Nuclear import of early growth response-1 involves importin-7 and the novel nuclear localization signal serine-proline-serine
Date
2011
Authors
Chen, Jinbiao
Liu, Mary Y
Chong, Beng
Khachigian, Levon M
Parish, Christopher
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Pergamon-Elsevier Ltd
Abstract
A three amino acid sequence, Ser/Thr-Pro-Ser/Thr, was recently identified and characterized as a novel nuclear localization signal (Chuderland et al., 2008). The immediate-early gene product, early growth response-1 is a three zinc finger containing transcription factor implicated in a wide variety of pathologies, and has a bipartite nuclear localization domain identified two decades ago. Efficient nuclear localization of Egr-1 is vital to its function as a transcription factor. Interestingly, Egr-1 also contains a C-terminal SPS domain (residues 482-484 in murine Egr-1). We hypothesized that482SPS484 may also serve as a novel nuclear localization signal in Egr-1. We found that this sequence directs Egr-1 to the nucleus in transfected Chinese hamster ovary cells and show by co-immunoprecipitation analysis that Egr-1 forms a complex with importin-7.482SPS484 is required for Egr-1's interaction with importin-7. Moreover, importin-7 knockdown with RNAi showed that Egr-1 nuclear translocation is importin-7-dependent. This study demonstrates that the nuclear translocation of Egr-1 is partially dependent on482SPS484 and involves importin-7, and sheds light on the molecular mechanisms regulating the cellular localization of this pathophysiologically important transcription factor.
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Keywords: early growth response factor 1; importin 7; karyopherin; proline; serine; unclassified drug; amino acid sequence; animal cell; article; carboxy terminal sequence; cell nucleus; cellular distribution; CHO cell; complex formation; human; human cell; immunop CHO cells; Egr-1; GFP; Importin-7; Smooth muscle cells; SPS
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The International Journal of Biochemistry and Cell Biology
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Journal article
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2037-12-31
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