WD-repeat-propeller-FYVE protein, ProF, binds VAMP2 and protein kinase Cζ

Thorsten Fritzius, Alexander D. Frey, Marc Schweneker, Daniel Mayer, Karin Moelling*

*Corresponding author for this work

Research output: Contribution to journalArticleScientificpeer-review

18 Citations (Scopus)


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 PKCζin 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.

Original languageEnglish
Pages (from-to)1552-1566
Number of pages15
Issue number6
Publication statusPublished - Mar 2007
MoE publication typeA1 Journal article-refereed


  • Protein interaction
  • Protein kinase Cζ
  • VAMP2
  • Vesicle transport
  • WD repeats

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