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Phosphorylation of Smad signaling proteins by receptor serine/threonine kinases
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Medicinska och farmaceutiska vetenskapsområdet, centrumbildningar mm, Ludwig Institute for Cancer Research.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Medicinska och farmaceutiska vetenskapsområdet, centrumbildningar mm, Ludwig Institute for Cancer Research.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Medicinska och farmaceutiska vetenskapsområdet, centrumbildningar mm, Ludwig Institute for Cancer Research.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Medicinska och farmaceutiska vetenskapsområdet, centrumbildningar mm, Ludwig Institute for Cancer Research.
2001 (English)In: Protein Kinase Protocols / [ed] Alastair D. Reith, Humana Press, 2001, Vol. 124, 107-120 p.Chapter in book (Other academic)
Abstract [en]

Transforming growth factor-β (TGF-β) family members, which include TGF-βs, activins, and bone morphogenetic proteins (BMPs), elicit their multifunctional effects by binding to and complex formation of type I and type II serine/threonine kinase receptors (see Fig. 1). Each family member signals via distinct combinations of type I and type II receptors, both of which are required for signaling. Upon formation of the heteromeric receptor complex, the type I receptor is phosphorylated by the type II receptor kinase. Phosphorylation occurs predominantly in a region rich in glycine and serine residues (GS domain) in the juxtamembrane domain of the type I receptor, which possibly leads to a conformational change and thereby activates the type I receptor kinase (see Fig. 1) (1–3). The activated type I receptor propagates the signal downstream through transient interaction with, and phosphorylation of, particular Smoeand mad related protein (Smad) molecules (1–3). Certain Smads are phosphorylated directly by activated type I receptors in a differential manner; they are therefore termed pathway-restricted Smads. Whereas Smad2 and Smad3 act in TGF-β and activin pathways, Smad1, Smad5, and Smad8 are thought to act in BMP pathways. Phosphorylation occurs at the two most C-terminal serine residues in a conserved C-terminal Ser-Ser-X-Ser motif (see Fig. 2). Pathway-restricted Smads oligomerize with Smad4, which acts as a common mediator in TGF-β, activin, and BMP signaling. After translocation to the nucleus, the oligomers interact with DNA directly, or in complex with other DNA-binding proteins, and control transcription of target genes (see Figs. 1 and 2). Recently, inhibitory Smads, Smad6, and Smad7, have been identified that antagonize TGF-β family signaling (3). Fig. 1.

Place, publisher, year, edition, pages
Humana Press, 2001. Vol. 124, 107-120 p.
Series
Methods in Molecular Biology, ISSN 1064-3745 ; 124
Keyword [en]
Animals, Blotting; Western/methods, COS Cells, Cell Line, Cercopithecus aethiops, DNA-Binding Proteins/*metabolism, Electrophoresis; Gel; Two-Dimensional/methods, Phosphates/metabolism, Phosphopeptides/chemistry, Phosphoproteins/chemistry/*metabolism, Phosphorus Radioisotopes, Phosphorylation, Protein-Serine-Threonine Kinases/*metabolism, Receptors; Cell Surface/metabolism, Recombinant Proteins/metabolism, Signal Transduction/*physiology, Trans-Activators/*metabolism, Transfection/methods, Transforming Growth Factor beta/*physiology
National Category
Medical and Health Sciences
Identifiers
URN: urn:nbn:se:uu:diva-73365DOI: 10.1385/1-59259-059-4:107PubMedID: 11100470ISBN: 978-0-89603-700-7 (print)ISBN: 978-1-59259-059-9 (print)OAI: oai:DiVA.org:uu-73365DiVA: diva2:101275
Available from: 2005-06-02 Created: 2005-06-02 Last updated: 2013-11-07Bibliographically approved

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Souchelnytskyi, SerhiyHeldin, Carl-Henrikten Dijke, Peter

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