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Coronin-7 (CORO7) is a member of the coronin family of WD-repeat proteins, distinguished by containing two stretches of WD-40 repeats, in contrast to most other coronins which have one. Unlike conventional coronins which bind actin directly, Coronin-7 functions primarily as a regulator of F-actin organization and is essential for post-Golgi trafficking, maintenance of Golgi apparatus morphology, and anterograde transport from Golgi to endosomes. It localizes mainly to the trans-Golgi network and the cytoplasm. Its role is further modulated via post-translational modifications such as phosphorylation and ubiquitination. Mutations or deficiencies in Coronin-7 are associated with genetic disorders such as spondyloepimetaphyseal dysplasia, Strudwick type. Currently, there is no evidence supporting its use as a therapeutic target, biomarker, or as having known drug interactions based on available data.
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