tfip11, ccnl1 and ewsr1 protein-protein interactions, and their nuclear localizationtfip11,ccnl1 ewsr1蛋白质-蛋白质之间的关系,他们的核本地化.pdf

Int. J. Mol. Sci. 2008, 9, 1504-1514; DOI: 10.3390/ijms9081504 OPEN ACCESS International Journal of Molecular Sciences ISSN 1422-0067 /ijms/ Article TFIP11, CCNL1 and EWSR1 Protein-protein Interactions, and Their Nuclear Localization Sissada Tannukit, Xin Wen, HongJun Wang and Michael L. Paine * University of Southern California, School of Dentistry, Center for Craniofacial Molecular Biology, 2250 Alcazar Street, CSA room 103, Los Angeles, California 90033-1004, USA. E-mail: paine@ * Author to whom correspondence should be addressed; Fax: +1-323-442-2981. Received: 23 May 2008; in revised form: 14 August 2008 / Accepted: 15 August 2008 / Published: 25 August 2008 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.