The process of recycling, which we often do with paper, glass, cans, and plastic, is also essential in our cells for reducing waste, conserving resources, and saving energy. In cellular biology, the recycling of membrane proteins is crucial for maintaining cellular function and equilibrium. A protein complex called endosomal sorting complex for promoting exit 1 (ESCPE-1) has recently been discovered as a key player in this process.

ESCPE-1 rescues transmembrane proteins from the endolysosomal pathway and ensures their safe transport to the trans-golgi network and eventually to the plasma membrane. While the importance of ESCPE-1 in recycling is well-known, the underlying mechanisms have remained a mystery. However, recent research published in the journal Nature Structural & Molecular Biology has provided valuable insights into the structure and function of ESCPE-1 in tubule-based endosomal sorting.

A multidisciplinary research team, led by Aitor Hierro, has successfully revealed the atomic-level architecture of ESCPE-1. This protein complex is responsible for transporting and reusing over 60 different proteins. The study has enhanced our understanding of how ESCPE-1 mediates tubular-based cargo sorting through membrane interactions, cargo recognition, and coat formation. This knowledge is crucial for understanding membrane protein recycling and its role in cellular processes.

Aitor Hierro explains, “Many of the proteins transported and reused by this cellular machinery for protein recycling are cell receptors involved in cell growth and proliferation, and they appear dysregulated in different types of cancer. In this study, we have revealed the organization of ESCPE-1 at the atomic level and how the receptors to be recycled contribute to their own transport. Going back to the analogy of paper, glass, cans, and plastic, it is like discovering the mechanism of selective collection for one of these containers.”

The research was conducted over the past five years and utilized two important techniques in structural biology: X-ray crystallography and cryo-electron microscopy. The collaborative effort between CIC bioGUNE, the Biofisika Institute, the National Institutes of Health (NIH), the Barcelona Supercomputing Center, and the Institute of Vine and Wine Sciences has successfully revealed the intricate workings of ESCPE-1.

 

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