|
|
|
|||||||
|
|||||||||
J. Biol. Chem., Vol. 277, Issue 35, 31834-31841, August 30, 2002
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
From the Afdeling Biochemie, Faculteit Geneeskunde, Katholieke
Universiteit Leuven, B-3000 Leuven, Belgium
NIPP1 is a ubiquitously expressed nuclear protein
that functions both as a regulator of protein Ser/Thr phosphatase-1 and as a splicing factor. The N-terminal part of NIPP1 consists of a
phosphothreonine-interacting Forkhead-associated (FHA) domain. We show
here that the FHA domain of NIPP1 interacts in vitro and in vivo with a TP dipeptide-rich fragment of the splicing
factor SAP155/SF3b155, a component of the U2 small nuclear
ribonucleoprotein particle. The NIPP1-SAP155 interaction was
entirely dependent on the phosphorylation of specific TP motifs in
SAP155. Mutagenesis and competition studies revealed that various
phosphorylated TP motifs competed for binding to the same site in the
FHA domain. The SAP155 kinases in cell lysates were blocked by
the Ca2+ chelator EGTA and by the
cyclin-dependent protein kinase inhibitor roscovitine. The
phosphorylation level of SAP155 was dramatically increased during
mitosis, and accordingly the activity of SAP155 kinases was augmented
in mitotic lysates. We discuss how the interaction between NIPP1 and
SAP155 could contribute to spliceosome (dis)assembly and the catalytic
steps of splicing.
Phosphorylation-dependent Interaction between the
Splicing Factors SAP155 and NIPP1*
,§,
*
This work was supported by Fund for Scientific
Research-Flanders Grant G.0374.01 and by a Flemish Concerted Research
Action.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Both authors contributed equally to this work.
§
A postdoctoral fellow of the National Fund for Scientific
Research-Flanders.
¶
To whom correspondence should be addressed: Afdeling
Biochemie, Campus Gasthuisberg, Herestraat 49, B-3000 Leuven, Belgium. Tel.: 32-16-34-57-01; Fax: 32-16-34-59-95; E-mail:
Mathieu.Bollen@med.kuleuven.ac.be.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  N. Tanuma, S.-E. Kim, M. Beullens, Y. Tsubaki, S. Mitsuhashi, M. Nomura, T. Kawamura, K. Isono, H. Koseki, M. Sato, et al. Nuclear Inhibitor of Protein Phosphatase-1 (NIPP1) Directs Protein Phosphatase-1 (PP1) to Dephosphorylate the U2 Small Nuclear Ribonucleoprotein Particle (snRNP) Component, Spliceosome-associated Protein 155 (Sap155) J. Biol. Chem., December 19, 2008; 283(51): 35805 - 35814. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
L. Li, K. Kozlowski, B. Wegner, T. Rashid, T. Yeung, C. Holmes, and B. J. Ballermann Phosphorylation of TIMAP by Glycogen Synthase Kinase-3beta Activates Its Associated Protein Phosphatase 1 J. Biol. Chem., August 31, 2007; 282(35): 25960 - 25969. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 E. R. Morris, D. Chevalier, and J. C. Walker DAWDLE, a Forkhead-Associated Domain Gene, Regulates Multiple Aspects of Plant Development Plant Physiology, July 1, 2006; 141(3): 932 - 941. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. Van Eynde, M. Nuytten, M. Dewerchin, L. Schoonjans, S. Keppens, M. Beullens, L. Moons, P. Carmeliet, W. Stalmans, and M. Bollen The Nuclear Scaffold Protein NIPP1 Is Essential for Early Embryonic Development and Cell Proliferation Mol. Cell. Biol., July 1, 2004; 24(13): 5863 - 5874. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
V. Vulsteke, M. Beullens, A. Boudrez, S. Keppens, A. Van Eynde, M. H. Rider, W. Stalmans, and M. Bollen Inhibition of Spliceosome Assembly by the Cell Cycle-regulated Protein Kinase MELK and Involvement of Splicing Factor NIPP1 J. Biol. Chem., March 5, 2004; 279(10): 8642 - 8647. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 H. T. Tran, A. Ulke, N. Morrice, C. J. Johannes, and G. B. G. Moorhead Proteomic Characterization of Protein Phosphatase Complexes of the Mammalian Nucleus Mol. Cell. Proteomics, March 1, 2004; 3(3): 257 - 265. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 H. CEULEMANS and M. BOLLEN Functional Diversity of Protein Phosphatase-1, a Cellular Economizer and Reset Button Physiol Rev, January 1, 2004; 84(1): 1 - 39. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
T. Ammosova, M. Jerebtsova, M. Beullens, Y. Voloshin, P. E. Ray, A. Kumar, M. Bollen, and S. Nekhai Nuclear Protein Phosphatase-1 Regulates HIV-1 Transcription J. Biol. Chem., August 22, 2003; 278(34): 32189 - 32194. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
Q. Jin, A. van Eynde, M. Beullens, N. Roy, G. Thiel, W. Stalmans, and M. Bollen 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., August 15, 2003; 278(33): 30677 - 30685. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |