JAK-STAT最新文献_第5页

JAK2-STAT5 signaling: A novel mechanism of resistance to targeted PI3K/mTOR inhibition. JAK2-STAT5信号传导:靶向PI3K/mTOR抑制的新机制

JAK-STAT Pub Date : 2013-10-01 Epub Date: 2013-04-15 DOI: 10.4161/jkst.24635

Jennifer E Yeh, Patricia A Toniolo, David A Frank

引用次数: 10

Interaction of JAK with steroid receptor function. JAK与类固醇受体功能的相互作用。

JAK-STAT Pub Date : 2013-10-01 Epub Date: 2013-05-07 DOI: 10.4161/jkst.24911

Nibedita Gupta, Doris Mayer

引用次数: 21

The role of the JAK-STAT pathway and related signal cascades in telomerase activation during the development of hematologic malignancies. JAK-STAT通路和相关信号级联在血液恶性肿瘤发展过程中端粒酶激活中的作用。

JAK-STAT Pub Date : 2013-10-01 Epub Date: 2013-06-12 DOI: 10.4161/jkst.25256

Osamu Yamada, Kiyotaka Kawauchi

引用次数: 38

IL-6-STAT3 signaling and premature senescence. IL-6-STAT3信号与早衰。

JAK-STAT Pub Date : 2013-10-01 Epub Date: 2013-07-22 DOI: 10.4161/jkst.25763

Hirotada Kojima, Toshiaki Inoue, Hiroyuki Kunimoto, Koichi Nakajima

引用次数: 127

Oxidative metabolism in cancer: A STAT affair? 癌症中的氧化代谢:STAT事件?

JAK-STAT Pub Date : 2013-10-01 Epub Date: 2013-08-12 DOI: 10.4161/jkst.25764

Jérome Bourgeais, Valérie Gouilleux-Gruart, Fabrice Gouilleux

引用次数: 37

The role of a non-canonical JAK-STAT pathway in IFN therapy of poxvirus infection and multiple sclerosis: An example of Occam's Broom? 非经典 JAK-STAT 通路在 IFN 治疗痘病毒感染和多发性硬化症中的作用：奥卡姆扫帚定律的实例？

JAK-STAT Pub Date : 2013-10-01 Epub Date: 2013-09-04 DOI: 10.4161/jkst.26227

Chulbul M Ahmed, Howard M Johnson

{"title":"The role of a non-canonical JAK-STAT pathway in IFN therapy of poxvirus infection and multiple sclerosis: An example of Occam's Broom?","authors":"Chulbul M Ahmed, Howard M Johnson","doi":"10.4161/jkst.26227","DOIUrl":"10.4161/jkst.26227","url":null,"abstract":"Signaling by cytokines such as the interferons (IFNs) involves Janus kinases (JAKs) and signal transducer and activator of transcription (STAT) transcription factors. The beauty of the classical model of JAK-STAT signaling is its simplicity in that JAK-activated STATs in the nucleus are responsible for specific gene activation. The fact that many ligands, growth factors, and hormones use the same STAT transcription factors, but exert different functions at the level of the cell, tissue, and organ would suggest significant shortcomings in the classical model. Our studies have resulted in the development of a non-canonical, more complex model of IFN signaling that bears a striking resemblance to that of steroid hormone (SH)/steroid receptor (SR) signaling. Thus, both types I and II IFN signaling involves nuclear translocation of complexed ligand, receptor, activated JAKs, and activated STATs to the promoters of the genes that are specifically activated by the IFNs, where they are involved in specific gene activation and epigenetic remodeling. Receptor intracellular domains play an important role in binding the C-terminus of the IFNs, which is the basis for our development of IFN mimetics. The IFN mimetics are not recognized by poxvirus decoy receptors, since the decoy receptors compete for extracellular binding and not intracellular binding. Further, the type I IFN mimetics provide therapeutic protection against experimental allergic encephalomyelitis (EAE), a model of multiple sclerosis, without the side effects. Extracellular receptor binding by intact IFN is the primary reason for undesirable side effects of flu-like symptoms, bone-marrow suppression, and weight loss. The non-canonical model of IFN signaling thus provides insight into the specificity of such signaling and a mechanism for development of IFN mimetics. It is our contention that this model applies to other cytokines. ","PeriodicalId":89791,"journal":{"name":"JAK-STAT","volume":"2 4","pages":"e26227"},"PeriodicalIF":0.0,"publicationDate":"2013-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/ab/02/jkst-2-e26227.PMC3876437.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"32023647","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

STAT5 in hematopoietic stem cell biology and transplantation. STAT5在造血干细胞生物学和移植中的作用。

JAK-STAT Pub Date : 2013-10-01 Epub Date: 2013-11-19 DOI: 10.4161/jkst.27159

Zhengqi Wang, Kevin D Bunting

引用次数: 29

JAK-STAT signaling and myocardial glucose metabolism. JAK-STAT信号与心肌葡萄糖代谢。

JAK-STAT Pub Date : 2013-10-01 Epub Date: 2013-09-27 DOI: 10.4161/jkst.26458

Miguel A Frias, Christophe Montessuit

引用次数: 24

STATs get their move on. STATs 开始行动。

JAK-STAT Pub Date : 2013-10-01 Epub Date: 2013-11-13 DOI: 10.4161/jkst.27080

Nancy C Reich

{"title":"STATs get their move on.","authors":"Nancy C Reich","doi":"10.4161/jkst.27080","DOIUrl":"10.4161/jkst.27080","url":null,"abstract":"Understanding the mechanisms that regulate dynamic localization of a protein within a cell can provide critical insight to its functional molecular interactions. Signal transducers and activators of transcription (STATs) play essential roles in development, proliferation, and immune defense. However the consequences of STAT hyperactivity can predispose to diseases including autoimmunity and cancer. To function as transcription factors STATs must gain access to the nucleus, and knowledge of the mechanisms that regulate STAT nuclear trafficking can provide a means to control STAT action. This review presents a synopsis of some of the studies that address the nuclear dynamics of the STAT proteins. Evidence suggests that not all STATs are the same. Nuclear import of STAT1 and STAT4 appears linked to their tyrosine phosphorylation and the formation of parallel dimers via reciprocal phosphotyrosine and Src homology 2 domain interactions. This dimer arrangement generates a conformational nuclear localization signal. STAT2 is imported continually to the nucleus in an unphosphorylated state due to its association with IRF9, but the dominant nuclear export signal of STAT2 shuttles the complex back to the cytoplasm. Following STAT2 tyrosine phosphorylation, it can form dimers with STAT1 to affect nuclear import as the trimeric complex (ISGF3). Distinctly, STAT3, STAT5, and STAT6 are continually imported to the nucleus independent of tyrosine phosphorylation. Mutational studies indicate the nuclear localization signals in these STATs require the conformational structure of their coiled-coil domains. Increases in STAT nuclear accumulation following cytokine stimulation appear coordinate with their ability to bind DNA. ","PeriodicalId":89791,"journal":{"name":"JAK-STAT","volume":"2 4","pages":"e27080"},"PeriodicalIF":0.0,"publicationDate":"2013-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3891633/pdf/jkst-2-e27080.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"32067675","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

JAK-STAT and intestinal mucosal immunology. JAK-STAT与肠黏膜免疫。

JAK-STAT Pub Date : 2013-10-01 Epub Date: 2013-06-26 DOI: 10.4161/jkst.25530

Aaron F Heneghan, Joseph F Pierre, Kenneth A Kudsk

引用次数: 45