Arginine residues within the DNA binding domain of STAT3 promote intracellular shuttling and phosphorylation of STAT3

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Arginine residues within the DNA binding domain of STAT3 promote intracellular shuttling and phosphorylation of STAT3

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作者：Torsten Ginter^a ; Jö ; rg Fahrer^b ; Ulrike Krö ; hnert^a ; Verena Fetz^c ; Alessio Garrone^a ; Roland H. Stauber^c ; Werner Reichardt^d ; Gerhard Mü ; ller-Newen^e ; Christian Kosan^a ; Thorsten Heinzel^a ; Oliver H. Kr&auml ; mer^b ; ^{okraemer@uni-mainz.de" class="auth_mail}
关键词：Acetylation ; NES ; NLS ; Phosphorylation ; STAT1 ; STAT3
刊名：Cellular Signalling
出版年：August 2014
年：2014
卷：26
期：8
页码：1698-1706
全文大小：1365 K

文摘

•: The STAT3 DBD can modulate cytokine-dependent phosphorylation of STAT3.
•: Amino acid residues within the STAT3 DBD regulate intracellular shuttling of STAT3.
•: Conserved arginine residues in the STAT3 DBD are required for DNA binding.
•: Overexpressed STAT3 with an intact DBD can substitute for STAT1 in STAT1 null cells.
•: Exchanging homologous moieties in STAT1/STAT3 DBDs can create different phenotypes.

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