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Titolo:
The carboxy-terminal hydrophobic domain of TIG3, a class II tumor suppressor protein, is required for appropriate cellular localization and optimal biological activity
Autore:
Deucher, A; Nagpal, S; Chandraratna, RAS; Di Sepio, D; Robinson, NA; Dashti, SR; Eckert, RL;
Indirizzi:
Case Western Reserve Univ, Sch Med, Dept Physiol & Biophys, Cleveland, OH 44106 USA Case Western Reserve Univ Cleveland OH USA 44106 Cleveland, OH 44106 USA Case Western Reserve Univ, Sch Med, Dept Dermatol, Cleveland, OH 44106 USACase Western Reserve Univ Cleveland OH USA 44106 Cleveland, OH 44106 USA Case Western Reserve Univ, Sch Med, Dept Biochem, Cleveland, OH 44106 USA Case Western Reserve Univ Cleveland OH USA 44106 Cleveland, OH 44106 USA Case Western Reserve Univ, Sch Med, Dept Reprod Biol, Cleveland, OH 44106 USA Case Western Reserve Univ Cleveland OH USA 44106 Cleveland, OH 44106 USA Case Western Reserve Univ, Sch Med, Dept Oncol, Cleveland, OH 44106 USA Case Western Reserve Univ Cleveland OH USA 44106 Cleveland, OH 44106 USA Allergan Pharmaceut Inc, Dept Chem, Irvine, CA 92713 USA Allergan Pharmaceut Inc Irvine CA USA 92713 pt Chem, Irvine, CA 92713 USA Allergan Pharmaceut Inc, Dept Biol, Irvine, CA 92713 USA Allergan Pharmaceut Inc Irvine CA USA 92713 pt Biol, Irvine, CA 92713 USA
Titolo Testata:
INTERNATIONAL JOURNAL OF ONCOLOGY
fascicolo: 6, volume: 17, anno: 2000,
pagine: 1195 - 1203
SICI:
1019-6439(200012)17:6<1195:TCHDOT>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
DOWN-REGULATION; GENE; H-REV107; GROWTH; CELLS; IMMORTALIZATION; IDENTIFICATION; METHYLATION; EXPRESSION; CLONING;
Keywords:
epidermal keratinocytes; TIG3 protein; green fluorescent proteins;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
19
Recensione:
Indirizzi per estratti:
Indirizzo: Eckert, RL Case Western Reserve Univ, Sch Med, Dept Physiol & Biophys, Rm E532,2109 Adelbert Rd, Cleveland, OH 44106 USA Case Western Reserve Univ RmE532,2109 Adelbert Rd Cleveland OH USA 44106
Citazione:
A. Deucher et al., "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(6), 2000, pp. 1195-1203

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, TIG3(1-164), results in a 50-70% reduction colony formation efficiency. Expression of a truncated mutant, TIG3(1-134), 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 cal carboxy-terminal regions of TIG3 are required fur optimal growth suppression. The full-length protein is distributed in a perinuclear location, and is not present in the nucleus. TIG3(1-134), 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-TIG3(1-164) was localized in a pattern similar to that observed for TIG3(1-164), while GFP-TIG3(1-134) displayed a distribution pattern similar to GFP. This suggests that the C-terminal hydrophobic domain has an important role in determining the intracellular localization ofTIG3. In addition, GFP-TIG3(1-164) retains the ability to inhibit cell function, while GFP-TIG3(1-134) is inactive.

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Documento generato il 01/12/20 alle ore 08:14:07