A ubiquitination-mediated degradation system to target 14-3-3-binding phosphoproteins.

Zhaokai Li, Xiaoqiang Huang, Mohan Li, Y Eugene Chen, Zhong Wang, Liu Liu

Abstract read

In one paragraph

Article in Heliyon, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed

–field-weighted citation impact

1 · What the graph read from it

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Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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2 · The registry

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0 citing papers in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

6 authors.

Zhaokai LiDepartment of Cardiac Surgery, Cardiovascular Center, University of Michigan, Ann Arbor, MI 48109, USA.

Xiaoqiang HuangCenter for Advanced Models for Translational Sciences and Therapeutics, Department of Internal Medicine, University of Michigan, Ann Arbor, MI 48109, USA.

Mohan LiDepartment of Geriatrics, Chinese Academy of Medical Sciences, Peking Union Medical College Hospital, Beijing 100730, China.

Y Eugene ChenDepartment of Cardiac Surgery, Cardiovascular Center, University of Michigan, Ann Arbor, MI 48109, USA.

Zhong WangDepartment of Cardiac Surgery, Cardiovascular Center, University of Michigan, Ann Arbor, MI 48109, USA.

Liu LiuDepartment of Cardiac Surgery, Cardiovascular Center, University of Michigan, Ann Arbor, MI 48109, USA.

Funding

Dissecting a post-translational modification code in cardiac reprogrammingR01HL163672 · NHLBI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI WANG, ZHONG · 2022 to 2025

$1.8M

NHLBI NIH HHS R01 HL163672

6 · The paper itself

Abstract

The phosphorylation of 14-3-3 binding motif is involved in many cellular processes. A strategy that enables targeted degradation of 14-3-3-binding phosphoproteins (14-3-3-BPPs) for studying their functions is highly desirable for basic research. Here, we report a phosphorylation-induced, ubiquitin-proteasome-system-mediated targeted protein degradation (TPD) strategy that allows specific degradation of 14-3-3-BPPs. Specifically, by ligating a modified von Hippel-Lindau E3-ligase with an engineered 14-3-3 bait, we generated a protein chimera referred to as Targeted Degradation of 14-3-3-binding PhosphoProtein (TDPP). TDPP can serve as a universal degrader for 14-3-3-BPPs based on the specific recognition of the phosphorylation in 14-3-3 binding motifs. TDPP shows high efficiency and specificity to a difopein-EGFP reporter, general and specific 14-3-3-BPPs. TDPP can also be applied for the validation of 14-3-3-BPPs. These results strongly support TDPP as a powerful tool for 14-3-3 related research.

Indexed as

14-3-3PhosphorylationTargeted protein degradationUbiquitinationvon hippel-lindau

Identifiers

PMID37251884

DOI10.1016/j.heliyon.2023.e16318

PMCPMC10213371

What Socratic holds

Textmetadata

LicenceCC BY-NC-ND

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.