ArticleMolecular and cellular biology1995
The serum response factor nuclear localization signal: general implications for cyclic AMP-dependent protein kinase activity in control of nuclear translocation.
Article in Molecular and cellular biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 44 citations in OpenAlex.
- The transcription factor serum response factor stimulates axon regeneration through cytoplasmic localization and cofilin interaction.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013Article
- Nuclear import of serum response factor in airway smooth muscle.American journal of respiratory cell and molecular biology · 2011Article
- A hitchhiker's guide to the MADS world of plants.Genome biology · 2010Review
- PKA-dependent phosphorylation of serum response factor inhibits smooth muscle-specific gene expression.Arteriosclerosis, thrombosis, and vascular biology · 2009Article
- Critical role of serum response factor in pulmonary myofibroblast differentiation induced by TGF-beta.American journal of respiratory cell and molecular biology · 2009Article
- Cell-specific nuclear import of plasmid DNA in smooth muscle requires tissue-specific transcription factors and DNA sequences.Gene therapy · 2008Article
- Protein kinase A phosphorylation modulates transport of the polypyrimidine tract-binding protein.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- High RhoA activity maintains the undifferentiated mesenchymal cell phenotype, whereas RhoA down-regulation by laminin-2 induces smooth muscle myogenesis.The Journal of cell biology · 2002Article
- Involvement of protein kinase A in fibroblast growth factor-2-activated transcription.Proceedings of the National Academy of Sciences of the United States of America · 2000Article
- Cell-specific nuclear import of plasmid DNA.Gene therapy · 1999Article
- cAMP-dependent protein kinase phosphorylates and activates nuclear Ca2+-ATPase.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- Cationic lipid-based gene delivery systems: pharmaceutical perspectives.Pharmaceutical research · 1997Review
- Stimulation of nuclear import by simian virus 40-transformed cell extracts is dependent on protein kinase activity.Molecular and cellular biology · 1995Article
- Direct selection of cDNAs using whole chromosomes.Nucleic acids research · 1995Article
- RSK3 encodes a novel pp90rsk isoform with a unique N-terminal sequence: growth factor-stimulated kinase function and nuclear translocation.Molecular and cellular biology · 1995Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have identified a basic sequence in the N-terminal region of the 67-kDa serum response factor (p67SRF or SRF) responsible for its nuclear localization. A peptide containing this nuclear localization signal (NLS) translocates rabbit immunoglobulin G (IgG) into the nucleus as efficiently as a peptide encoding the simian virus 40 NLS. This effect is abolished by substituting any two of the four basic residues in this NLS. Overexpression of a modified form of SRF in which these basic residues have been mutated confirms the absolute requirement for this sequence, and not the other basic amino acid sequences adjacent to it, in the nuclear localization of SRF. Since this NLS is in close proximity to potential phosphorylation sites for the cAMP-dependent protein kinase (A-kinase), we further investigated if A-kinase plays a role in the nuclear location of SRF. The nuclear transport of SRF proteins requires basal A-kinase activity, since inhibition of A-kinase by using either the specific inhibitory peptide PKIm or type II regulatory subunits (RII) completely prevents the nuclear localization of plasmid-expressed tagged SRF or an SRF-NLS-IgG conjugate. Direct phosphorylation of SRF by A-kinase can be discounted in this effect, since mutation of the putative phosphorylation sites in either the NLS peptide or the encoded full-length SRF protein had no effect on nuclear transport of the mutants. Finally, in support of an implication of A-kinase-dependent phosphorylation in a more general mechanism affecting nuclear import, we show that the nuclear transport of a simian virus 40-NLS-conjugated IgG or purified cyclin A protein is also blocked by inhibition of A-kinase, even though neither contains any potential sites for phosphorylation by A-kinase or can be phosphorylated by A-kinase in vitro.
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