Abstract:
:WT1 encodes a zinc finger protein with a key role in urogenital development that is inactivated in a subset of Wilms' tumors. This tumor suppressor gene product contains an amino-terminal dimerization domain required for trans-inhibition of wild-type WT1 activity by mutants defective for DNA binding. In the course of characterizing truncation mutants of WT1, we noted that the WT1 zinc fingers contain two functionally independent targeting signals required for nuclear localization of the protein. These novel signals lie within zinc fingers I and within zinc fingers II and III. We demonstrate that nuclear targeting of the WT1 homodimerization domain functionally antagonizes activity of the wild-type protein activity.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Bruening W,Moffett P,Chia S,Heinrich G,Pelletier Jdoi
10.1016/0014-5793(96)00853-8subject
Has Abstractpub_date
1996-09-09 00:00:00pages
41-7issue
1eissn
0014-5793issn
1873-3468pii
0014-5793(96)00853-8journal_volume
393pub_type
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