Endosome-lysosome associated apoptosis and autophagy regulator 1 (ELAPOR1)

Endosome-lysosome associated apoptosis and autophagy regulator 1 (ELAPOR1) is a conserved, transmembrane protein containing mannose-6-phosphate receptor-like domains, specifically expressed in exocrine zymogenic (secretory) cells, particularly in the human and mouse stomach[1][2][3][7]. ELAPOR1 is transcribed in response to estrogen and is a direct transcriptional target of the MIST1 (BHLHA15) transcription factor, which orchestrates cellular secretory function and architecture. ELAPOR1 is primarily localized to the trans-Golgi and late endosome/lysosome compartments and is required for normal secretory granule maturation[1]. Loss of ELAPOR1 leads to defects in granule maturation and is observed in pathologies such as gastric cancer, where its reduced expression associates with loss of cell differentiation and worse prognosis[1][2]. Functionally, ELAPOR1 is implicated in regulating autophagy and apoptosis, potentially protecting cells from death by promoting cytosolic vacuolization and facilitating autophagy[2][7]. It interacts with proteins such as HSPA5, suggesting roles in cell proliferation and stress responses. Alternative splicing produces multiple transcript variants[2][3][4][7]. No approved drugs or clinical inhibitors currently target ELAPOR1 directly.

Other names

EIG121KIAA1324Estrogen-induced gene 121 proteinEstrogen induced gene 121UNQ2426/PRO4985maba15330417C22Rik (mouse)IirInceptorInsulin inhibitory receptorRGD1310209

Drugs/modulators targeting ELAPOR1 would theoretically regulate autophagy, apoptosis, or potentially secretory granule function via modulation of endosomal/lysosomal function or interaction with chaperone proteins like HSPA5[2].