GOSR1 (Golgi SNAP receptor complex member 1) is a t-SNARE protein localized to chromosome 17 that functions primarily in vesicular transport. It mediates docking and fusion of transport vesicles during ER-to-Golgi and intra-Golgi trafficking, playing a critical role in VLDL delivery to hepatic cis-Golgi 1. GOSR1 contains a SNARE domain that facilitates membrane fusion events essential for protein transport through the secretory pathway. Beyond canonical trafficking functions, GOSR1 negatively regulates NRF2 (nuclear factor erythroid 2-like 2), a master transcription factor controlling cellular stress responses 2. This regulatory role connects GOSR1 to autophagy pathways, as knockout of GOSR1 leads to sustained NRF2 activation, suggesting GOSR1 functions as an autophagy-dependent NRF2 suppressor. Additionally, GOSR1 regulates GLUT4 trafficking in human cells, identifying it as a potential modulator of glucose homeostasis 3. Disease relevance includes stress urinary incontinence, where GOSR1 is overexpressed in affected patients, implicating cytoskeletal and extracellular matrix dysregulation 4. GOSR1 has also been identified in gene fusion events in breast implant-associated anaplastic large-cell lymphoma (NF1-GOSR1 fusion), suggesting potential oncogenic involvement 5. These findings position GOSR1 as a multifunctional trafficking protein with emerging roles in stress response regulation and disease pathogenesis.