tailieunhanh - Báo cáo khoa học: PACSIN 1 forms tetramers via its N-terminal F-BAR domain

The ability of protein kinase C and casein kinase 2 substrate in neurons (PACSIN)⁄syndapin proteins to self-polymerize is crucial for the simulta-neous interactions with more than one Src homology 3 domain-binding partner or with lipid membranes. | ỊFEBS Journal PACSIN 1 forms tetramers via its N-terminal F-BAR domain Arndt Halbach1 Matthias Morgelin2 Maria Baumgarten2 Mark Milbrandt1 Mats Paulsson1 and Markus Plomann1 1 Center for Biochemistry and Center for Molecular Medicine CMMC MedicalFaculty University of Cologne Germany 2 Department of ClinicalSciences Section for Clinicaland ExperimentalInfectious Medicine University of Lund Sweden Keywords F-BAR domain membrane oligomerization PACSIN 1 syndapin 1 Correspondence M. Plomann Center for Biochemistry MedicalFaculty University of Cologne Joseph-Stelzmann-Str. 52 D-50931 Cologne Germany Fax 49 221 478 6977 Tel 49 221 478 6944 E-mail Received 13 October 2006 revised 23 November 2006 accepted 4 December 2006 doi The ability of protein kinase C and casein kinase 2 substrate in neurons PACSIN syndapin proteins to self-polymerize is crucial for the simultaneous interactions with more than one Src homology 3 domain-binding partner or with lipid membranes. The assembly of this network has profound effects on the neural Wiskott-Aldrich syndrome protein-mediated attachment of the actin polymerization machinery to vesicle membranes as well as on the movement of the corresponding vesicles. Also the sensing of vesicle membranes and or the induction of membrane curvature are more easily facilitated in the presence of larger PACSIN complexes. The N-ter-minal Fes-CIP homology and Bin-Amphiphysin-Rvs F-BAR domains of several PACSIN-related proteins have been shown to mediate self-interactions whereas studies using deletion mutants derived from closely related proteins led to the view that oligomerization depends on the formation of a trimeric complex via a coiled-coil region present in these molecules. To address whether the model of trimeric complex formation is applicable to PACSIN 1 the protein was recombinantly expressed and tested in four different assays for homologous interactions. The results showed that