The nuclear PP1 interacting protein ZAP3 (ZAP) is a putative nucleoside kinase that complexes with SAM68, CIA, NF110/45, and HNRNP-G

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1774, Issue 10, 2007, Pages 1339-1350

  Ulke Lemée, Annegret ^a   Trinkle Mulcahy, Laura ^b   Chaulk, Steve ^c   Bernstein, Nina K ^c   Morrice, Nick ^b   Glover, Mark ^c   Lamond, Angus I ^b   Moorhead, Greg B G ^a  

^a UNIVERSITY OF CALGARY   (Canada)

^b UNIVERSITY OF DUNDEE   (United Kingdom)

^c UNIVERSITY OF ALBERTA   (Canada)

Author keywords

Nucleus; Phosphatase; Phosphohydrolase; Polynucleotide kinase; PP1; Targeting

Indexed keywords

CYTIDINE; NUCLEAR RECEPTOR COACTIVATOR 5; NUCLEIC ACID; NUCLEOSIDE; PHOSPHATASE; PHOSPHOPROTEIN PHOSPHATASE 1; PHOSPHOTRANSFERASE; POLYNUCLEOTIDE 5' HYDROXYL KINASE; PROTEIN; PROTEIN PHOSPHATASE 1 INTERACTING PROTEIN ZAP3; RNA BINDING PROTEIN; RNA BINDING PROTEIN HNRNP G; RNA BINDING PROTEIN NF110 45; RNA BINDING PROTEIN SAM68; UNCLASSIFIED DRUG; URIDINE;

ARTICLE; BIOINFORMATICS; CELL NUCLEUS; COMPLEX FORMATION; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME SUBSTRATE; FUNCTIONAL PROTEOMICS; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN;

ADAPTOR PROTEINS, SIGNAL TRANSDUCING; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CELL CYCLE PROTEINS; CONSERVED SEQUENCE; DNA-BINDING PROTEINS; HELA CELLS; HETEROGENEOUS-NUCLEAR RIBONUCLEOPROTEIN GROUP F-H; HUMANS; MOLECULAR SEQUENCE DATA; NUCLEAR FACTOR 45 PROTEIN; NUCLEAR FACTOR 90 PROTEINS; NUCLEAR PROTEINS; NUCLEOPROTEINS; PHOSPHOTRANSFERASES; PHOSPHOTRANSFERASES (ALCOHOL GROUP ACCEPTOR); PROTEIN BINDING; PROTEIN PHOSPHATASE 1; PROTEIN SUBUNITS; RABBITS; RATS; RNA-BINDING PROTEINS;

MAMMALIA;

EID: 34748880010     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2007.07.015     Document Type: Article

References (58)

