LMW-PTP associates and dephosphorylates STAT5 interacting with its C-terminal domain
LMW-PTP associates and dephosphorylates STAT5 interacting with its C-terminal domain
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DOI：
10.1016/j.bbrc.2003.10.126
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发表时间：
2003-12-12
影响因子：
3.1
通讯作者：
Berti, A
中科院分区：
文献类型：
--
作者：
Rigacci, S;Talini, D;Berti, A
造血细胞，特别是巨核细胞，表现出低水平的M-r磷酸酪氨酸蛋白磷酸酶(LMW-PTP)表达；然而，这种PTP在这类细胞谱系中的作用几乎没有被研究过。在这里，我们证明了LMW-PTP能够结合并去磷酸化Dami巨核细胞中的信号转导和转录激活因子-5(STAT5)。许多研究人员反复假设调节性磷酸酪氨酸蛋白磷酸酶与STAT5 C末端的关系，但这种磷酸酪氨酸蛋白磷酸酶仍不清楚。我们的证据表明，STAT5和LMW-PTP的结合不仅涉及STAT5的磷酸酶活性部位和磷酸酪氨酸残基，而且我们在STAT5的C末端个体化了一个必要的相互作用区域，这与先前假设的PTP结合结构域一致。(C)2003 Elsevier Inc.保留所有权利。
Hematopoietic cells, particularly megakaryoblastic ones, display a high level of low M-r phosphotyrosine protein phosphatase (LMW-PTP) expression; nevertheless, the role of this PTP in such cellular lineages has been scarcely investigated. Here, we demonstrate that LMW-PTP is able to associate and dephosphorylate signal transducer and activator of transcription-5 (STAT5) in DAMI megakaryocytic cells. Numerous researchers repeatedly hypothesized the association of a regulatory phosphotyrosine protein phosphatase with STAT5 C-terminus, but such phosphotyrosine protein phosphatase remained unknown. We show evidence indicating that the association of STAT5 and LMW-PTP does not exclusively involve the phosphatase active site and phosphotyrosine residue of STAT5, and we individuate an essential region of interaction at STAT5 C-terminus, coinciding with the previously hypothesized PTP-associating domain. (C) 2003 Elsevier Inc. All rights reserved.