BCL11A is a SUMOylated protein and recruits SUMO-conjugation enzymes in its nuclear body

BCL11A is a SUMOylated protein and recruits SUMO-conjugation enzymes in its nuclear body
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DOI:
10.1111/j.1365-2443.2008.01216.x
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发表时间:
2008-09-01
期刊:
影响因子:
2.1
通讯作者:
Nakamura, Takuro
Nakamura, Takuro
中科院分区:
生物学4区
文献类型:
--
作者:
Kuwata, Takeshi;Nakamura, Takuro

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BCL11A/EVI9是一种锌指蛋白,主要表达于脑和造血细胞。既往研究表明,BCL11A分别参与小鼠急性髓细胞白血病和人慢性淋巴细胞白血病的发生。此外,BCL11A定位于与BCL6共定位的特征性核体中。然而,BCL11A在白血病发生和核功能中的意义尚不清楚。在这项研究中,我们发现BCL11A与UBC9(一个小的泛素样修饰物(SUMO) E2偶联酶)相互作用,并将SUMO1招募到核体中。BCL11A氨基酸634处的赖氨酸残基被SUMO1化,但不是SUMO1募集所必需的。BCL11A的n端区域负责SUMO1的募集和核体的形成。我们还发现SUMO特异性肽酶SENP2在核体中共定位。这些结果提示BCL11A可能参与SUMO偶联系统,并可能在蛋白修饰中发挥重要作用。
BCL11A/EVI9 is a zinc-finger protein predominantly expressed in brain and hematopoietic cells. Previous studies show that BCL11A is involved in acute myelomonocytic leukemia and chronic lymphoid leukemia in mouse and human, respectively. Moreover, BCL11A is localized in the characteristic nuclear body in which BCL6 is co-localized. However, the significance of BCL11A in leukemogenesis and nuclear function remains unknown. In this study we show that BCL11A interacts with UBC9, a small ubiquitin-like modifier (SUMO) E2 conjugating enzyme, and recruits SUMO1 into the nuclear body. A lysine residue at amino acid 634 of BCL11A is SUMOylated but not required for the SUMO1 recruitment. The N-terminal region of BCL11A is responsible for SUMO1 recruitment as well as its nuclear body formation. We also show that SENP2, a SUMO specific peptidase, is co-localized in the nuclear body. These results suggest that BCL11A could be involved in the SUMO conjugation system, and that BCL11A might play an important role in protein modification.