tailieunhanh - Báo cáo khoa học: Ion channel activity of brain abundant protein BASP1 in planar lipid bilayers

BASP1 (also known as CAP-23 and NAP-22) is a brain abundant myri-stoylated protein localized at the inner surface of the presynaptic plasma membrane. Emerging evidence suggests that BASP1 is critically involved in various cellular processes, in particular, in the accumulation of phosphati-dylinositol-4,5-diphosphate (PIP2) in lipid raft microdomains. | IFEBS Journal Ion channel activity of brain abundant protein BASP1 in planar lipid bilayers Olga S. Ostroumova1 Ludmila V. Schagina1 Mark I. Mosevitsky2 and Vladislav V. Zakharov2 1 Laboratory of Ionic Channels of CellMembranes Institute of Cytology of RAS St Petersburg Russia 2 Division of Molecular and Radiation Biophysics Petersburg Nuclear Physics Institute of RAS Gatchina Leningrad District Russia Keywords amyloid proteins BASP1 ion channels lipid bilayer protein oligomers Correspondence V. V. Zakharov Division of Molecular and Radiation Biophysics Petersburg Nuclear Physics Institute of Russian Academy of Sciences 188300 Gatchina Leningrad District Russia Fax 7 813 7132303 Tel 7 812 3282802 E-mail Received 23 September 2010 revised 14 November 2010 accepted 18 November 2010 doi BASP1 also known as CAP-23 and NAP-22 is a brain abundant myri-stoylated protein localized at the inner surface of the presynaptic plasma membrane. Emerging evidence suggests that BASP1 is critically involved in various cellular processes in particular in the accumulation of phosphati-dylinositol-4 5-diphosphate PIP2 in lipid raft microdomains. We have recently shown that BASP1 forms heterogeneously-sized oligomers and higher aggregates with an outward similarity to oligomers and protofibrils of amyloid proteins. However BASP1 is not known to be related to any amyloid disease. In the present study we show that BASP1 induces single channel currents across negatively-charged planar lipid bilayers containing phosphatidylserine or PIP2 bathed in M KCl pH . By their characteristics BASP1 channels are similar to amyloid protein channels. BASP1 channels exhibit multiple conductance levels in the range 10-3000 pS with the most frequently observed conductance state of approximately 50 pS. The channels demonstrate a linear current-voltage relationship and voltage-independent kinetics of opening and closing. Their K to Cl .

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