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West Ashley Library
9 a.m. – 7 p.m.
Phone: (843) 766-6635
Main Library
9 a.m. - 8 p.m.
Phone: (843) 805-6930
Folly Beach Library
Closed for renovations
Phone: (843) 588-2001
John L. Dart Library
9 a.m. – 7 p.m.
Phone: (843) 722-7550
St. Paul's/Hollywood Library
9 a.m. - 8 p.m.
Phone: (843) 889-3300
Mt. Pleasant Library
9 a.m. – 8 p.m.
Phone: (843) 849-6161
Dorchester Road Library
9 a.m. - 8 p.m.
Phone: (843) 552-6466
Edgar Allan Poe/Sullivan's Island Library
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John's Island Library
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McClellanville Library
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Edisto Library
9 a.m. - 6 p.m.
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Wando Mount Pleasant Library
9 a.m. - 8 p.m.
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Otranto Road Library
9 a.m. - 8 p.m.
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Hurd/St. Andrews Library
9 a.m. - 8 p.m.
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Bees Ferry West Ashley Library
9 a.m. - 8 p.m.
Phone: (843) 805-6892
Village Library
9 a.m. - 6 p.m.
Phone: (843) 884-9741
Keith Summey North Charleston Library
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Phone: (843) 805-6909
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Cytoplasmic PML function in TGF-ßsignalling.
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- Author(s): Hui-Kuan Lin; Bergmann, Stephan; Pandolfi, Pier Paolo
- Source:
Nature; 9/9/2004, Vol. 431 Issue 7005, p205-211, 7p- Subject Terms:
- Source:
- Additional Information
- Abstract: Transforming growth factor β (TGF-β) is a pluripotent cytokine that controls key tumour suppressive functions1-3, but cancer cells are often unresponsive to it1,4. The promyelocytic leukaemia (PML) tumour suppressor of acute promyelocytic leukaemia (APL) accumulates in the PML nuclear body, but cytoplasmic PML isoforms of unknown function have also been described5,6. Here we show that cytoplasmic Pml is an essential modulator of TGF-β signalling. Pml-null primary cells are resistant to TGF-β-dependent growth arrest, induction of cellular senescence and apoptosis. These cells also have impaired phosphorylation and nuclear translocation of the TGF-β signalling proteins Smad2 and Smad3, as well as impaired induction of TGF-β target genes. Expression of cytoplasmic Pml is induced by TGF-β. Furthermore, cytoplasmic PML physically interacts with Smad2/3 and SARA (Smad anchor for receptor activation) and is required for association of Smad2/3 with SARA and for the accumulation of SARA and TGF-β receptor in the early endosome. The PML-RARa oncoprotein of APL can antagonize cytoplasmic PML function and APL cells have defects in TGF-β signalling similar to those observed in Pml-null cells. Our findings identify cytoplasmic PML as a critical TGF-β regulator, and further implicate deregulated TGF-β signalling in cancer pathogenesis. [ABSTRACT FROM AUTHOR]
- Abstract:
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