Comparative analysis of Arabidopsis zinc finger-containing glycine-rich RNA-binding proteins during cold adaptation

2010 ◽  
Vol 48 (10-11) ◽  
pp. 866-872 ◽  
Author(s):  
Won Yong Kim ◽  
Joo Yeol Kim ◽  
Hyun Ju Jung ◽  
Seung Han Oh ◽  
Yeon Soo Han ◽  
...  
Cancers ◽  
2020 ◽  
Vol 12 (6) ◽  
pp. 1539 ◽  
Author(s):  
Yogesh Saini ◽  
Jian Chen ◽  
Sonika Patial

Post-transcriptional regulation of gene expression plays a key role in cellular proliferation, differentiation, migration, and apoptosis. Increasing evidence suggests dysregulated post-transcriptional gene expression as an important mechanism in the pathogenesis of cancer. The tristetraprolin family of RNA-binding proteins (RBPs), which include Zinc Finger Protein 36 (ZFP36; commonly referred to as tristetraprolin (TTP)), Zinc Finger Protein 36 like 1 (ZFP36L1), and Zinc Finger Protein 36 like 2 (ZFP36L2), play key roles in the post-transcriptional regulation of gene expression. Mechanistically, these proteins function by binding to the AU-rich elements within the 3′-untranslated regions of their target mRNAs and, in turn, increasing mRNA turnover. The TTP family RBPs are emerging as key regulators of multiple biological processes relevant to cancer and are aberrantly expressed in numerous human cancers. The TTP family RBPs have tumor-suppressive properties and are also associated with cancer prognosis, metastasis, and resistance to chemotherapy. Herein, we summarize the various hallmark molecular traits of cancers that are reported to be regulated by the TTP family RBPs. We emphasize the role of the TTP family RBPs in the regulation of trait-associated mRNA targets in relevant cancer types/cell lines. Finally, we highlight the potential of the TTP family RBPs as prognostic indicators and discuss the possibility of targeting these TTP family RBPs for therapeutic benefits.


1997 ◽  
Vol 61 (5) ◽  
pp. 905-906 ◽  
Author(s):  
Yuichi Matsushima ◽  
Kiyoshi Matsumura ◽  
Yasuo Kitagawa

2010 ◽  
Vol 61 (9) ◽  
pp. 2317-2325 ◽  
Author(s):  
Joo Yeol Kim ◽  
Won Yong Kim ◽  
Kyung Jin Kwak ◽  
Seung Han Oh ◽  
Yeon Soo Han ◽  
...  

2011 ◽  
Vol 12 (1) ◽  
pp. R3 ◽  
Author(s):  
Tanja Scherrer ◽  
Christian Femmer ◽  
Ralph Schiess ◽  
Ruedi Aebersold ◽  
André P Gerber

2021 ◽  
Author(s):  
Tania Bishola ◽  
Christine Clayton

In Trypanosoma brucei and related Kinetoplastids, regulation of gene expression occurs mostly post-transcriptionally, and RNA-binding proteins play a critical role in the regulation of mRNA and protein abundance. Trypanosoma brucei ZC3H28 is a 114 KDa cytoplasmic mRNA-binding protein with a single C(x)7C(x)5C(x)sH zinc finger at the C-terminus and numerous proline-, histine- or glutamine-rich regions. We here show that N-terminally tagged ZC3H28 copurifies ribosomes, various RNA-binding proteins, and the translation initiation complex EIF4E4/EIF4G3. ZC3H28 is preferentially associated with long RNAs that have low complexity sequences in their 3'-untranslated regions. When tethered to a reporter mRNA, ZC3H28 increased the mRNA level without a corresponding increase in protein expression; this suggests that it stabilized the reporter but at the same time suppressed its translation. Indeed, there was a clear negative correlation between ZC3H28 mRNA binding and ribosome density. After ZC3H28 depletion, the relative levels of ribosomal protein mRNAs increased while levels of some long mRNAs decreased, but there is no overall correlation between binding and RNAi effects on mRNA abundance. We speculate that ZC3H28 might be implicated in stabilizing poorly-translated mRNAs.


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