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

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 μ140 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.

• Authors: Sissada Tannukit, Xin Wen, HongJun Wang, Michael L Paine
• Journal: International journal of molecular sciences (Int J Mol Sci) Vol. 9 Issue 8 Pg. 1504-1514 (Aug 2008) ISSN: 1422-0067 [Electronic] Switzerland
• PMID: 19122807 (Publication Type: Journal Article)