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Micrographs of phosphorylated Cyclin D1 bound DDB1-AMBRA1 WD40 complex

ABSTRACT:

SUBMITTER: Ming-Yuan Su

PROVIDER: EMPIAR-12646 | biostudies-other |

REPOSITORIES: biostudies-other

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Mechanism of D-type cyclin recognition by the AMBRA1 E3 ligase receptor.

Wang Yang Y Liu Ming M Wang Shan S Mai Xinyi X Wang Xi X Teng Fei F Lyu Tianrui T Su Ming-Yuan MY Stjepanovic Goran G

Science advances 20250523 21

AMBRA1 is a tumor suppressor protein that functions as a substrate receptor in the ubiquitin conjugation system and regulates the stability of D-type cyclins and cell proliferation. Here, we present the cryo-EM structure of cyclin D1-bound AMBRA1-DDB1 complex at 3.55-Å resolution. The structure reveals a substrate interaction surface on the AMBRA1 WD40 domain that specifically binds to the C-terminal region of D-type cyclins. This interaction is dependent on the phosphorylation of Thr<sup>286</s ...[more]

PMID: 40408472

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