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Title:

Inability to phosphorylate Y88 of p27Kip1 enforces reduced p27 protein levels and accelerates leukemia progression.

Document type:
Journal Article; Research Support, Non-U.S. Gov't
Author(s):
Jäkel, Heidelinde; Taschler, Martin; Jung, Karin; Weinl, Christina; Pegka, Fragka; Kullmann, Michael Keith; Podmirseg, Silvio Roland; Dutta, Sayantanee; Moser, Markus; Hengst, Ludger
Abstract:
The cyclin-dependent kinase (CDK) inhibitor p27Kip1 regulates cell proliferation. Phosphorylation of tyrosine residue 88 (Y88) converts the inhibitor into an assembly factor and activator of CDKs, since Y88-phosphorylation restores activity to cyclin E,A/CDK2 and enables assembly of active cyclin D/CDK4,6. To investigate the physiological significance of p27 tyrosine phosphorylation, we have generated a knock-in mouse model where Y88 was replaced by phenylalanine (p27-Y88F). Young p27-Y88F mice...     »
Journal title abbreviation:
Leukemia
Year:
2022
Journal volume:
36
Journal issue:
7
Pages contribution:
1916-1925
Fulltext / DOI:
doi:10.1038/s41375-022-01598-x
Pubmed ID:
http://view.ncbi.nlm.nih.gov/pubmed/35597806
Print-ISSN:
0887-6924
TUM Institution:
Experimentelle Hämatologie (Prof. Schmidt-Supprian)
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