![[Feedback]](/icons/banner/feedbackACT.gif){kind=icon}
![[For Subscribers]](/icons/banner/subscriberACT.gif){kind=icon}
![[Archive]](/icons/banner/archiveACT.gif){kind=icon}
![[Search]](/icons/banner/searchACT.gif){kind=icon}
|
|
|
|
|
||
A more recent version of this article appeared on March 1, 2003
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Submitted on June 13, 2002
Revised on October 30, 2002
Accepted on November 25, 2002
1 Department of Microbiology, Showa University School of Pharmaceutical Sciences, Hatanodai 1-5-8, Shinagawa-ku, Tokyo, Japan
* Corresponding author. E-mail address: smotoko{at}pharm.showa-u.ac.jp.
hic-5 was originally isolated as an H2O2-inducible cDNA clone whose product was normally found at focal adhesions. In this study, we found that Hic-5 accumulated in the nucleus in response to oxidants such as H2O2. Other focal adhesion proteins including paxillin, the most homologous to Hic-5, remained in the cytoplasm. Mutation analyses revealed that the C- and N-terminal halves of Hic-5 contributed to its nuclear localization in a positive and negative manner, respectively. Following the finding that leptomycin B (LMB), an inhibitor of nuclear export signal (NES), caused Hic-5 to be retained in the nucleus, Hic-5 was demonstrated to harbor NES in the N-terminal, which was sensitive to oxidants, thereby regulating the nuclear accumulation of Hic-5. NES consisted of a leucine-rich stretch and two cysteines with a limited similarity to Yap/Pap-type NES. In the nucleus, Hic-5 was suggested to participate in the gene expression of c-fos. Using dominant negative mutants, we found that Hic-5 was actually involved in endogenous c-fos gene expression upon H2O2 treatment. Hic-5 was thus proposed as a focal adhesion protein with the novel aspect of shuttling between focal adhesions and the nucleus through an oxidant-sensitive NES, mediating the redox signaling directly to the nucleus.
This article has been cited by other articles:
|
|
 |
|
  S. Kaulfuss, M. Grzmil, B. Hemmerlein, P. Thelen, S. Schweyer, J. Neesen, L. Bubendorf, A. G. Glass, H. Jarry, B. Auber, et al. Leupaxin, a Novel Coactivator of the Androgen Receptor, Is Expressed in Prostate Cancer and Plays a Role in Adhesion and Invasion of Prostate Carcinoma Cells Mol. Endocrinol., July 1, 2008; 22(7): 1606 - 1621. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 L. J. Sundberg-Smith, L. A. DiMichele, R. L. Sayers, C. P. Mack, and J. M. Taylor The LIM Protein Leupaxin Is Enriched in Smooth Muscle and Functions As an Serum Response Factor Cofactor to Induce Smooth Muscle Cell Gene Transcription Circ. Res., June 20, 2008; 102(12): 1502 - 1511. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 E. Saijou, T. Itoh, K.-W. Kim, S.-i. Iemura, T. Natsume, and A. Miyajima Nucleocytoplasmic Shuttling of the Zinc Finger Protein EZI Is Mediated by Importin-7-dependent Nuclear Import and CRM1-independent Export Mechanisms J. Biol. Chem., November 2, 2007; 282(44): 32327 - 32337. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 Y. H. Lee, U. S. Kayyali, A. M. Sousa, T. Rajan, R. J. Lechleider, and R. M. Day Transforming Growth Factor-beta1 Effects on Endothelial Monolayer Permeability Involve Focal Adhesion Kinase/Src Am. J. Respir. Cell Mol. Biol., October 1, 2007; 37(4): 485 - 493. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
K. Mori, M. Asakawa, M. Hayashi, M. Imura, T. Ohki, E. Hirao, J.-r. Kim-Kaneyama, K. Nose, and M. Shibanuma Oligomerizing Potential of a Focal Adhesion LIM Protein Hic-5 Organizing a Nuclear-Cytoplasmic Shuttling Complex J. Biol. Chem., August 4, 2006; 281(31): 22048 - 22061. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. D. Heitzer and D. B. DeFranco Hic-5/ARA55, a LIM Domain-Containing Nuclear Receptor Coactivator Expressed in Prostate Stromal Cells. Cancer Res., July 15, 2006; 66(14): 7326 - 7333. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. Velichkova and T. Hasson Keap1 Regulates the Oxidation-Sensitive Shuttling of Nrf2 into and out of the Nucleus via a Crm1-Dependent Nuclear Export Mechanism Mol. Cell. Biol., June 1, 2005; 25(11): 4501 - 4513. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J.-r. Kim-Kaneyama, W. Suzuki, K. Ichikawa, T. Ohki, Y. Kohno, M. Sata, K. Nose, and M. Shibanuma Uni-axial stretching regulates intracellular localization of Hic-5 expressed in smooth-muscle cells in vivo J. Cell Sci., March 1, 2005; 118(5): 937 - 949. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
H. Wang, K. Song, T. L. Sponseller, and D. Danielpour Novel Function of Androgen Receptor-associated Protein 55/Hic-5 as a Negative Regulator of Smad3 Signaling J. Biol. Chem., February 18, 2005; 280(7): 5154 - 5162. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
C. Wu Migfilin and its binding partners: from cell biology to human diseases J. Cell Sci., February 15, 2005; 118(4): 659 - 664. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S. Drori, G. D. Girnun, L. Tou, J. D. Szwaya, E. Mueller, X. Kia, R. A. Shivdasani, and B. M. Spiegelman Hic-5 regulates an epithelial program mediated by PPAR{gamma} Genes & Dev., February 1, 2005; 19(3): 362 - 375. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
K. Mori, M. Shibanuma, and K. Nose Invasive Potential Induced under Long-Term Oxidative Stress in Mammary Epithelial Cells Cancer Res., October 15, 2004; 64(20): 7464 - 7472. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. C. Brown and C. E. Turner Paxillin: Adapting to Change Physiol Rev, October 1, 2004; 84(4): 1315 - 1339. [Abstract] [Full Text] [PDF]
|
|