1. Egloff M.P., Johnson D.F., Moorhead G., Cohen P.T., Cohen P., and Barford D. Structural basis for the recognition of regulatory subunits by the catalytic subunit of protein phosphatase 1. EMBO J. 16 (1997) 1876-1887
2. Wakula P., Beullens M., Ceulemans H., Stalmans W., and Bollen M. Degeneracy and function of the ubiquitous RVXF motif that mediates binding to protein phosphatase-1. J. Biol. Chem. 278 (2003) 18817-18823
3. Zhao S., and Lee E.Y. A protein phosphatase-1-binding motif identified by the panning of a random peptide display library. J. Biol. Chem. 272 (1997) 28368-28372
4. Roadcap D., Matthew H., and Shenolikar S. Identification of Cellular Protein Phosphatase-1 Regulators. Methods in Molecular Biology vol. 365 (2006), Humana Press
5. Ceulemans H., and Bollen M. Functional diversity of protein phosphatase-1, a cellular economizer and reset button. Physiol. Rev. 84 (2004) 1-39
6. Trinkle-Mulcahy L., Andersen J., Lam Y.W., Moorhead G., Mann M., and Lamond A.I. Repo-Man recruits PP1 gamma to chromatin and is essential for cell viability. J. Cell Biol. 172 (2006) 679-692
7. Tran H.T., Ulke A., Morrice N., Johannes C.J., and Moorhead G.B. Proteomic characterization of protein phosphatase complexes of the mammalian nucleus. Mol. Cell Proteomics 3 (2004) 257-265
8. Bollen M., and Beullens M. Signaling by protein phosphatases in the nucleus. Trends Cell Biol. 12 (2002) 138-145
9. Moorhead G.B., Trinkle-Mulcahy L., and Ulke-Lemée A. Emerging roles of nuclear protein phosphatases. Nat. Rev., Mol. Cell Biol. 8 (2007) 234-244
10. Jin Q., van Eynde A., Beullens M., Roy N., Thiel G., Stalmans W., and Bollen M. The protein phosphatase-1 (PP1) regulator, nuclear inhibitor of PP1 (NIPP1), interacts with the polycomb group protein, embryonic ectoderm development (EED), and functions as a transcriptional repressor. J. Biol. Chem. 278 (2003) 30677-30685
11. Van Eynde A., Beullens M., Stalmans W., and Bollen M. Full activation of a nuclear species of protein phosphatase-1 by phosphorylation with protein kinase A and casein kinase-2. Biochem. J. 297 Pt 3 (1994) 447-449
12. Jagiello I., Beullens M., Vulsteke V., Wera S., Sohlberg B., Stalmans W., von Gabain A., and Bollen M. NIPP-1, a nuclear inhibitory subunit of protein phosphatase-1, has RNA-binding properties. J. Biol. Chem. 272 (1997) 22067-22071
13. Trinkle-Mulcahy L., Ajuh P., Prescott A., Claverie-Martin F., Cohen S., Lamond A.I., and Cohen P. Nuclear organisation of NIPP1, a regulatory subunit of protein phosphatase 1 that associates with pre-mRNA splicing factors. J. Cell Sci. 112 Pt 2 (1999) 157-168
14. Boudrez A., Beullens M., Groenen P., Van Eynde A., Vulsteke V., Jagiello I., Murray M., Krainer A.R., Stalmans W., and Bollen M. NIPP1-mediated interaction of protein phosphatase-1 with CDC5L, a regulator of pre-mRNA splicing and mitotic entry. J. Biol. Chem. 275 (2000) 25411-25417
15. Landsverk H.B., Kirkhus M., Bollen M., Kuntziger T., and Collas P. PNUTS enhances in vitro chromosome decondensation in a PP1-dependent manner. Biochem. J. 390 (2005) 709-717
16. Allen P.B., Kwon Y.G., Nairn A.C., and Greengard P. Isolation and characterization of PNUTS, a putative protein phosphatase 1 nuclear targeting subunit. J. Biol. Chem. 273 (1998) 4089-4095
17. Kreivi J.P., Trinkle-Mulcahy L., Lyon C.E., Morrice N.A., Cohen P., and Lamond A.I. Purification and characterisation of p99, a nuclear modulator of protein phosphatase 1 activity. FEBS Lett. 420 (1997) 57-62
18. Kim Y.M., Watanabe T., Allen P.B., Lee S.J., Greengard P., Nairn A.C., and Kwon Y.G. PNUTS, a protein phosphatase 1 (PP1) nuclear targeting subunit: characterization of its PP1- and RNA-binding domains and regulation by phosphorylation. J. Biol. Chem. 278 (2003) 13819-13828
