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MBC in Press, published online ahead of print December 25, 2002
Mol. Biol. Cell 10.1091/mbc.E02-09-0622

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Submitted on September 30, 2002
Revised on November 20, 2002
Accepted on December 9, 2002

Regulation of sodium channel activity by capping of actin filaments

Ekaterina V. Shumilina1, Yuri A. Negulyaev1*, Elena A. Morachevskaya1, Horst Hinssen2, and Sofia Yu. Khaitlina1

1 Institute of Cytology RAS, 4 Tikhoretsky Ave., St. Petersburg 194064, Russia
2 Department of Biochemical Cell Biology, University of Bielefeld, 33501 Bielefeld, Germany

* Corresponding author. E-mail address: yurineg{at}link.cytspb.rssi.ru.

Ion transport in various tissues can be regulated by the cortical actin cytoskeleton. Specifically, involvement of actin dynamics in the regulation of non-voltage-gated sodium channels has been shown. Here, inside-out patch clamp experiments were performed to study the effect of the heterodimeric actin capping protein CapZ on sodium channel regulation in leukemia K562 cells. The channels were activated by cytochalasin-induced disruption of actin filaments and inactivated by G-actin under ionic conditions promoting rapid actin polymerization. CapZ had no direct effect on channel activity. However, being added together with G-actin, CapZ prevented actin-induced channel inactivation, and this effect occurred at CapZ/actin molar ratios from 1:5 to 1:100. When actin was allowed to polymerize at the plasma membrane to induce partial channel inactivation, subsequent addition of CapZ restored the channel activity. These results can be explained by CapZ-induced inhibition of further assembly of actin filaments at the plasma membrane due to the modification of actin dynamics by CapZ. No effect on the channel activity was observed in response to F-actin confirming that the mechanism of channel inactivation does not involve interaction of the channel with preformed filaments. Our data show that actin-capping protein can participate in the cytoskeleton-associated regulation of sodium transport in nonexcitable cells.




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