کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10163689 | 1152650 | 2012 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Role of Smad phosphatases in BMP-Smad signaling axis-induced osteoblast differentiation
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کلمات کلیدی
TGF-βSCPsCarboxy terminalSmurf1osterixPPM1ABMPs - BMP هاMAPKs - MAPK هاTGF-β Superfamily - TGF-β سرپرست خانوارALP - آلکالن فسفاتازAlkaline phosphatase - آلکالین فسفاتاز یا فسفاتاز قلیاییOsteocalcin - استئوکلسین Osx - اکسBone reconstruction - بازسازی استخوانtransforming growth factor-β - تبدیل فاکتور رشد βC-terminal - ترمینال Cbone morphogenetic proteins - پروتئین های مورفوژنیک استخوانmitogen-activated protein kinases - کیناز پروتئین فعال Mitogen
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
بیوشیمی بالینی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Bone morphogenetic proteins (BMPs) are members of the transforming growth factor-β (TGF-β) superfamily and stimulate the osteoblast differentiation of various types of cells. Smads play central roles downstream of BMP signaling. Receptor-regulated Smads (R-Smads) are phosphorylated by BMP receptors on 2 serine residues in the Ser-X-Ser (SXS) motif at the C terminus. Phosphorylated R-Smads form heteromeric complexes with Smad4 and directly activate the transcription of BMP-responsive genes such as Id1. In contrast, the phosphorylation of a linker region of R-Smads by mitogen-activated protein kinases suppresses their translocation to the nucleus and thus represses their transcriptional activity. Recently, distinct types of phosphatases, i.e., small C-terminal domain phosphatases (SCPs) and protein phosphatase magnesium-dependent 1A (PPM1A), have been identified as enzymes that suppress BMP activity by dephosphorylating the C-terminal SXS motifs in Smads. In this review, we focus on these Smad phosphatases and the role of the phosphorylation and dephosphorylation of Smad by introducing our own studies. To determine the role of the phosphorylation and dephosphorylation of Smad1, we used a constitutively active Smad1 mutant expression plasmid, Smad1 (DVD), in which the C-terminal serine residues have been substituted by aspartic acids. PPM1A and SCP1 suppressed the activity of Smad1 (DVD). PPM1A suppressed the osteoblast differentiation induced by BMPs by decreasing Smad protein levels. In contrast, SCP1 did not reduce Smad protein levels but suppressed osteoblast differentiation to target the downstream effectors of Smad, especially Runx2. In conclusion, SCP1 and PPM1A suppress the osteoblast differentiation induced by BMPs independent of Smad dephosphorylation.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Oral Biosciences - Volume 54, Issue 2, May 2012, Pages 73-78
Journal: Journal of Oral Biosciences - Volume 54, Issue 2, May 2012, Pages 73-78
نویسندگان
Shoichiro Kokabu, Takenobu Katagiri, Tetsuya Yoda, Vicki Rosen,