Coronin 7 (CORO7) Antibody

Background

Coronin 7 (CORO7) is a member of the coronin protein family, distinguished by its lack of actin-binding capability, unlike other coronins. Instead, it functions as an F-actin regulator involved in directing anterograde transport from the Golgi apparatus to endosomes. CORO7 localizes to the trans-Golgi network and is essential for maintaining Golgi apparatus morphology. Its recruitment to Golgi membranes requires Src kinase activity and the integrity of the AP-1 adaptor protein complex. CORO7 interacts with the μ1-subunit of AP-1 via a tyrosine-288-based sorting signal and is phosphorylated by Src kinase, which is crucial for its membrane targeting. Additionally, CORO7 undergoes K33-linked polyubiquitination via an E3 ligase complex, influencing its function in Golgi trafficking. Notably, CORO7 does not interact with actin or participate in actin-mediated processes but plays a significant role in vesicular trafficking pathways.