Nuclear localization of the pre-mRNA associating protein THOC7 depends upon its direct interaction with Fms tyrosine kinase interacting protein (FMIP).
AuthorsEl Bounkari, Omar
Griffiths, John R
Whetton, Anthony D
AffiliationInstitut fuer Biochemie, OE4310 Medizinische Hochschule Hannover, Hannover, Germany.
MetadataShow full item record
AbstractTHOC7 and Fms-interacting protein (FMIP) are members of the THO complex that associate with the mRNA export apparatus. FMIP is a nucleocytoplasmic shuttling protein with a nuclear localization signal (NLS), whereas THOC7 does not contain a typical NLS motif. We show here that THOC7 (50-137, amino acid numbers) binds to the N-terminal portion (1-199) of FMIP directly. FMIP is detected mainly in the nucleus. In the absence of exogenous FMIP, THOC7 resides mainly in the cytoplasm, while in the presence of FMIP, THOC7 is transported into the nucleus with FMIP. Furthermore, THOC7 lacking the FMIP binding site does not co-localize with FMIP, indicating that THOC7/FMIP interaction is required for nuclear localization of THOC7.
CitationNuclear localization of the pre-mRNA associating protein THOC7 depends upon its direct interaction with Fms tyrosine kinase interacting protein (FMIP). 2009, 583 (1):13-8 FEBS Lett.
- FMIP controls the adipocyte lineage commitment of C2C12 cells by downmodulation of C/EBP alpha.
- Authors: Mancini A, El Bounkari O, Norrenbrock AF, Scherr M, Schaefer D, Eder M, Banham AH, Pulford K, Lyne L, Whetton AD, Tamura T
- Issue date: 2007 Feb 15
- The M-CSF receptor substrate and interacting protein FMIP is governed in its subcellular localization by protein kinase C-mediated phosphorylation, and thereby potentiates M-CSF-mediated differentiation.
- Authors: Mancini A, Koch A, Whetton AD, Tamura T
- Issue date: 2004 Aug 26
- Application of bioinformatics-coupled experimental analysis reveals a new transport-competent nuclear localization signal in the nucleoprotein of influenza A virus strain.
- Authors: Ketha KM, Atreya CD
- Issue date: 2008 Apr 28
- RNA-binding of the human cytomegalovirus transactivator protein UL69, mediated by arginine-rich motifs, is not required for nuclear export of unspliced RNA.
- Authors: Toth Z, Lischka P, Stamminger T
- Issue date: 2006
- RNA-regulated interaction of transportin-1 and exportin-5 with the double-stranded RNA-binding domain regulates nucleocytoplasmic shuttling of ADAR1.
- Authors: Fritz J, Strehblow A, Taschner A, Schopoff S, Pasierbek P, Jantsch MF
- Issue date: 2009 Mar