|
|
|
|
|
|
|
||
| ||||||||||||||||||||||||||
Index of Online Supplemental Material for
J. Cell Biol. 10.1083/jcb.200604073
Kawashima et al.
• Figure S1 STAT5A and Rac1 interact with MgcRacGAP in the cys-rich and GAP domains, whereas MgcRacGAP interacts with the DNA-binding domain of STAT5A.
• Figure S2 A dominant-negative mutant of Rac1, N17Rac1, prevented p-STAT5 from translocating to the nucleus.
• Figure S3 The mutant of STAT3, which lack MgcRacGAP binding site, did not bind MgcRacGAP and lost transcriptional activities.
• Figure S4 The molecular weight and the DNA-binding activity of the in vivo or in vitro phosphorylated recombinant STAT5A were identical to those of the endogenous STAT5A.
• Figure S5 The in vitro phosphorylated recombinant STAT5A required GTP-bound Rac1 and MgcRacGAP as well as import factors of the importin/Ran system to enter the nucleus in the nuclear transport assay.
| ||||||||||||||||||||||||||
|
|
