Work

The DID of CAPS-1 anchors plasma membrane to promote vesicle exocytosis

Year: 2025

Type: article

Abstract: -dependent activator proteins for secretion contain a dynactin1-interacting domain (DID), previously implicated in vesicle sorting. Here, we reveal a novel role for the DID in direct membrane association. Using structural modeling, liposome binding, and fusion assays, we demonstrate that the DID binds to and clusters negatively charged phospholipids, such as phosphatidylserine and phosphatidylinositol 4,5-bisphosphate, and significantly enhances SNARE-mediated liposome fusion. Furthermore, deletion of the DID in PC12 cells impairs evoked vesicle release. Our findings establish the DID as a critical plasma membrane-anchoring module that promotes efficient vesicle exocytosis.

Source: Journal of Biological Chemistry

DOI: 10.1016/j.jbc.2025.110902

Authors: Li Zhang, Yuwan Dai, Ting Sun, Wanhai Wang, Ziqing Wei

Institutions: Zhengzhou University, First Affiliated Hospital of Zhengzhou University, Henan Provincial People's Hospital

Language: English

Topic: Cellular transport and secretion

Subfield: Cell Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: gold

Estimated APC paid: $3,430

Funders: National Natural Science Foundation of China, Zhengzhou University, Natural Science Foundation of Henan Province, First Affiliated Hospital of Zhengzhou University