New Study Uncovers Key Role of Exocyst Complex in Cell Function and Vesicle Fusion

[davidfremnbe]

A recent study sheds light on the crucial role of the exocyst, a large protein complex, in cell growth, division, and communication. The research reveals new functions and mechanisms that are fundamental to how molecules move across a membrane via vesicles within a cell.

Understanding these mechanisms at the basic biological level is essential for advancing research on how disruptions in these processes contribute to developmental and neurological disorders.

“This is the first time we’ve identified a role for membrane fusion within the exocyst complex, marking a breakthrough in our understanding of how it operates,” said Mary Munson, Ph.D., professor and vice chair for diversity in the Department of Biochemistry & Molecular Biotechnology, and associate vice provost for equity in science in the Office of Health Equity. Munson is a co-corresponding author on the study, which was published in Nature Structural & Molecular Biology.

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The research, conducted in collaboration with Tae-Young Yoon, Ph.D., professor of biological sciences at Seoul National University in South Korea, highlights the complex’s involvement in vesicle fusion. Prior to this study, the exocyst was thought to mainly recognize and possibly tether secretory vesicles to the cell membrane before exocytosis. This new work reveals that the exocyst plays critical roles that directly facilitate the fusion of vesicles with the cell membrane, driving cargo delivery.

“Robust regulation of exocytosis is essential for cell growth, division, and communication,” Dr. Munson explained. “Dysfunction in exocyst regulation has been linked to various physiological issues across organisms.”

"This is an exciting development for our field," Dr. Munson added, noting that the exocyst complex had not previously been shown to directly control vesicle fusion. "The complex ensures that the right vesicle reaches the right spot on the cell surface at the right time to deliver cargo. It does this by interacting with the membrane fusion protein."