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Article

A LIM protein, Hic‐5, functions as a potential coactivator for Sp1

14 Jan 2004

Abstract excerpt

Hic-5 is a LIM protein with striking similarity to paxillin, and shuttles between focal adhesions and the nucleus. Our previous study suggested that Hic-5 participates in the transcriptional control of several genes such as the c-fos and p21 genes. In the present study, we examined the function of Hic-5 in the nucleus using the transcriptional promoter region of the p21 gene. When localized to the nucleus, Hic-5...

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Identifiers

PMID: 14755691
DOI: 10.1002/jcb.10754

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Related research

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Research trail→

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A LIM protein, Hic‐5, functions as a potential coactivator for Sp1PMID 14755691Read ↗

Transcriptional activation of the c-fos gene by a LIM protein, Hic-5.Semantic proximity Read ↗

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Identification and characterization of hic-5/ARA55 as an hsp27 binding protein.Semantic proximity Read ↗

[Regulation of cellular phenotypes by Hic-5 that localizes both in the focal adhesion and in the nucleus].Semantic proximity Read ↗

Paxillin enables attachment-independent tyrosine phosphorylation of focal adhesion kinase and transformation by RAS.Semantic proximity Read ↗

Hic-5 regulates extracellular matrix-associated gene expression and cytokine secretion in cancer associated fibroblastsSemantic proximity Read ↗

The HumanTRIP6Gene Encodes a LIM Domain Protein and Maps to Chromosome 7q22, a Region Associated with TumorigenesisSemantic proximity Read ↗

Hic-5 contributes to epithelial-mesenchymal transformation through a RhoA/ROCK-dependent pathway.Semantic proximity Read ↗

The nuclear isoform of the LIM domain protein Trip6 integrates activating and repressing signals at the promoter-bound glucocorticoid receptor.Semantic proximity Read ↗

p57Kip2 regulates actin dynamics by binding and translocating LIM-kinase 1 to the nucleus.Semantic proximity Read ↗

Phosphorylation of Hic-5 at tyrosine 60 by CAKbeta and Fyn.Semantic proximity Read ↗

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