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Phosphorylation of ...
Phosphorylation of Smad signaling proteins by receptor serine/threonine kinases
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- Souchelnytskyi, Serhiy (författare)
- Uppsala universitet,Ludwiginstitutet för cancerforskning
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- Rönnstrand, Lars (författare)
- Uppsala universitet,Ludwiginstitutet för cancerforskning
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- Heldin, Carl-Henrik (författare)
- Uppsala universitet,Ludwiginstitutet för cancerforskning
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- ten Dijke, Peter (författare)
- Uppsala universitet,Ludwiginstitutet för cancerforskning
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(creator_code:org_t)
- New Jersey : Humana Press, 2001
- 2001
- Engelska.
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Ingår i: Protein Kinase Protocols. - New Jersey : Humana Press. - 9780896037007 - 9781592590599 ; , s. 107-120
- Relaterad länk:
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http://www.ncbi.nlm....
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- 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.
Nyckelord
- 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
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