Proteomics

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Proteomic analysis of the physiological E3 ubiquitin ligase responsible for PIN1 degradation

ABSTRACT: Induced oncoproteins degradation provides an attractive anti-cancer modality. Activation of anaphase-promoting complex (APC/CCDH1) prevents cell cycle entry by targeting crucial mitotic proteins for degradation. Phosphorylation of its co-activator CDH1 modulates the E3 ligase activity, but little is known about its regulation after phosphorylation and how to effectively harness APC/CCDH1 activity to treat cancer. Notably, Proline-directed phosphorylation is regulated by PIN1-catalyzed cis-trans prolyl isomerization to drive tumor malignancy. However, the mechanisms controlling its protein turnover remain elusive. Through proteomic screens, we identify a reciprocal antagonism of PIN1-APC/CCDH1 mediated by domain-oriented phosphorylation-dependent dual interactions as a fundamental mechanism governing mitotic protein stability and cell cycle entry.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

DISEASE(S): Breast Cancer

SUBMITTER: Wenxue Li  

LAB HEAD: Yansheng Liu

PROVIDER: PXD046325 | Pride | 2024-02-28

REPOSITORIES: Pride

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Publications

Cyclin-dependent kinases (CDKs) mediated phosphorylation inactivates the anaphase-promoting complex (APC/C<sup>CDH1</sup>), an E3 ubiquitin ligase that contains the co-activator CDH1, to promote G1/S transition. PIN1 is a phosphorylation-directed proline isomerase and a master cancer signaling regulator. However, little are known about APC/C<sup>CDH1</sup> regulation after phosphorylation and about PIN1 ubiquitin ligases. Here we uncover a domain-oriented reciprocal inhibition that controls the  ...[more]

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