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.
Keywords: Cyclin L1; Ewing’s sarcoma protein; nuclear speckles; pre-mRNA splicing; spliceosomal component 35; spliceosome; tuftelin-interacting protein 11.
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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.
Tannukit S, Wen X, Wang H, Paine ML. TFIP11, CCNL1 and EWSR1 Protein-protein Interactions, and Their Nuclear Localization. International Journal of Molecular Sciences. 2008; 9(8):1504-1514.
Tannukit, Sissada; Wen, Xin; Wang, HongJun; Paine, Michael L. 2008. "TFIP11, CCNL1 and EWSR1 Protein-protein Interactions, and Their Nuclear Localization." Int. J. Mol. Sci. 9, no. 8: 1504-1514.