TEX264: A Potential Drug Target and Biomarker for ER-Phagy Receptor in testis

Target Name: TEX264

NCBI ID: G51368

TEX264: A Potential Drug Target and Biomarker for ER-Phagy Receptor in testis

Testis is a vital organ that plays a crucial role in the male reproductive system, producing sperm and maintaining the balance of hormones. One of the critical functions of the testis is to maintain the integrity of the barrier between the body and the external environment, which is known as the testicular barrier. The testicular barrier is a vital component of the immune system and plays a significant role in the fight against infections and other harmful substances that can enter the body. One of the proteins that is expressed in the testis and is involved in this barrier function is TEX264. In this article, we will explore the potential implications of TEX264 as a drug target and biomarker for the ER-Phagy receptor.

The ER-Phagy Receptor

The endoplasmic reticulum (ER) is a complex organell

Protein Name: Testis Expressed 264, ER-phagy Receptor

Functions: Major reticulophagy (also called ER-phagy) receptor that acts independently of other candidate reticulophagy receptors to remodel subdomains of the endoplasmic reticulum into autophagosomes upon nutrient stress, which then fuse with lysosomes for endoplasmic reticulum turnover (PubMed:31006538, PubMed:31006537). The ATG8-containing isolation membrane (IM) cradles a tubular segment of TEX264-positive ER near a three-way junction, allowing the formation of a synapse of 2 juxtaposed membranes with trans interaction between the TEX264 and ATG8 proteins (PubMed:31006537). Expansion of the IM would extend the capture of ER, possibly through a 'zipper-like' process involving continued trans TEX264-ATG8 interactions, until poorly understood mechanisms lead to the fission of relevant membranes and, ultimately, autophagosomal membrane closure (PubMed:31006537). Also involved in the repair of covalent DNA-protein cross-links (DPCs) during DNA synthesis: acts by bridging VCP/p97 to covalent DNA-protein cross-links (DPCs) and initiating resolution of DPCs by SPRTN (PubMed:32152270)

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