NDLI: Molecular mechanism underlying the association of Coronin-7 with Golgi membranes

Content Provider	Springer Nature Link
Author	Rybakin, V. Rastetter, R. H. Stumpf, M. Uetrecht, A. C. Bear, J. E. egel, A. A. Clemen, C. S.
Copyright Year	2008
Abstract	Coronin-7 (Crn7) is a ubiquitous mammalian WD40-repeat protein that localizes to the Golgi complex, interacts with AP-1 adaptor complex via binding of a tyrosine-288-based sorting signal to the μ1-subunit of AP-1, and participates in the maintenance of the Golgi structure and function. Here, we define the requirements for the recruitment of Crn7 from the cytosol to the Golgi. We establish that Src activity is indispensable for the interaction of Crn7 with Golgi membranes. Crn7 binds Src in vivo and can be phosphorylated by recombinant Src in vitro. We demonstrate that tyrosine-758 is the major Src phosphorylation site. Further, to be targeted to membranes Crn7 requires the presence of cargo in the Golgi complex. Finally, downregulation of the μ1-subunit of AP-1 leads to the dispersal of Crn7 from the Golgi membranes. We propose a mechanism whereby sequential events of protein interaction and posttranslational modification result in the membrane targeting of Crn7.
Starting Page	2419
Ending Page	2430
Page Count	12
File Format	PDF
ISSN	1420682X
Journal	Cellular and Molecular Life Sciences
Volume Number	65
Issue Number	15
e-ISSN	14209071
Language	English
Publisher	SP Birkhäuser Verlag Basel
Publisher Date	2008-06-26
Publisher Place	Basel
Access Restriction	Subscribed
Subject Keyword	Coronin family Golgi complex Src phosphorylation membrane binding Biochemistry Life Sciences Biomedicine general Cell Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Molecular Biology Molecular Medicine Pharmacology Cellular and Molecular Neuroscience

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