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WD‐repeat‐propeller‐FYVE protein, ProF, binds VAMP2 and protein kinase Cζ
Author(s) -
Fritzius Thorsten,
Frey Alexander D.,
Schweneker Marc,
Mayer Daniel,
Moelling Karin
Publication year - 2007
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2007.05702.x
Subject(s) - microbiology and biotechnology , biology , vesicle , protein kinase c , signal transducing adaptor protein , phosphorylation , biochemistry , membrane
We have recently identified a protein, consisting of seven WD repeats, presumably forming a β‐propeller, and a domain identified in Fab1p, YOTB, VAC1p, and EEA1 (FYVE) domain, ProF. The FYVE domain targets the protein to vesicular membranes, while the WD repeats allow binding of the activated kinases Akt and protein kinase (PK)Cζ. Here, we describe the vesicle‐associated membrane protein 2 (VAMP2) as interaction partner of ProF. The interaction is demonstrated with overexpressed and endogenous proteins in mammalian cells. ProF and VAMP2 partially colocalize on vesicular structures with PKCζ and the proteins form a ternary complex. VAMP2 can be phosphorylated by activated PKCζ in vitro and the presence of ProF increases the PKCζ‐dependent phosphorylation of VAMP2 in vitro . ProF is an adaptor protein that brings together a kinase with its substrate. VAMP2 is known to regulate docking and fusion of vesicles and to play a role in targeting vesicles to the plasma membrane. The complex may be involved in vesicle cycling in various secretory pathways.