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Transmembrane protein 87A (TMEM87A) is a eukaryotic transmembrane protein with a conserved structure consisting of an extracellular GOLD (Golgi-dynamics) domain atop a seven-transmembrane domain. It is part of a larger family of structurally related GOST proteins, which includes TMEM87B, GPR107, GPR108, WLS, GPR180, TMEM145, and TMEM181. TMEM87A is highly expressed in the Golgi of various cells and has been implicated in protein trafficking processes, particularly in regulating retrograde traffic from endosomes to the Golgi. Some studies have proposed a role in mechanosensitive or voltage-dependent cation channel activity, especially in the context of the Golgi apparatus, though direct evidence for ion channel activity remains controversial and structurally TMEM87A lacks many canonical features of established ion channels or GPCRs. Disruption of TMEM87A function has been associated with impaired protein trafficking, increased cell adhesion, and decreased migration in cancer models, as well as developmental anomalies. Although its potential as a new type of channel or a trafficking regulator is being investigated, TMEM87A's precise mechanisms and druggability are still under study
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