SCOC (short coiled-coil protein) is a Golgi-associated protein that functions as a positive regulator of amino acid starvation-induced autophagy. Structurally, SCOC forms a parallel left-handed coiled-coil dimer with conformational flexibility due to polar and charged residues at its core 1. The protein contains a functional LC3-interacting region (LIR) domain whose phosphorylation by autophagy-related kinases (ULK1-3, TBK1) modulates binding affinity and specificity for ATG8 family members, including LC3A-C and GABARAP proteins 2. SCOC operates within a macromolecular complex with FEZ1, ULK1, and NBR1 to regulate autophagosome formation and selective cargo delivery to lysosomes 1, 3. The SCOC-FEZ1 interaction is mediated by SCOC dimerization and the surface residue R117 1. Disease relevance includes post-stroke depression, where reduced miR-129-5p expression leads to increased FEZ1/SCOC/ULK1/NBR1 complex formation and excessive autophagy; miR-129-5p-mediated downregulation of these proteins restores neuronal function in PSD models 3. Additionally, SCOC-AS1, a long non-coding RNA, serves as a biomarker for salt sensitivity of blood pressure in cardiovascular disease contexts 4. SCOC's role in selective autophagy and protein complex stability positions it as a critical regulator of cellular homeostasis.