The ER-Golgi intermediate compartment (ERGIC) is a crucial membrane system that lies between the rough endoplasmic reticulum (ER) and the Golgi apparatus. It plays a significant role in the transport of proteins and lipids from the ER to the Golgi. ERGIC-53, a 53 kDa membrane protein, is a well-known marker of this compartment .
The ERGIC is composed of tubulovesicular membrane clusters that serve as mobile transport complexes. These clusters facilitate the delivery of secretory cargo from ER-exit sites to the Golgi . The dynamic nature of the ERGIC has been a subject of extensive research, with recent studies suggesting that it functions as a stable compartment where ER-derived cargo is first shuttled from ER-exit sites to stationary ERGIC clusters in a COPII-dependent step. Subsequently, the cargo is transported to the Golgi in a second vesicular transport step .
The ERGIC is not only involved in the transport of proteins but also plays a critical role in the concentration, folding, and quality control of newly synthesized proteins. It acts as a major site for anterograde and retrograde sorting, which is regulated by coat proteins, Rab and Arf GTPases, tethering complexes, SNAREs, and cytoskeletal networks .
Human recombinant ERGIC3 refers to the ERGIC3 protein that has been produced using recombinant DNA technology. This involves inserting the gene encoding ERGIC3 into a suitable expression system, such as bacteria or yeast, to produce the protein in large quantities. Recombinant proteins are essential for various research and therapeutic applications, as they allow for the study of protein function and the development of targeted treatments.