Signal Transducers and Activators of Transcription (STATs): by James E. Darnell Jr. (auth.), Pravin B. Sehgal, David E.

By James E. Darnell Jr. (auth.), Pravin B. Sehgal, David E. Levy, Toshio Hirano (eds.)

The yr 2003 marks the 10th anniversary of the 1st use of the acronym "Stat" (also written "STAT") within the medical literature for a family members of transcription components which speedily transduce cytokine-and progress issue­ elicited signs from the plasma membrane to the cellphone nucleus thereby activating gene transcription (thus, . s. ignal Transducers and Activators of Transcription). From these beginnings, the sphere of STAT transcription elements, their similar regulatory molecules and their biology has grown exponentially in lots of various instructions. In popularity of the fast development and huge scope of the STAT transcription issue box this present day, and to rejoice the 10th anniversary of using this time period within the medical literature, Kluwer educational Publishers B. V. asked us to bring together a quantity on STAT transcription components which can function an summary of this burgeoning sector. hence, we needed a quantity that may function a reference for what's recognized approximately STAT proteins and their biology, might describe the present kingdom of ongoing learn during this vast quarter, and might glance towards the long run to aim to foretell the discoveries that lie forward. Our cost was once to search out some of the best specialists within the box and to coax them to in short summarize their parts of expertise.

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12. 13. 14. 15. 16. 17. 18. 19. 20. 21. 22. 23. 24. 25. 26. 27. , Aebersold, R. and Darnell, J. , Jr. , Aebersold, R. and Damell, J. , Jr. (1992) Proc Natl Acad Sci USA 89, 7836-7839 Levy, D. and Darnell, J. , Jr. (1990) New Biologist 2,923-928 St-Johnston, D. and Nusslein-Volhard, C. (1992) Cell 68, 201-219 Nusslein-Volhard, C. and Wieshaus, E. (1980) Nature 287,795-801 Lamer, A. , Jr. and Darnell, J. , Jr. (1984) Proc Natl Acad Sci USA 81, 6733-6737 Lamer, A. , Chaudhuri, A. and Damell, J. , Jr.

The exposed position of this domain predestines it for interactions with other proteins as well as with other domains within a STAT protein (intramolecular interactions with potentially regulatory functions). Several interactions with other proteins have been described. The coiled-coil domain of STATl interacts with IRF9 (formerly p48), a component of interferon stimulated gene factor 3 (ISGF3) (25). The coiledcoil domains of all STATs except STAT2 can interact with N-myc interactor (Nmi), and in the case of STATl and STAT5 this interaction has been shown to augment STAT mediated transcription in response to IFNy and IL-2, respectively (26).

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