An FF Domain-Dependent Protein Interaction Mediates a Signaling Pathway for Growth Factor-Induced Gene Expression

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 activati...

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Published inMolecular cell Vol. 17; no. 1; pp. 23 - 35
Main Authors Jiang, Wei, Sordella, Raffaella, Chen, Guang-Chao, Hakre, Shweta, Roy, Ananda L., Settleman, Jeffrey
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 07.01.2005
Subjects
Active Transport, Cell Nucleus
Amino Acid Sequence
Animals
Cell Cycle
Cell Line
DNA-Binding Proteins
Gene Expression
Genes, fos
GTPase-Activating Proteins
Guanine Nucleotide Exchange Factors - chemistry
Guanine Nucleotide Exchange Factors - deficiency
Guanine Nucleotide Exchange Factors - genetics
Guanine Nucleotide Exchange Factors - metabolism
Mice
Molecular Sequence Data
Nuclear Proteins - chemistry
Nuclear Proteins - deficiency
Nuclear Proteins - genetics
Nuclear Proteins - metabolism
Phosphorylation
Platelet-Derived Growth Factor - pharmacology
Promoter Regions, Genetic
Protein Structure, Tertiary
Receptors, Platelet-Derived Growth Factor - metabolism
Recombinant Fusion Proteins - chemistry
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - metabolism
Repressor Proteins
Signal Transduction
Transcription Factors, TFII - metabolism
Tyrosine - chemistry
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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.
AbstractList 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.
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.
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 TF II-I as a specific interactor with the p190 RhoGAP FF domains. p190 sequesters TF II-I in the cytoplasm via the FF domains, but upon PDGF receptor-mediated phosphorylation of an FF domain, TF II-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.
Author Chen, Guang-Chao
Sordella, Raffaella
Hakre, Shweta
Roy, Ananda L.
Jiang, Wei
Settleman, Jeffrey
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Snippet 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...
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SubjectTerms Active Transport, Cell Nucleus
Amino Acid Sequence
Animals
Cell Cycle
Cell Line
DNA-Binding Proteins
Gene Expression
Genes, fos
GTPase-Activating Proteins
Guanine Nucleotide Exchange Factors - chemistry
Guanine Nucleotide Exchange Factors - deficiency
Guanine Nucleotide Exchange Factors - genetics
Guanine Nucleotide Exchange Factors - metabolism
Mice
Molecular Sequence Data
Nuclear Proteins - chemistry
Nuclear Proteins - deficiency
Nuclear Proteins - genetics
Nuclear Proteins - metabolism
Phosphorylation
Platelet-Derived Growth Factor - pharmacology
Promoter Regions, Genetic
Protein Structure, Tertiary
Receptors, Platelet-Derived Growth Factor - metabolism
Recombinant Fusion Proteins - chemistry
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - metabolism
Repressor Proteins
Signal Transduction
Transcription Factors, TFII - metabolism
Tyrosine - chemistry
Title An FF Domain-Dependent Protein Interaction Mediates a Signaling Pathway for Growth Factor-Induced Gene Expression
URI https://dx.doi.org/10.1016/j.molcel.2004.11.024
https://www.ncbi.nlm.nih.gov/pubmed/15629714
https://search.proquest.com/docview/19937307
https://search.proquest.com/docview/67341005
Volume 17
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