L -- HD32429/HD/NICHD NIH HHS/ -- R01 HD032429/HD/NICHD NIH HHS/ -- R01 HD032429-06/HD/NICHD NIH HHS/ -- R01 HD032429-07/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 2003 Dec 5;302(5651):1775-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Molecular Biology and Cancer, Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto M56 1x5, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14657501" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cell Line, Tumor ; Cell Membrane/metabolism/physiology ; *Cell Movement ; *Cell Polarity ; Cell Size ; Cell Transformation, Neoplastic ; Cytoskeleton/ultrastructure ; Guanine Nucleotide Exchange Factors/metabolism ; Humans ; Intercellular Junctions/metabolism ; Mice ; NIH 3T3 Cells ; Protein Kinase C/metabolism ; Protein Structure, Tertiary ; Pseudopodia/*metabolism/ultrastructure ; RNA, Small Interfering ; Signal Transduction ; Transfection ; Ubiquitin-Protein Ligases/chemistry/genetics/*metabolism ; cdc42 GTP-Binding Protein/metabolism ; rhoA GTP-Binding Protein/genetics/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    High-throughput mapping of a dynamic signaling network in mammalian cells (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-03-12
    Description: Signaling pathways transmit information through protein interaction networks that are dynamically regulated by complex extracellular cues. We developed LUMIER (for luminescence-based mammalian interactome mapping), an automated high-throughput technology, to map protein-protein interaction networks systematically in mammalian cells and applied it to the transforming growth factor-beta (TGFbeta) pathway. Analysis using self-organizing maps and k-means clustering identified links of the TGFbeta pathway to the p21-activated kinase (PAK) network, to the polarity complex, and to Occludin, a structural component of tight junctions. We show that Occludin regulates TGFbeta type I receptor localization for efficient TGFbeta-dependent dissolution of tight junctions during epithelial-to-mesenchymal transitions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barrios-Rodiles, Miriam -- Brown, Kevin R -- Ozdamar, Barish -- Bose, Rohit -- Liu, Zhong -- Donovan, Robert S -- Shinjo, Fukiko -- Liu, Yongmei -- Dembowy, Joanna -- Taylor, Ian W -- Luga, Valbona -- Przulj, Natasa -- Robinson, Mark -- Suzuki, Harukazu -- Hayashizaki, Yoshihide -- Jurisica, Igor -- Wrana, Jeffrey L -- P50 GM-62413/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Mar 11;307(5715):1621-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Molecular Biology and Cancer, Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, Canada, M5G 1X5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15761153" target="_blank"〉PubMed〈/a〉
    Keywords: Activin Receptors, Type I/metabolism ; Animals ; Cell Line ; Cell Polarity ; DNA-Binding Proteins/metabolism ; Epithelial Cells/cytology/physiology ; Humans ; Immunoprecipitation ; Luciferases ; Membrane Proteins/metabolism ; Mesoderm/cytology ; Mice ; Occludin ; Phosphorylation ; *Protein Interaction Mapping ; Protein-Serine-Threonine Kinases/metabolism ; Receptors, Transforming Growth Factor beta/metabolism ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; Smad2 Protein ; Smad4 Protein ; Tight Junctions/ultrastructure ; Trans-Activators/metabolism ; Transforming Growth Factor beta/*metabolism ; p21-Activated Kinases
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 4
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    Regulation of the polarity protein Par6 by TGFbeta receptors controls epithelial cell plasticity (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-03-12
    Description: The transition of cells from an epithelial to a mesenchymal phenotype is a critical event during morphogenesis in multicellular organisms and underlies the pathology of many diseases, including the invasive phenotype associated with metastatic carcinomas. Transforming growth factor beta (TGFbeta) is a key regulator of epithelial-to-mesenchymal transition (EMT). However, the molecular mechanisms that control the dissolution of tight junctions, an early event in EMT, remain elusive. We demonstrate that Par6, a regulator of epithelial cell polarity and tight-junction assembly, interacts with TGFbeta receptors and is a substrate of the type II receptor, TbetaRII. Phosphorylation of Par6 is required for TGFbeta-dependent EMT in mammary gland epithelial cells and controls the interaction of Par6 with the E3 ubiquitin ligase Smurf1. Smurf1, in turn, targets the guanosine triphosphatase RhoA for degradation, thereby leading to a loss of tight junctions. These studies define how an extracellular cue signals to the polarity machinery to control epithelial cell morphology.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ozdamar, Barish -- Bose, Rohit -- Barrios-Rodiles, Miriam -- Wang, Hong-Rui -- Zhang, Yue -- Wrana, Jeffrey L -- New York, N.Y. -- Science. 2005 Mar 11;307(5715):1603-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medical Genetics and Microbiology, University of Toronto, Toronto, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15761148" target="_blank"〉PubMed〈/a〉
    Keywords: Activin Receptors, Type I/*metabolism ; Amino Acid Sequence ; Animals ; Cell Line ; Cell Polarity ; DNA-Binding Proteins/metabolism ; Epithelial Cells/*cytology/*physiology ; Humans ; Mesoderm/cytology ; Mice ; Models, Biological ; Molecular Sequence Data ; Mutation ; Phosphorylation ; Protein Binding ; Protein Kinase C/metabolism ; Protein Kinase C-epsilon ; Protein-Serine-Threonine Kinases ; Proteins/genetics/*metabolism ; Receptors, Transforming Growth Factor beta/*metabolism ; Smad2 Protein ; Tight Junctions/metabolism/ultrastructure ; Trans-Activators/metabolism ; Transforming Growth Factor beta/metabolism/pharmacology ; Ubiquitin-Protein Ligases/metabolism ; rhoA GTP-Binding Protein/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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