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Int. J. Mol. Sci. 2008, 9(8), 1504-1514; doi:10.3390/ijms9081504

TFIP11, CCNL1 and EWSR1 Protein-protein Interactions, and Their Nuclear Localization

University of Southern California, School of Dentistry, Center for Craniofacial Molecular Biology, 2250 Alcazar Street, CSA room 103, Los Angeles, California 90033-1004, USA
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Received: 22 May 2008 / Revised: 14 August 2008 / Accepted: 15 August 2008 / Published: 25 August 2008
(This article belongs to the Section Biochemistry, Molecular Biology and Biophysics)
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Abstract

Previous studies using the yeast two-hybrid assay (Y2H) have identified cyclin L1 (CCNL1) and Ewing sarcoma breakpoint region 1 protein (EWSR1) as being interacting partners of tuftelin-interacting protein 11 (TFIP11). All three proteins are functionally related to the spliceosome and involved in pre-mRNA splicing activities. The spliceosome is a dynamic ribonucleoprotein complex responsible for pre-mRNA splicing of intronic regions, and is composed of five small nuclear RNAs (snRNAs) and ~140 proteins. TFIP11 appears to play a role in spliceosome disassembly allowing for the release of the bound lariat-intron. The roles of CCNL1 and EWSR1 in the spliceosome are poorly understood. Using fluorescently-tagged proteins and confocal microscopy we show that TFIP11, CCNL1 and EWSR1 frequently co-localize to speckled nuclear domains. These data would suggest that all three proteins participate in a common cellular activity related to RNA splicing events. View Full-Text
Keywords: Cyclin L1; Ewing’s sarcoma protein; nuclear speckles; pre-mRNA splicing; spliceosomal component 35; spliceosome; tuftelin-interacting protein 11. Cyclin L1; Ewing’s sarcoma protein; nuclear speckles; pre-mRNA splicing; spliceosomal component 35; spliceosome; tuftelin-interacting protein 11.
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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MDPI and ACS Style

Tannukit, S.; Wen, X.; Wang, H.; Paine, M.L. TFIP11, CCNL1 and EWSR1 Protein-protein Interactions, and Their Nuclear Localization. Int. J. Mol. Sci. 2008, 9, 1504-1514.

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