Mutual Enhanced Dynamic Interactions among Three Intrinsically Disordered Proteins.

Shi Yu, Tingting Li, Zhijun Liu, Wenning Wang

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Article in JACS Au, 2025. 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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4 authors.

Shi YuDepartment of Chemistry, Institute of Biomedical Sciences and Multiscale Research Institute of Complex Systems, Fudan University, Shanghai 200438, China.

Tingting LiDepartment of Chemistry, Institute of Biomedical Sciences and Multiscale Research Institute of Complex Systems, Fudan University, Shanghai 200438, China.

Zhijun LiuNational Facility for Protein Science in Shanghai, Zhangjiang Lab, Shanghai Advanced Research Institute, Chinese Academy of Sciences, Shanghai 201210, China.

Wenning WangDepartment of Chemistry, Institute of Biomedical Sciences and Multiscale Research Institute of Complex Systems, Fudan University, Shanghai 200438, China.ORCID https://orcid.org/0000-0002-8712-0536

Funding

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6 · The paper itself

Abstract

The intrinsically disordered C-terminal domain (CTD) of the 4.1 proteins functions as a modular hub for interactions with diverse binding partners. Previous research has demonstrated that 4.1G-CTD associates with an intrinsically disordered region of the nuclear mitotic apparatus (NuMA) through dynamic interactions. Given that many binding partners of CTD consist of intrinsically disordered segments of membrane proteins, it is intriguing to explore whether CTD employs a similar binding mechanism with other partners. Here, we characterize the interaction between 4.1G-CTD and the third intracellular loop of dopamine receptor D2. Our findings reveal that 4.1G-CTD forms a dynamic complex with D2. Notably, the binding sites of D2 on 4.1G-CTD overlap with those of NuMA. However, D2 and NuMA can bind 4.1G-CTD simultaneously to form a ternary complex. Furthermore, bindings of D2 and NuMA exhibit mutual enhancement, suggesting a positive cooperativity between these two pairs of dynamic interactions. These insights shed new light on the mechanisms by which disordered proteins engage with multiple partners.

Indexed as

4.1G-CTDcooperative bindingdopamine receptor D2Intrinsically disordered proteinsNuMA

Identifiers

PMID41169557

DOI10.1021/jacsau.5c01010

PMCPMC12569655

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