An FF domain-dependent protein interaction mediates a signaling pathway for growth factor-induced gene expression

Jiang, W., Sordella, R., Chen, G. C., Hakre, S., Roy, A. L., Settleman, J. (January 2005) An FF domain-dependent protein interaction mediates a signaling pathway for growth factor-induced gene expression. Molecular Cell, 17 (1). pp. 23-35. ISSN 1097-2765

URL: http://www.ncbi.nlm.nih.gov/pubmed/15629714
DOI: 10.1016/j.molcel.2004.11.024

Abstract

FF domains are poorly understood protein motifs found in all eukaryotes but in a very small number of proteins. They typically occur in tandem arrays and appear predominantly in splicing and transcription factors. Curiously, they are also present in the p190 family of cytoplasmic Rho GTPase activating proteins (GAPs). We identified the serum-responsive transcriptional regulator TFII-I as a specific interactor with the p190 RhoGAP FF domains. p190 sequesters TFII-I in the cytoplasm via the FF domains, but upon PDGF receptor-mediated phosphorylation of an FF domain, TFII-I is released from p190 and translocates to the nucleus where it can activate transcription of serum-inducible genes including c-fos. These findings reveal a pathway by which mitogens promote gene transcription and indicate a role for FF domains in phosphorylation-mediated signal transduction.

Item Type: Paper
Uncontrolled Keywords: Active Transport Cell Nucleus Amino Acid Sequence Animals Cell Cycle Cell Line DNA-Binding Proteins GTPase-Activating Proteins Gene Expression Genes fos Guanine Nucleotide Exchange Factors chemistry deficiency genetics metabolism Mice Molecular Sequence Data Nuclear Proteins chemistry deficiency genetics metabolism Phosphorylation Platelet-Derived Growth Factor pharmacology Promoter Regions Genetic Protein Structure Tertiary Receptors, Platelet-Derived Growth Factor metabolism Recombinant Fusion Proteins chemistry genetics metabolism Repressor Proteins Signal Transduction Transcription Factors TFII metabolism Tyrosine chemistry
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > transcription
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > GTPase
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > genes, structure and function > gene expression
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein characterization
CSHL Authors:
Communities: CSHL labs > Sordella lab
Depositing User: CSHL Librarian
Date: 7 January 2005
Date Deposited: 24 Apr 2012 16:05
Last Modified: 13 Mar 2013 16:05
Related URLs:
URI: http://repository.cshl.edu/id/eprint/26251

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