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Multiple isoforms of UDP-GalNAc:polypeptide N-acetylgalactosaminyl-
transferase (ppGaNTase) have been cloned and expressed from a variety of
organisms. In general, these isoforms display different patterns of
tissue-specific expression, but exhibit overlapping substrate
specificities, in vitro . A peptide substrate, derived from the sequence of
the V3 loop of the HIV gp120 protein (HIV peptide), has previously been
shown to be glycosylated in vitro exclusively by the ppGaNTase-T3 (Bennett
et al. , 1996). To determine if this isoform- specificity is maintained in
vivo , we have examined the glycosylation of this substrate when it is
expressed as a reporter peptide (rHIV) in a cell background (COS7 cells)
which lacks detectable levels of the ppGaNTase-T3. Glycosylation of rHIV
was greatly increased by coexpression of a recombinant ppGaNTase-T3.
Overexpression of ppGaNTase- T1 yielded only partial glycosylation of the
reporter. We have also determined that the introduction of a proline
residue at the +3 position flanking the potential glycosylation site
eliminated ppGaNTase- T3 selectivity toward rHIV observed both in vivo and
in vitro .
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Collak FK Yagiz K Luthringer DJ Erkaya B Cinar B 《The Journal of biological chemistry》2012,287(28):23698-23709
Mst1/Stk4, a hippo-like serine-threonine kinase, is implicated in many cancers, including prostate cancer. However, the mechanisms regulating Mst1 remain obscure. Here, we characterized the effects of phospho-Thr-120 on Mst1 in prostate cancer cells. We demonstrated that phospho-Thr-120 did not alter the nuclear localization or cleavage of Mst1 in a LNCaP or castration-resistant C4-2 prostate tumor cell model, as revealed by a mutagenesis approach. Phospho-Thr-120 appeared to be specific to cancer cells and predominantly localized in the nucleus. In contrast, phospho-Thr-183, a critical regulator of Mst1 cell death, was exclusively found in the cytoplasm. As assessed by immunohistochemistry, a similar distribution of phospho-Mst1-Thr-120/Thr-183 was also observed in a prostate cancer specimen. In addition, the blockade of PI3K signaling by a small molecule inhibitor, LY294002, increased cytoplasmic phospho-Mst1-Thr-183 without having a significant effect on nuclear phospho-Mst1-Thr-120. However, the attenuation of mammalian target of rapamycin (mTOR) activity by a selective pharmacologic inhibitor, Ku0063794 or CCI-779, caused the up-regulation of nuclear phospho-Mst1-Thr-120 without affecting cytoplasmic phospho-Mst1-Thr-183. This suggests that PI3K and mTOR pathway signaling differentially regulate phospho-Mst1-Thr-120/Thr-183. Moreover, mutagenesis and RNAi data revealed that phospho-Thr-120 resulted in C4-2 cell resistance to mTOR inhibition and reduced the Mst1 suppression of cell growth and androgen receptor-driven gene expression. Collectively, these findings indicate that phospho-Thr-120 leads to the loss of Mst1 functions, supporting cancer cell growth and survival. 相似文献
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