STAT5-Interacting Proteins: A Synopsis of Proteins that Regulate STAT5 Activity

被引：48

作者：

Able, Ashley A. ^{[1
,2
]}

Burrell, Jasmine A. ^{[1
,2
]}

Stephens, Jacqueline M. ^{[1
,2
]}

机构：

[1] Pennington Biomed Res Ctr, Adipocyte Biol Lab, Baton Rouge, LA 70808 USA

[2] Louisiana State Univ, Dept Biol Sci, Baton Rouge, LA 70803 USA

来源：

BIOLOGY-BASEL | 2017年 / 6卷 / 01期

关键词：

JAK; STATs; signaling; MAMMARY-GLAND; GLUCOCORTICOID-RECEPTOR; SIGNAL TRANSDUCER; PROGESTERONE-RECEPTORS; GROWTH-HORMONE; DNA-BINDING; LMW-PTP; PHOSPHATIDYLINOSITOL; 3-KINASE; FUNCTIONAL INTERACTIONS; SERINE PHOSPHORYLATION;

D O I：

10.3390/biology6010020

中图分类号：

Q [生物科学];

学科分类号：

090105 [作物生产系统与生态工程];

摘要：

Signal Transducers and Activators of Transcription (STATs) are key components of the JAK/STAT pathway. Of the seven STATs, STAT5A and STAT5B are of particular interest for their critical roles in cellular differentiation, adipogenesis, oncogenesis, and immune function. The interactions of STAT5A and STAT5B with cytokine/hormone receptors, nuclear receptors, transcriptional regulators, proto-oncogenes, kinases, and phosphatases all contribute to modulating STAT5 activity. Among these STAT5 interacting proteins, some serve as coactivators or corepressors to regulate STAT5 transcriptional activity and some proteins can interact with STAT5 to enhance or repress STAT5 signaling. In addition, a few STAT5 interacting proteins have been identified as positive regulators of STAT5 that alter serine and tyrosine phosphorylation of STAT5 while other proteins have been identified as negative regulators of STAT5 via dephosphorylation. This review article will discuss how STAT5 activity is modulated by proteins that physically interact with STAT5.

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页数：16

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