VPS52

Vps52 is a protein found in yeast and other eukaryotes. It is a component of the yeast vacuolar protein sorting complex, also known as the GARP complex. This complex plays a crucial role in the retrograde transport of proteins from the Golgi apparatus to the endoplasmic reticulum. Specifically, Vps52 is a subunit of the GARP complex that is involved in binding to specific protein targets, thereby ensuring their correct localization and function.

The GARP complex, with Vps52 as a key member, is essential for maintaining the integrity of the secretory pathway. Disruptions in GARP complex function, including mutations in Vps52, can lead to mislocalization of proteins, affecting various cellular processes. Research has shown that Vps52 interacts with other GARP complex subunits, such as Vps53, Vps54, and Vps51, to form a functional unit. These interactions are critical for the recruitment of the complex to the Golgi membrane and for its ability to mediate protein transport.

Studies have utilized genetic and biochemical approaches to elucidate the role of Vps52. For instance, deletion of the VPS52 gene in yeast results in observable defects in vacuolar protein sorting. The protein has also been investigated in the context of autophagy, another essential cellular process. While the primary role of Vps52 is established within the GARP complex and retrograde transport, ongoing research continues to explore its potential involvement in other cellular functions and pathways. The conservation of Vps52 homologs across different species suggests a fundamental importance for this protein in eukaryotic cell biology.