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Articles by Sheng-Cai Lin
Total Records ( 2 ) for Sheng-Cai Lin
  Zailian Lu , Wei Liu , Huizhe Huang , Ying He , Ying Han , Yanning Rui , Yanhai Wang , Qinxi Li , Ka Ruan , Zhiyun Ye , Boon Chuan Low , Anming Meng and Sheng-Cai Lin
  Axin plays an architectural role in many important signaling pathways that control various aspects of development and tumorigenesis, including the Wnt, transforming growth factor-β, MAP kinase pathways, as well as p53 activation cascades. It is encoded by the mouse Fused (Fu) locus; the AxinFu allele is caused by insertion of an IAP transposon. AxinFu/Fu mice display varying phenotypes ranging from embryonic lethality to relatively normal adulthood with kinky tails. However, the protein product(s) has not been identified or characterized. In the present study, we conducted immunoprecipitation using brain extracts from the AxinFu mice with specific antibodies against different regions of Axin and found that a truncated Axin containing amino acids 1–596 (designated as AxinFu-NT) and the full-length complement of Axin (AxinWT) can both be generated from the AxinFu allele. When tested for functionality changes, AxinFu-NT was found to abolish Axin-mediated activation of JNK, which plays a critical role in dorsoventral patterning. Together with a proteomics approach, we found that AxinFu-NT contains a previously uncharacterized dimerization domain and can form a heterodimeric interaction with AxinWT. The AxinFu-NT/AxinWT is not conducive to JNK activation, providing a molecular explanation for the dominant negative effect of AxinFu-NT on JNK activation by wild-type Axin. Importantly, AxinFu-NT exhibits no difference in the inhibition of Wnt signaling compared with AxinWT as determined by reporter gene assays, interaction with key Wnt regulators, and expression of Wnt marker genes in zebrafish embryos, suggesting that altered JNK signaling contributes, at least in part, to the developmental defects seen in AxinFu mice.
  Qinxi Li , Na Zhang , Duanwu Zhang , Yuqian Wang , Tianwei Lin , Yanhai Wang , Huamin Zhou , Zhiyun Ye , Faming Zhang , Sheng-Cai Lin and Jiahuai Han
  p38α and p38β MAPKs (mitogen-activated protein kinases) share about 80% of their protein sequence identity, but have quite different biological functions. One such difference is in regulating the subcellular localization of their downstream kinases, such as PRAK (p38-regulated/activated protein kinase or MK5). The p38α-PRAK complex is found in the nucleus, whereas the p38β-PRAK complex is exclusively localized to the cytosol. By generating a series of chimeric and point mutants of p38α and p38β, we found two amino acid residues (Asp145 and Leu156 in p38α, Gly145 and Val156 in p38β) that determine the distinct subcellular locations of p38α-PRAK and p38β-PRAK. The subcellular localization of MK2 (MAPK-activated protein kinase 2), another downstream kinase of p38, was regulated in the same manner as that of PRAK. We found that nuclear import, but not export, determines the subcellular localization of p38α-PRAK and p38β-PRAK. The published structure of the p38α-MK2 complex suggests Leu156 of p38α is involved in the interaction with the nuclear localization signal in PRAK. The difference at this residue between p38α and p38β may affect the nuclear localization signal in PRAK differently, and thereby influence the import of the complexes. Asp145 in p38α (or Gly145 in p38β) is located on a different surface patch, and further random mutagenesis revealed that mutation of Asp145, Thr123, and Gln325, the residues that can directly interact with importin α as predicted by modeling, but not mutation of the other 7 amino acid residues that cannot reach importin α, re-locate p38α-PRAK to the cytosol, suggesting that interaction with import machinery is involved in determining the subcellular localization of the p38α-PRAK and p38β-PRAK complexes. Last, we show that nuclear localization of PRAK is required for its role in inhibiting the proliferation of NIH3T3 cells. In conclusion, multiple determinants control the distinct subcellular localization of p38α-PRAK and p38β-PRAK complexes, and the location of PRAK plays a role in its function.
 
 
 
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