Journal of Life Science (생명과학회지)

Korean Society of Life Science (한국생명과학회)
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Expression of Ajuba, a Novel LIM Protein, is Regulated by Endorlasmic Reticulum Stress

소포체 스트레스가 Ajuba 발현유도

  • Park, Sang-Mi (Department of Anatomy, College of medicine, Chungnam National University) ;
  • Kwon, Ki-Sang (Department of Anatomy, College of medicine, Chungnam National University) ;
  • Yun, Eun-Young (Department of Sericulture and Entomology, National Institute of Agriculture Science and Technology) ;
  • Goo, Tae-Won (Department of Sericulture and Entomology, National Institute of Agriculture Science and Technology) ;
  • Kwon, O-Yu (Department of Anatomy, College of medicine, Chungnam National University)
  • 박상미 (충남대학교 의과대학 해부학교실) ;
  • 권기상 (충남대학교 의과대학 해부학교실) ;
  • 윤은영 (농업과학기술원 농업생물부) ;
  • 구태원 (농업과학기술원 농업생물부) ;
  • 권오유 (충남대학교 의과대학 해부학교실)
  • Published : 2007.07.30
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Abstract

Ajuba is a number of proteins containing cytosolic LIM domain. Its function may provide a new pathway whereby cell-cell adhesive events are transmitted to the nucleus to regulate cell proliferation and differentiation decisions. Here, Ajuba gene expression was investigated its molecular properties associated with endoplasmic reticulum (ER) stresses (tunicamycin, DTT, A23187 and BFA) which induced remarkable ex-pression of Ajuba mRNA. The mRNA half life of Ajuba was also determined, its half life of Ajuba mRNA in FRTL-5 cells was approximately 2 hr after the initial translation. Although the obvious bioligical function of Ajuba is not clear, on the base of the results, Ajuba gene expression is deeply associated with ER stresses.

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References

  1. Crawford, A. W. and M. C. Beckerle, 1991. Purification and characterization of zyxin, an 82,000-dalton component of adherens junctions. J. Biol. Chem. 266(9), 5847-5853.
  2. Credle, J. J., J. S. Finer-Moore, F. R. Papa, R. M. Stround and P. Walter. 2005. On the mechanism of sensing unfolded protein in the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA. 102, 18773-18784. https://doi.org/10.1073/pnas.0509487102
  3. Harding, H. P., Y. Zhang, A. Bertolotti, H. Zeng and D. Ron. 2000. Perk is essential for translational regulation and cell survival during the unfolded protein response. Mol. Cell 5, 897-904. https://doi.org/10.1016/S1097-2765(00)80330-5
  4. Kwon, O. Y., S. Park, W. Lee, K. H. You, H. Kim and M. Shong. 2000. ISH regulates a gene expression encoding ERp29, an endoplasmic reticulum stress protein, in the thyrocytes of FRTL-5 cells. FEBS Lett. 475, 27-30. https://doi.org/10.1016/S0014-5793(00)01617-3
  5. Nix, D. A. and M. C. Beckerle, 1997. Nuclear-cytoplasmic shuttling of the focal contact protein, zyxin: a potential mechanism for communication between sites of cell adhesion and the nucleus. J. Cell Biol. 138, 1139-1147. https://doi.org/10.1083/jcb.138.5.1139
  6. Oyadomari, S., E. Araki and M. Mori, 2002. Endoplasmic reticulum stress mediated a poptosis in pancreatic-cells. Apoptosis 7, 335-345. https://doi.org/10.1023/A:1016175429877
  7. Petit, M. M., J. Fradelizi, R. M. Golsteyn, T. A. Ayoubi, B. Menichi, D. Louvard, W. J. Van deVen and E. Friederich. 2000. LPP, an actin cytoskeleton protein related to zyxin, harbors a nuclear export signal and transcriptional activation capacity. Mol. Biol. Cell 11, 117-129. https://doi.org/10.1091/mbc.11.1.117
  8. Sanchez-Garcia, I. and T. H. Rabbitts. 1993. LIM domain proteins in leukaemia and development. Semi. Cancer Biol. 4, 349-358.
  9. Yoshida, H., K. Haze, H. Yanagi, T. Yura and K. Mori, 1998. Identification of the cis-acting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucose-regulated proteins. Involvement of basic leucine zipper transcription factors. J. Biol. Chem. 273, 33741-33749. https://doi.org/10.1074/jbc.273.50.33741
  10. Yoshida, H., T. Matsui, N. Hosokawa, R. J. Kaufman, K. Nagata and K. Mori. 2003. A time-dependent phase shift in the mammalian unfolded protein response. Dev. Cell. 4, 265-271. https://doi.org/10.1016/S1534-5807(03)00022-4