19. Vagnarelli P., Hudson D.F., Ribeiro S.A., Trinkle-Mulcahy L., Spence J.M., Lai F., Farr C.J., Lamond A.I., and Earnshaw W.C. Condensin and Repo-Man-PP1 co-operate in the regulation of chromosome architecture during mitosis. Nat. Cell Biol. 8 (2006) 1133-1142
20. Misawa K., Nosaka T., Morita S., Kaneko A., Nakahata T., Asano S., and Kitamura T. A method to identify cDNAs based on localization of green fluorescent protein fusion products. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 3062-3066
21. Sutherland H.G., Mumford G.K., Newton K., Ford L.V., Farrall R., Dellaire G., Caceres J.F., and Bickmore W.A. Large-scale identification of mammalian proteins localized to nuclear sub-compartments. Hum. Mol. Genet. 10 (2001) 1995-2011
22. Bennett D., Lyulcheva E., and Alphey L. Towards a comprehensive analysis of the protein phosphatase 1 interactome in Drosophila. J. Mol. Biol. 364 (2006) 196-212
23. Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., and Gygi S.P. Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 12130-12135
24. Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., and Mann M. Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 127 (2006) 635-648
25. Trinkle-Mulcahy L., Sleeman J.E., and Lamond A.I. Dynamic targeting of protein phosphatase 1 within the nuclei of living mammalian cells. J. Cell Sci. 114 (2001) 4219-4228
26. Xiao H., Tao Y., Greenblatt J., and Roeder R.G. A cofactor, TIP30, specifically enhances HIV-1 Tat-activated transcription. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 2146-2151
27. Tran H.T., Bridges D., Ulke A., and Moorhead G.B. Detection of multiple splice variants of the nuclear protein phosphatase 1 regulator sds22 in rat liver nuclei. Biochem. Cell. Biol. 80 (2002) 811-815
28. Goodarzi A.A., and Lees-Miller S.P. Biochemical characterization of the ataxia-telangiectasia mutated (ATM) protein from human cells. DNA Repair (Amst) 3 (2004) 753-767
29. Chen Y.M., Ferrar T.S., Lohmeier-Vogel E.M., Morrice N., Mizuno Y., Berenger B., Ng K.K., Muench D.G., and Moorhead G.B. The PII signal transduction protein of Arabidopsis thaliana forms an arginine-regulated complex with plastid N-acetyl glutamate kinase. J. Biol. Chem. 281 (2006) 5726-5733
30. Moorhead G., MacKintosh R.W., Morrice N., Gallagher T., and MacKintosh C. Purification of type 1 protein (serine/threonine) phosphatases by microcystin-sepharose affinity chromatography. FEBS Lett. 356 (1994) 46-50
31. Trinkle-Mulcahy L., Andrews P.D., Wickramasinghe S., Sleeman J., Prescott A., Lam Y.W., Lyon C., Swedlow J.R., and Lamond A.I. Time-lapse imaging reveals dynamic relocalization of PP1gamma throughout the mammalian cell cycle. Mol. Biol. Cell 14 (2003) 107-117
32. Kerk D., Conley T.R., Rodriguez F.A., Tran H.T., Nimick M., Muench D.G., and Moorhead G.B. A chloroplast-localized dual-specificity protein phosphatase in Arabidopsis contains a phylogenetically dispersed and ancient carbohydrate-binding domain, which binds the polysaccharide starch. Plant J. 46 (2006) 400-413
33. Cuff J.A., Clamp M.E., Siddiqui A.S., Finlay M., and Barton G.J. JPred: a consensus secondary structure prediction server. Bioinformatics 14 (1998) 892-893
34. Cuff J.A., and Barton G.J. Application of multiple sequence alignment profiles to improve protein secondary structure prediction. Proteins 40 (2000) 502-511
35. Spector D.L. Higher order nuclear organization: three-dimensional distribution of small nuclear ribonucleoprotein particles. Proc. Natl. Acad. Sci. U. S. A. 87 (1990) 147-151
36. Shav-Tal Y., Blechman J., Darzacq X., Montagna C., Dye B.T., Patton J.G., Singer R.H., and Zipori D. Dynamic sorting of nuclear components into distinct nucleolar caps during transcriptional inhibition. Mol. Biol. Cell 16 (2005) 2395-2413
