The carboxy-terminal hydrophobic domain of TIG3, a class II tumor suppressor protein, is required for appropriate cellular localization and optimal biological activity.

  • Authors:
    • A Deucher
    • S Nagpal
    • R A Chandraratna
    • D Di Sepio
    • N A Robinson
    • S R Dashti
    • R L Eckert
  • View Affiliations

  • Published online on: December 1, 2000     https://doi.org/10.3892/ijo.17.6.1195
  • Pages: 1195-1398
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Abstract

TIG3 is a recently discovered class II tumor suppressor protein, originally isolated from retinoid-treated cultured epidermal keratinocytes, that suppresses the proliferation of a variety of epithelial cell types. In the present study, we examine the ability of this protein to reduce CHO, T47D and HaCaT cell proliferation, and the role of the carboxy-terminal hydrophobic domain in this regulation. Vector-mediated expression of the full length TIG3 protein, TIG31-164, results in a 50-70% reduction colony formation efficiency. Expression of a truncated mutant, TIG31-134, that lacks the putative carboxy-terminal membrane-anchoring domain, results in a partial loss of ability to suppress colony formation. The fact that the truncated protein remains partially active suggests that both the amino- and carboxy-terminal regions of TIG3 are required for optimal growth suppression. The full-length protein is distributed in a perinuclear location, and is not present in the nucleus. TIG31-134, in contrast, is distributed in the cytoplasm. Thus, a change in location is associated with the partial loss of activity. We also monitored the distribution of green fluorescent protein (GFP)-TIG3 fusion proteins. GFP-TIG31-164 was localized in a pattern similar to that observed for TIG31-164, while GFP-TIG31-134 displayed a distribution pattern similar to GFP. This suggests that the c-terminal hydrophobic domain has an important role in determining the intracellular localization of TIG3. In addition, GFP-TIG31-164 retains the ability to inhibit cell function, while GFP-TIG31-134 is inactive.

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Dec 2000
Volume 17 Issue 6

Print ISSN: 1019-6439
Online ISSN:1791-2423

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Spandidos Publications style
Deucher A, Nagpal S, Chandraratna R, Di Sepio D, Robinson N, Dashti S and Eckert R: The carboxy-terminal hydrophobic domain of TIG3, a class II tumor suppressor protein, is required for appropriate cellular localization and optimal biological activity.. Int J Oncol 17: 1195-1398, 2000.
APA
Deucher, A., Nagpal, S., Chandraratna, R., Di Sepio, D., Robinson, N., Dashti, S., & Eckert, R. (2000). The carboxy-terminal hydrophobic domain of TIG3, a class II tumor suppressor protein, is required for appropriate cellular localization and optimal biological activity.. International Journal of Oncology, 17, 1195-1398. https://doi.org/10.3892/ijo.17.6.1195
MLA
Deucher, A., Nagpal, S., Chandraratna, R., Di Sepio, D., Robinson, N., Dashti, S., Eckert, R."The carboxy-terminal hydrophobic domain of TIG3, a class II tumor suppressor protein, is required for appropriate cellular localization and optimal biological activity.". International Journal of Oncology 17.6 (2000): 1195-1398.
Chicago
Deucher, A., Nagpal, S., Chandraratna, R., Di Sepio, D., Robinson, N., Dashti, S., Eckert, R."The carboxy-terminal hydrophobic domain of TIG3, a class II tumor suppressor protein, is required for appropriate cellular localization and optimal biological activity.". International Journal of Oncology 17, no. 6 (2000): 1195-1398. https://doi.org/10.3892/ijo.17.6.1195