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Angaben zur Quelle [Bearbeiten]

Autor     Gregory J Anderson, Deepak Darshan
Titel    Small-molecule dissection of BMP signaling
Zeitschrift    Nature Chemical Biology
Verlag    Nature Publishing Group
Ausgabe    4
Jahr    2008
Seiten    15-16
DOI    10.1038/nchembio0108-15
URL    http://www.nature.com/nchembio/journal/v4/n1/full/nchembio0108-15.html

Literaturverz.   

ja
Fußnoten    ja
Fragmente    1


Fragmente der Quelle:
[1.] Src/Fragment 017 07 - Diskussion
Zuletzt bearbeitet: 2014-09-27 20:22:12 Kybot
Anderson and Darshan 2008, BauernOpfer, Fragment, SMWFragment, Schutzlevel, Src, ZuSichten

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Seite: 17, Zeilen: Abbildung
Quelle: Anderson and Darshan 2008
Seite(n): 15, Zeilen: Abbildung
Scr 017a diss.png

Fig. 1.8. BMP signalling: The BMPs bind to type I and II receptors and facilitate their association. The constitutively active kinase domains of type II receptors phosphorylate type I receptors, and this in turn activates the SMAD signaling pathway through phosphorylation of receptor SMADs (SMAD1, SMAD5 and SMAD8). These associate with co-SMADs (SMAD4) to form a heteromeric complex that translocates to the nucleus and stimulates the expression of a wide range of target genes. BMPs can also signal through SMAD-independent pathways, notably via MAP kinases. Dorsomorphin inhibits BMP signaling through the SMAD pathway, likely by affecting BMPR-I kinase activity. Many of the previously known inhibitors of BMP signaling (such as noggin and chordin) act upstream to sequester BMPs and cannot differentiate SMAD-dependent from SMAD-independent signaling. (Modified from Anderson and Darshan et al 2008).

Scr 017a source.png

Figure 1 The BMPs bind to type I and II receptors and facilitate their association. The constitutively active kinase domains of type II receptors phosphorylate type I receptors, and this in turn activates the SMAD signaling pathway through phosphorylation of receptor SMADs (SMAD1, SMAD5 and SMAD8). These associate with co-SMADs (SMAD4) to form a heteromeric complex that translocates to the nucleus and stimulates the expression of a wide range of target genes, including the gene encoding the iron regulatory peptide hepcidin. BMPs can also signal through SMAD-independent pathways, notably via MAP kinases. Dorsomorphin inhibits BMP signaling through the SMAD pathway, likely by affecting BMPR-I kinase activity. Many of the previously known inhibitors of BMP signaling (such as noggin and chordin) act upstream to sequester BMPs and cannot differentiate SMAD-dependent from SMAD-independent signaling. The activation of the hepcidin gene by IL-6 requires both the JAK-STAT and BMP-SMAD pathways, but how the pathways interact is unclear. Similarly, TfR2 and the HFE–TfR1 complex can alter hepcidin expression, but it is not known whether their functions require the BMPSMAD system. Modified from ref. 10.

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