Protein disulfide-isomerase-like protein of the testis (PDILT)

Protein disulfide-isomerase-like protein of the testis (PDILT) is a testis-specific member of the protein disulfide isomerase (PDI) family that functions as a redox-inactive chaperone, uniquely expressed in postmeiotic male germ cells during spermatid differentiation and spermatogenesis[1][2][3][4][5]. Unlike many PDI family proteins, PDILT lacks the canonical catalytic cysteines required for oxidoreductase activity and instead operates via chaperone-mediated protein folding in the endoplasmic reticulum, where it forms a complex with the testis-specific lectin chaperone calmegin[1][2][4]. This partnership is critical for the maturation of sperm cells and proper folding of spermatogenesis-specific glycoproteins[2]. Mutations or deficiencies in PDILT or its partners result in male infertility due to defective sperm differentiation or acrosome formation[1][2]. PDILT is not known as a direct drug target or therapeutic receptor/enzyme/transporter and no drugs are currently reported to interact with it[3][4][5].

Other names

PDILTPDIA7Protein disulfide isomerase family A member 7Protein disulfide-isomerase-like protein of the testis