Please use this identifier to cite or link to this item: https://hdl.handle.net/20.500.12540/222
Title: C-terminal domain (CTD) phosphatase links Rho GTPase signaling to Pol II CTD phosphorylation in Arabidopsis and yeast
Authors: Zhang, Bo 
Yang, Guohua 
Chen, Yu 
Zhao, Yihong 
Gao, Peng 
Liu, Bo 
Wang, Haiyang 
Zheng, Zhi-Liang 
Issue Date: 2016
Publisher: National Academy of Sciences
Source: Zhang, B., Yang, G., Chen, Y., Zhao, Y., Gao, P., Liu, B., Wang,H., Zheng, Z.-L. (2016). C-terminal domain (CTD) phosphatase links Rho GTPase signaling to Pol II CTD phosphorylation in Arabidopsis and yeast. Proceedings of the National Academy of Sciences of the United States of America, 113(50), 8197.
Journal: Proceedings of the National Academy of Sciences 
Abstract: Rho GTPases, including the Rho, Cdc42, Rac, and ROP subfamilies, act as pivotal signaling switches in various growth and developmental processes. Compared with the well-defined role of cytoskeletal organization in Rho signaling, much less is known regarding transcriptional regulation. In a mutant screen for phenotypic enhancers of transgenic Arabidopsis plants expressing a constitutively active form of ROP2 (designated CA1-1), we identified RNA polymerase II (Pol II) C-terminal domain (CTD) phosphatase-like 1 (CPL1) as a transcriptional regulator of ROP2 signaling. We show that ROP2 activation inhibits CPL1 activity by promoting its degradation, leading to an increase in CTD Ser5 and Ser2 phosphorylation. We also observed similar modulation of CTD phosphorylation by yeast Cdc42 GTPase and enhanced degradation of the yeast CTD phosphatase Fcp1 by activated ROP2 signaling. Taken together, our results suggest that modulation of the Pol II CTD code by Rho GTPase signaling represents an evolutionarily conserved mechanism in both unicellular and multicellular eukaryotes.
Description: Please note that preprint copy is not available on WIRE. Please contact wire@wku.edu.cn to request an electronic copy of this item.
URI: https://hdl.handle.net/20.500.12540/222
DOI: 10.1073/pnas.1605871113
Appears in Collections:Scholarly Publications

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