Smad linker region phosphorylation in the regulation of extracellular matrix synthesis

Burch, Micah L., Zheng, Wenhua and Little, Peter J. (2011) Smad linker region phosphorylation in the regulation of extracellular matrix synthesis. Cellular and Molecular Life Sciences, 68 1: 97-107. doi:10.1007/s00018-010-0514-4


Author Burch, Micah L.
Zheng, Wenhua
Little, Peter J.
Title Smad linker region phosphorylation in the regulation of extracellular matrix synthesis
Journal name Cellular and Molecular Life Sciences   Check publisher's open access policy
ISSN 1420-682X
1420-9071
Publication date 2011-01
Sub-type Critical review of research, literature review, critical commentary
DOI 10.1007/s00018-010-0514-4
Open Access Status Not Open Access
Volume 68
Issue 1
Start page 97
End page 107
Total pages 11
Place of publication Basel, Switzerland
Publisher Springer Basel
Language eng
Abstract The canonical TGF-β signalling pathway involves Smad transcription factors through direct serine phosphorylation of the carboxy termini, nuclear translocation and regulation of transcription by receptor-regulated (R)-Smad complexes. Smads can also be phosphorylated in the linker region most prominently by the action of mitogen-activated protein (MAP) kinases, which in turn have been activated by TGF-β or a multitude of other growth factors and hormones. Linker region phosphorylation can prevent nuclear translocation of Smads and inhibit TGF-β signalling, potentially leading to oncogenesis. However, some evidence has revealed that linker region phosphorylated Smads can be translocated to the nucleus where they regulate transcription particularly of the synthesis of extracellular matrix molecules. Matrix molecules such as collagen and proteoglycans are involved in diseases such a fibrosis and atherosclerosis, respectively, and the involvement of linker region phosphorylation may represent a new therapeutic target.
Keyword Transforming growth factor-β
Smads
Phosphorylation
Signalling
Vascular smooth muscle
Collagen
Proteoglycans
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Critical review of research, literature review, critical commentary
Collection: School of Pharmacy Publications
 
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