Abstract
Most coronin proteins rely on interaction with actin in their functions. Mammalian coronin 7 has not been shown to interact with actin, but rather to bind to the outer side of Golgi complex membranes. Targeting of coronin 7 to Golgi membranes requires the activity of Src kinase and integrity of AP-1 adaptor protein complex. Coronin 7 further physically interacts with both AP-1 and Src in vivo and in vitro and is phosphorylated by Src. Depletion of coronin 7 by RNAi results in Golgi breakdown and accumulation of arrested cargo proteins, suggesting the protein functions in the later stages of cargo sorting and export from the Golgi complex. We suggest that coronin 7 acts as a mediator of cargo vesicle formation at the trans-Golgi network (TGN) downstream of AP-1 interaction with cargo but upstream of protein kinase D dependent membrane fission.
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© 2008 Landes Bioscience and Springer Science+Business Media
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Rybakin, V. (2008). Role of Mammalian Coronin 7 in the Biosynthetic Pathway. In: Clemen, C.S., Eichinger, L., Rybakin, V. (eds) The Coronin Family of Proteins. Subcellular Biochemistry, vol 48. Springer, New York, NY. https://doi.org/10.1007/978-0-387-09595-0_10
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DOI: https://doi.org/10.1007/978-0-387-09595-0_10
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