Calreticulin (CALR) is a pleiotropic and highly conserved molecule and is recognized as an unfolded protein response effector protein. Moreover, CALR is an endoplasmic reticulum protein involved in a range of cellular processes. CALR can be translocated from the endoplasmic reticulum to the cell surface through co-localization with protein disulfide isomerase family A member 3 (PDIA3).1 Furthermore, CALR mutations affected the spindle assembly checkpoint, leading to erroneous mitosis.2 In particular, the loss-of-function CALR mutations not only impair cellular homeostasis but also compromise both natural and therapy-driven immune surveillance, thereby promoting tumorigenesis.3 Also, CALR frameshift mutations, a primary cause of myeloproliferative neoplasms, lead to rogue interactions with the thrombopoietin receptor (TpoR).4 Type I CALR mutations, but not type II, activate the inositol-requiring enzyme 1α (IRE1α)/X-box binding protein 1 (XBP1) pathway of the unfolded protein response, driving the development of myeloproliferative neoplasms.5 In this study, we demonstrate that CALR accelerates the growth of liver cancer cells by enhancing telomere activity dependent on ARAF (A-Raf proto-oncogene, serine/threonine kinase). Therefore, these results provide a basis for research on liver cancer prevention and treatment.