Intramolecular interaction of B‐MYB is regulated through Ser‐577 phosphorylation

The transcription factor B‐MYB is an important regulator of cell cycle‐related processes that is activated by step‐wise phosphorylation of multiple sites by cyclin‐dependent kinases (CDKs) and conformational changes induced by the peptidylprolyl cis/trans isomerase Pin1. Here, we show that a conserv...

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Bibliographic Details
Published in:FEBS letters 2020-12, Vol.594 (24), p.4266-4279
Main Authors: Werwein, Eugen, Biyanee, Abhiruchi, Klempnauer, Karl‐Heinz
Format: Article
Language:English
Subjects:
B‐MYB
cyclin‐dependent kinase
DNA‐binding domain
phosphatase
phosphorylation
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Summary:The transcription factor B‐MYB is an important regulator of cell cycle‐related processes that is activated by step‐wise phosphorylation of multiple sites by cyclin‐dependent kinases (CDKs) and conformational changes induced by the peptidylprolyl cis/trans isomerase Pin1. Here, we show that a conserved amino acid sequence around Ser‐577 in the C‐terminal part of B‐MYB is able to interact with the B‐MYB DNA‐binding domain. Phosphorylation of Ser‐577 disrupts this interaction and is regulated by the interplay of CDKs and the phosphatase CDC14B. Deletion of sequences surrounding Ser‐577 hyperactivates the transactivation potential of B‐MYB, decreases its proteolytic stability, and causes cell cycle defects. Overall, we show for the first time that B‐MYB can undergo an intramolecular interaction that is controlled by the phosphorylation state of Ser‐577.
ISSN:0014-5793
1873-3468
DOI:10.1002/1873-3468.13940