Ergic1, encoding a putative transmembrane protein at the ER-Golgi interface, may play a role in protein trafficking between the endoplasmic reticulum and Golgi [2]. This function is crucial for normal cellular activities as proper protein transport is essential for various biological processes within the cell.

Mutations in Ergic1 have been associated with several human diseases. Homozygous missense variants or complete loss-of-function mutations in Ergic1 cause relatively mild non-syndromic arthrogryposis, a condition characterized by multiple joint-contractures [1,2]. In addition, aberrant expression of Ergic1 may be involved in the initiation and progression of gastric cancer. Its expression gradually decreases from normal gastric mucosa to early mucosal gastric cancer, and overexpression of Ergic1 in gastric cancer cell lines inhibits cell proliferation and enhances apoptosis [3,4]. In prostate cancer, ERGIC1 silencing specifically regulates the proliferation of ERG oncogene-positive prostate cancer cells, indicating it could be a potent drug target in this subgroup of prostate cancers [5].

In conclusion, Ergic1 is important for protein trafficking at the ER-Golgi interface. Its dysfunction, as revealed through genetic mutations in human studies, is associated with arthrogryposis and may play roles in the development of gastric and prostate cancers. Understanding Ergic1's function provides insights into the mechanisms of these diseases and potential therapeutic targets.