Abstract:
:Growth factors such as epidermal growth factor (EGF) and insulin regulate development and metabolism via genes containing both POU homeodomain (Pit-1) and phorbol ester (AP-1) response elements. Although CREB binding protein (CBP) functions as a coactivator on these elements, the mechanism of transactivation was previously unclear. We now demonstrate that CBP is recruited to these elements only after it is phosphorylated at serine 436 by growth factor-dependent signaling pathways. In contrast, p300, a protein closely related to CBP that lacks this phosphorylation site, binds only weakly to the transcription complex and in a growth factor-independent manner. A small region of CBP (amino acids 312-440), which we term GF box, contains a potent transactivation domain and mediates this effect. Direct phosphorylation represents a novel mechanism controlling coactivator recruitment to the transcription complex.
journal_name
Mol Celljournal_title
Molecular cellauthors
Zanger K,Radovick S,Wondisford FEdoi
10.1016/s1097-2765(01)00202-7subject
Has Abstractpub_date
2001-03-01 00:00:00pages
551-8issue
3eissn
1097-2765issn
1097-4164pii
S1097-2765(01)00202-7journal_volume
7pub_type
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