Publications by authors named "Jing-Ping Hsin"
Article Synopsis
- - The study presents a novel cell therapy called Tmod that uses antigens like EGFR and HLA-E, commonly found on cancer cells, to create targeted attacks while sparing noncancerous cells.
- - Noncancerous cells are protected from the therapy due to an inhibitory receptor that modulates the presence of CAR on their surface, triggered by a specific HLA allele often missing in many solid tumors.
- - Mouse models show that Tmod can effectively prevent toxicity from CAR treatments and manage immune responses without requiring extra gene-editing, suggesting its potential for easy, off-the-shelf therapeutic applications.
Numerous microRNAs and their target mRNAs are coexpressed across diverse cell types. However, it is unknown whether they are regulated in a manner independent of or dependent on cellular context. Here, we explored transcriptome-wide targeting and gene regulation by miR-155, whose activation-induced expression plays important roles in innate and adaptive immunity.
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- The study investigates how microRNA (miRNA), specifically miR-155, influences gene expression and cellular responses by focusing on its interaction with a single target gene, SOCS1.
- Researchers created a mutation in SOCS1's 3' UTR to disrupt its regulation by miR-155 and examined the effects under normal and stressed conditions like autoimmune inflammation or viral infection.
- Findings revealed that while some immune functions dependent on miR-155 were directly linked to SOCS1, others were influenced by different mechanisms, suggesting the importance of context and cell type in miRNA regulation.
The RNA polymerase II largest subunit (Rpb1) contains a unique C-terminal domain (CTD) that plays multiple roles during transcription. The CTD is composed of consensus Y(1)S(2)P(3)T(4)S(5)P(6)S(7) repeats, in which Ser, Thr and Tyr residues can all be phosphorylated. Here we report analysis of CTD Tyr1 using genetically tractable chicken DT40 cells.
View Article and Find Full Text PDFThe C-terminal domain of the RNA polymerase II largest subunit (the Rpb1 CTD) is composed of tandem heptad repeats of the consensus sequence Y(1)S(2)P(3)T(4)S(5)P(6)S(7). We reported previously that Thr 4 is phosphorylated and functions in histone mRNA 3'-end formation in chicken DT40 cells. Here, we have extended our studies on Thr 4 and to other CTD mutations by using these cells.
View Article and Find Full Text PDFThe C-terminal domain (CTD) of the RNA polymerase II largest subunit consists of multiple heptad repeats (consensus Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7), varying in number from 26 in yeast to 52 in vertebrates. The CTD functions to help couple transcription and processing of the nascent RNA and also plays roles in transcription elongation and termination. The CTD is subject to extensive post-translational modification, most notably phosphorylation, during the transcription cycle, which modulates its activities in the above processes.
View Article and Find Full Text PDFThe RNA polymerase II (RNAP II) largest subunit contains a C-terminal domain (CTD) with up to 52 Tyr(1)-Ser(2)-Pro(3)-Thr(4)-Ser(5)-Pro(6)-Ser(7) consensus repeats. Serines 2, 5, and 7 are known to be phosphorylated, and these modifications help to orchestrate the interplay between transcription and processing of messenger RNA (mRNA) precursors. Here, we provide evidence that phosphorylation of CTD Thr(4) residues is required specifically for histone mRNA 3' end processing, functioning to facilitate recruitment of 3' processing factors to histone genes.
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