Prolyl isomerase Pin1 shares functional similarity with phosphorylated CTD interacting factor PCIF1 in vertebrate cells Export

@article{citeulike:5760501, abstract = {The carboxy-terminal domain (CTD) of the RNA polymerase II (Pol II) largest subunit undergoes reversible phosphorylation during transcription cycle. The phosphorylated CTD plays critical roles in coordinating transcription with chromatin modification and RNA processing by serving as a scaffold to recruit various proteins. Recently, we identified a novel human WW domain-containing protein PCIF1 as a phosphorylated CTD-interacting factor and demonstrated that PCIF1 negatively modulates Pol II activity in vivo. In the present study, to explore cellular functions of PCIF1, we generated PCIF1-deficient chicken DT40 cell lines. We observed significant up-regulation of WW domain-containing prolyl isomerase Pin1 in two independently established PCIF1-deficient mutant clones. As reconstitution of PCIF1 in the mutants did not reduce Pin1 expression, PCIF1 may not be a negative regulator of Pin1 expression. We assume that Pin1 over-expression might suppress defects caused by PCIF1 deficiency in DT40 cells. We furthermore compared PCIF1 and Pin1 for their functional properties and found that these two proteins exhibit most similar target specificity among other CTD-binding WW proteins, overlapping subcellular localization and comparative inhibitory effects on transcriptional activation by Pol II in human cultured cells. These results suggest that Pin1 may have overlapping cellular function with PCIF1 in vertebrate cells. 10.1111/j.1365-2443.2009.01339.x}, author = {Yunokuchi, Izumi and Fan, Hong and Iwamoto, Yu and Araki, Chisato and Yuda, Masamichi and Umemura, Hiroyasu and Harada, Fumio and Ohkuma, Yoshiaki and Hirose, Yutaka}, citeulike-article-id = {5760501}, citeulike-linkout-0 = {http://dx.doi.org/10.1111/j.1365-2443.2009.01339.x}, citeulike-linkout-1 = {http://www.genestocellsonline.org/content/14/9/1105.abstract}, citeulike-linkout-2 = {http://www.genestocellsonline.org/content/14/9/1105.full.pdf}, citeulike-linkout-3 = {http://www.ingentaconnect.com/content/bsc/gtc/2009/00000014/00000009/art00006}, day = {1}, doi = {10.1111/j.1365-2443.2009.01339.x}, issn = {1356-9597}, journal = {Genes to Cells}, keywords = {ctd, d-polymerase}, month = {September}, number = {9}, pages = {1105--1118}, posted-at = {2009-11-08 03:24:22}, priority = {2}, publisher = {Blackwell Publishing}, title = {Prolyl isomerase Pin1 shares functional similarity with phosphorylated CTD interacting factor PCIF1 in vertebrate cells}, url = {http://dx.doi.org/10.1111/j.1365-2443.2009.01339.x}, volume = {14}, year = {2009} }

TY - JOUR ID - citeulike:5760501 L3 - citeulike-article-id:5760501 N2 - The carboxy-terminal domain (CTD) of the RNA polymerase II (Pol II) largest subunit undergoes reversible phosphorylation during transcription cycle. The phosphorylated CTD plays critical roles in coordinating transcription with chromatin modification and RNA processing by serving as a scaffold to recruit various proteins. Recently, we identified a novel human WW domain-containing protein PCIF1 as a phosphorylated CTD-interacting factor and demonstrated that PCIF1 negatively modulates Pol II activity in vivo. In the present study, to explore cellular functions of PCIF1, we generated PCIF1-deficient chicken DT40 cell lines. We observed significant up-regulation of WW domain-containing prolyl isomerase Pin1 in two independently established PCIF1-deficient mutant clones. As reconstitution of PCIF1 in the mutants did not reduce Pin1 expression, PCIF1 may not be a negative regulator of Pin1 expression. We assume that Pin1 over-expression might suppress defects caused by PCIF1 deficiency in DT40 cells. We furthermore compared PCIF1 and Pin1 for their functional properties and found that these two proteins exhibit most similar target specificity among other CTD-binding WW proteins, overlapping subcellular localization and comparative inhibitory effects on transcriptional activation by Pol II in human cultured cells. These results suggest that Pin1 may have overlapping cellular function with PCIF1 in vertebrate cells. 10.1111/j.1365-2443.2009.01339.x IS - 9 JF - Genes to Cells SN - 1356-9597 EP - 1118 TI - Prolyl isomerase Pin1 shares functional similarity with phosphorylated CTD interacting factor PCIF1 in vertebrate cells PB - Blackwell Publishing VL - 14 SP - 1105 KW - ctd KW - d-polymerase AU - Yunokuchi, Izumi AU - Fan, Hong AU - Iwamoto, Yu AU - Araki, Chisato AU - Yuda, Masamichi AU - Umemura, Hiroyasu AU - Harada, Fumio AU - Ohkuma, Yoshiaki AU - Hirose, Yutaka PY - 2009/09/01/ UR - http://dx.doi.org/10.1111/j.1365-2443.2009.01339.x ER -