37. www.bind.ca.
38. Bader G.D., Betel D., and Hogue C.W. BIND: the biomolecular interaction network database. Nucleic Acids Res. 31 (2003) 248-250
39. Beullens M., and Bollen M. The protein phosphatase-1 regulator NIPP1 is also a splicing factor involved in a late step of spliceosome assembly. J. Biol. Chem. 277 (2002) 19855-19860
40. Dreyfuss G., Kim V.N., and Kataoka N. Messenger-RNA-binding proteins and the messages they carry. Nat. Rev., Mol. Cell Biol. 3 (2002) 195-205
41. Taylor S.J., and Shalloway D. An RNA-binding protein associated with Src through its SH2 and SH3 domains in mitosis. Nature 368 (1994) 867-871
42. Soulard M., Barque J.P., Della Valle V., Hernandez-Verdun D., Masson C., Danon F., and Larsen C.J. A novel 43-kDa glycoprotein is detected in the nucleus of mammalian cells by autoantibodies from dogs with autoimmune disorders. Exp. Cell Res. 193 (1991) 59-71
43. Soulard M., Della Valle V., Siomi M.C., Pinol-Roma S., Codogno P., Bauvy C., Bellini M., Lacroix J.C., Monod G., Dreyfuss G., et al. hnRNP G: sequence and characterization of a glycosylated RNA-binding protein. Nucleic Acids Res. 21 (1993) 4210-4217
44. Saunders L.R., Perkins D.J., Balachandran S., Michaels R., Ford R., Mayeda A., and Barber G.N. Characterization of two evolutionarily conserved, alternatively spliced nuclear phosphoproteins, NFAR-1 and-2, that function in mRNA processing and interact with the double-stranded RNA-dependent protein kinase, PKR. J. Biol. Chem. 276 (2001) 32300-32312
45. Hartmann A.M., Nayler O., Schwaiger F.W., Obermeier A., and Stamm S. The interaction and colocalization of Sam68 with the splicing-associated factor YT521-B in nuclear dots is regulated by the Src family kinase p59(fyn). Mol. Biol. Cell 10 (1999) 3909-3926
46. Gary J.D., and Clarke S. RNA and protein interactions modulated by protein arginine methylation. Prog. Nucleic Acid Res. Mol. Biol. 61 (1998) 65-131
47. Liu Q., and Dreyfuss G. In vivo and in vitro arginine methylation of RNA-binding proteins. Mol. Cell. Biol. 15 (1995) 2800-2808
48. Saraste M., Sibbald P.R., and Wittinghofer A. The P-loop-a common motif in ATP- and GTP-binding proteins. Trends Biochem. Sci. 15 (1990) 430-434
49. Walker J.E., Saraste M., Runswick M.J., and Gay N.J. Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1 (1982) 945-951
50. Kelley L., Bennett-Lovsey R., Herbert A., and Fleming K. Structural Bioinformatics Group (2005), Imperial College, London, UK 0.2 ed.
51. Eastberg J.H., Pelletier J., and Stoddard B.L. Recognition of DNA substrates by T4 bacteriophage polynucleotide kinase. Nucleic Acids Res. 32 (2004) 653-660
52. Galburt E.A., Pelletier J., Wilson G., and Stoddard B.L. Structure of a tRNA repair enzyme and molecular biology workhorse: T4 polynucleotide kinase. Structure (Camb) 10 (2002) 1249-1260
53. Bernstein N.K., Williams R.S., Rakovszky M.L., Cui D., Green R., Karimi-Busheri F., Mani R.S., Galicia S., Koch C.A., Cass C.E., Durocher D., Weinfeld M., and Glover J.N. The molecular architecture of the mammalian DNA repair enzyme, polynucleotide kinase. Mol. Cell 17 (2005) 657-670
54. Suzuki N.N., Koizumi K., Fukushima M., Matsuda A., and Inagaki F. Structural basis for the specificity, catalysis, and regulation of human uridine-cytidine kinase. Structure 12 (2004) 751-764
55. Eddy S.R. Where did the BLOSUM62 alignment score matrix come from?. Nat. Biotechnol. 22 (2004) 1035-1036
56. Nicholas K.N.H. GeneDoc: a tool for editing and annotating multiple sequence alignments (1997) (Distributed by the author)
57. Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., and Higgins D.G. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25 (1997) 4876-4882
58. Genedoc, http://www.psc.edu/biomed/dissem/genedoc/index.html.