Dishevelled C-terminus: prolyl and histidinyl motifs.
Dishevelled C-terminus: prolyl and histidinyl motifs.
复制标题
蓬乱的 C 末端:脯氨酰和组氨酰基序。
DOI:
10.1111/j.1748-1716.2011.02291.x
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发表时间:
2012-01
期刊:
影响因子:
--
通讯作者:
Malbon CC
中科院分区:
文献类型:
--
作者:
Wang HY;Malbon CC
The phosphoprotein scaffold Dishevelled is an essential component of both Wnt signaling and of the signalsome that constitutes the supermolecular “punctae” of assembled proteins often observed in fluorescence microscopy. The C-terminal region beyond the DEP domain displays unique and interesting character, exploited herein by careful analysis of the primary structure. Human Dishevelled-1, -2, -3 and fly Dishevelled (Dsh) sequences were downloaded and interrogated in silico. The C-terminus of Dishevelled-3 is revealed by FoldIndex® to be rich in ordered structure. It displays primary sequence that is unique and divergent in important ways from vertebrate isoforms as well as from the fly Dsh. The region is amphipathic, high in prolyl content, and harbors polyprolines. Dishevelled-3 displays some regions where the proline content is >40%. Polyprolyl sequences (2–4 residues) likely constitute important sites of interaction with other Dishevelled isoforms. Several histidine-single amino acid repeats are notable. The 637,638/647,648 repeats of Dvl3 are essential for Wnt non-canonical, but not canonical signaling. Mutagenesis reveals that the C-terminal sequence is essential for the formation of punctae, made visible by fluorescence microscopy. These Dvl3-based signalsomes are very large (25–35 MDa MW), supermolecular complexes that display dynamic reorganization in response to Wnt stimulation. Dishevelled-3 C-terminus is rich in structure and unique motifs, worthy of detailed analysis with modern molecular tools.
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影响因子:
4.8
作者:
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通讯作者:
Bryja, Vitezslav
影响因子:
21.3
作者:
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Moon, RT
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作者:
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Niehrs, Christof
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作者:
Ma L;Wang Y;Malbon CC;Wang HY
通讯作者:
Wang HY
影响因子:
4.5
作者:
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通讯作者:
Wynshaw-Boris A