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http://dx.doi.org/10.5483/BMBRep.2016.49.6.240

A systematic study of nuclear interactome of C-terminal domain small phosphatase-like 2 using inducible expression system and shotgun proteomics  

Kang, NaNa (Department of Brain & Cognitive Sciences, DGIST)
Koo, JaeHyung (Department of Brain & Cognitive Sciences, DGIST)
Wang, Sen (Qiqihar Medical University)
Hur, Sun Jin (Department of Animal Science and Technology, Chung-Ang University)
Bahk, Young Yil (Department of Biotechnology, Konkuk University)
Publication Information
BMB Reports / v.49, no.6, 2016 , pp. 319-324 More about this Journal
Abstract
RNA polymerase II C-terminal domain phosphatases are newly emerging family of phosphatases that contain FCPH domain with Mg+2-binding DXDX(T/V) signature motif. Its subfamily includes small CTD phosphatases (SCPs). Recently, we identified several interacting partners of human SCP1 with appearance of dephosphorylation and O-GlcNAcylation. In this study, using an established cell line with inducible CTDSPL2 protein (a member of the new phosphatase family), proteomic screening was conducted to identify binding partners of CTDSPL2 in nuclear extract through immunoprecipitation of CTDSPL2 with its associated. This approach led to the identification of several interacting partners of CTDSPL2. This will provide a better understanding on CTDSPL2.
Keywords
CTD phosphatase; CTDSPL2 inducible HEK293T cell line; CTDSPL2; Immunoprecipitation; Nuclear interactome;
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Times Cited By KSCI : 2  (Citation Analysis)
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1 Licciardo P, Amente S and Ruggiero L (2003) The FCP1 phosphatase interacts with RNA polymerase II and with MEP50 a component of the methylosome complex involved in the assembly of snRNP. Nucleic Acids Res 31, 999-1005   DOI
2 Bataille AR, Jeronimo C and Jacques PE (2012) A universal RNA polymerase II CTD cycle is orchestrated by complex interplays between kinase, phosphatase, and isomerase enzymes along genes. Mol Cell 45, 158-170   DOI
3 Chambers RS and Dahmus ME (1994) Purification and characterization of a phosphatase from HeLa cells, which dephosphorylates the C terminal domain of RNA polymerase II. J Biol Chem 269, 26243-26248
4 Kemmer D, Podowki RM and Arenillas D (2006) Novel-Fam3000-uncharacterized human protein domains. BMC Genomics 7, 1471-2164   DOI
5 Hsin J-P and Manley JL (2012) The RNA polymerase II CTD coordinates transcription and RNA processing. Genes Dev 26, 2119-2137   DOI
6 Zhao Y, Xiao M, Sun B et al (2014) C-terminal domain (CTD) small phosphatase-like 2 modulates the canonical bone morphogenetic protein (BMP) signaling and mesenchymal differentiation via smad dephosphorylation. J Biol Chem 289, 26441-26450
7 Harikrishna RR, Kim H, Noh K and Kim YJ (2014) Diverse roles in RNA polymerase II C-terminal domain phosphatase SCP1. BMB Rep 47, 192-196   DOI
8 Kamenski T, Heilmeier S, Meinhart A et al (2004) Structure and mechanism of RNA polymerase II CTD phosphatases. Mol Cell 15, 399-407   DOI
9 Ma YN, Zhang X, Yu HC and Zhang JW (2010) CTD small phosphatase like 2 (CTDSPL2) can increase ε- and γ-globin gene expression in K562 cells and CD34+ cells derived from umbilical cord blood. BMC Cell Biol 11, 75-86   DOI
10 Qian H, Ji C, Zhao S et al (2007) Expression and characterization of HSPC129, a RNA polymerase II C-terminal domain phosphatase. Mol Cell Biochem 303, 183-188   DOI
11 Alberts B (1998) The cell as a collection of protein machines: preparing the next generation of molecular biologists. Cell 92, 291-294   DOI
12 Koo JH and Bahk YY (2014) In vivo putative O-GlcNAcylation of human SCP1 and evidence for possible role of its N-terminal disorder structure. BMB Rep 47, 593-598   DOI
13 Blalock W, Piazzi M, Bavelloni A et al (2014) Identification of the PKR nuclear interactome reveals roles in ribosome biogenesis, mRNA processing and cell division. J Cell Physiol 229, 1047-1060   DOI
14 Bahk YY, Cho IH and Kim TS (2008) A cross-talk between oncogenic Ras and tumor suppressor PTEN through FAK Tyr861 phosphorylation in NIH/3T3 mouse embryonic fibroblasts. Biochem Biophys Res Comm 377, 1199-1204   DOI
15 Maehama T, Taylor GS, Slama JT and Dixon JE (2000) A sensitive assay for phosphoinositide phosphatases. Anal Biochem 279, 248-250   DOI
16 Kwon Y, Vinayagam A, Sun X et al (2013) The Hippo signaling pathway interactome. Science 342, 737-740   DOI
17 Bahk YY, Lee J, Cho IH and Lee HW (2010) An analysis of an interactome for apoptosis factor, Ei24/PIG8, using the inducible expression system and shotgun proteomics. J Proteome Res 9, 5270-5283   DOI
18 Kim S, Lee YZ and Bahk YY (2008) A proteomic approach for protein-profiling the oncogenic ras induced transformation (H-, K-, and N-Ras) in NIH/3T3 mouse embryonic fibroblasts. Proteomics 8, 3082-3093   DOI
19 Powers CA, Mathur M, Raaka BM, Ron D and Samuels HH (1998) TLS (translocated-in liposarcoma) is a high-affinity interactor for steroid, thyroid hormone, and retinoid receptors. Mol Endocrinol 12, 4-18   DOI
20 Kim YJ and Bahk YY (2014) A study of substrate specificity for a CTD phosphatase, SCP1, by proteomics screening of binding partners. Biochem Biophys Res Comm 448, 189-124   DOI
21 Zhao G, Shi L, Qiu D, Hu H and Kao PN (2005) NF45/ILF2 tissue expression, promoter analysis, and interleukin-2 transactivating function. Exp Cell Res 305, 312-323   DOI
22 Neumann M, Sampathu DM, Kwong LK et al (2006) Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science 314, 130-133   DOI
23 Sun M, Yamashita T, Shang J et al (2014) Acceleration of TDP43 and FUS/TLS protein expressions in the preconditioned hippocampus following repeated transient ischemia. J Neurosci Res 92, 53-63   DOI
24 Perkins DN, Pappin DJ, Cressy DM and Cottrell JS (1999) Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20, 3551-3567   DOI