TAILIEUCHUNG - Báo cáo khoa học: WD-repeat-propeller-FYVE protein, ProF, binds VAMP2 and protein kinase Cf

We have recently identified a protein, consisting of seven WD repeats, pre-sumably forming a b-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)Cf. | ễFEBS Journal WD-repeat-propeller-FYVE protein ProF binds VAMP2 and protein kinase Cf Thorsten Fritzius Alexander D. Frey Marc Schweneker1 Daniel Mayeri and Karin Moelling Institute of MedicalVirology University of Zurich Switzerland Keywords protein interaction protein kinase Cf VAMP2 vesicle transport WD repeats Correspondence K. Moelling Institute of MedicalVirology University of Zurich Gloriastrasse 30 Zurich CH-8006 Switzerland Fax 41 44 6344967 Tel 41 44 6342652 E-mail moelling@ Website http Present address Institute of Microbiology ETH Zurich Switzerland fGladstone Institute of Virology and Immunology San Francisco CA USA ỊDepartment of Virology Institute for MedicalMicrobiology and Hygiene University of Freiburg Germany Received 20 December 2006 accepted 16 January 2007 doi We have recently identified a protein consisting of seven WD repeats presumably forming a b-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 Cf. 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 PKCf and the proteins form a ternary complex. VAMP2 can be phosphorylated by activated PKCf in vitro and the presence of ProF increases the PKCf-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. We have recently identified the propeller-FYVE domain identified in Fab1p YOTB VAC1p and EEA1 .

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