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Physical and functional interactions of histone deacetylase 3 with TFII-I family proteins and PIASαβ
被引:82
作者:
Tussié-Luna, MI
Bayarsaihan, D
Seto, E
Ruddle, RH
Roy, AL
机构:
[1] Tufts Univ, Dept Pathol, Sch Med, Boston, MA 02111 USA
[2] Yale Univ, Dept Mol Cellular & Dev Biol, New Haven, CT 06520 USA
[3] Univ S Florida, H Lee Moffitt Canc Ctr & Res Inst, Tampa, FL 33612 USA
来源:
关键词:
D O I:
10.1073/pnas.192464499
中图分类号:
O [数理科学和化学];
P [天文学、地球科学];
Q [生物科学];
N [自然科学总论];
学科分类号:
07 ;
0710 ;
09 ;
摘要:
TFII-I family proteins are characterized structurally by the presence of multiple reiterated I-repeats, each containing a putative helix-loop-helix domain. Functionally, they behave as multifunctional transcription factors that are activated by a variety of extracellular signals. In studying their subcellular localization, we noticed that these transcription factors frequently reside in subnuclear domains/dots. Because nuclear dots are believed often to harbor components of histone deacetylase enzymes (HDACs), we investigated whether TFII-I family proteins colocalize and interact with HDACs. Here, we show that TFII-I and its related member hMusTRD1/BEN physically and functionally interact with HDAC3. The TFII-I family proteins and HDAC3 also show nearly identical expression patterns in early mouse development. Consistent with our earlier observation that TFII-l family proteins also interact with PIASxbeta, a member of the E3 ligase family involved in the small ubiquitin-like modifier (SUMO) pathway, we show further that PIASxbeta physically and functionally interacts with HDAC3 and relieves the transcriptional repression exerted by HDAC3 upon TFII-I-mediated gene activation. These results suggest a complex interplay between two post-translational pathways-histone modification and SUMOylation-brokered in part by TFII-l family proteins.
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页码:12807 / 12812
页数:6
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