Rapid de-localization of actin leading edge components with BDM treatment
1 Dept of Cell Biology, Harvard Medical School, 240 Longwood Ave, Boston MA. 02115, USA
2 Institute of Chemistry and Cell Biology Harvard Medical School, 250 Longwood Ave, SGM 604, Boston MA. 02115, USA
3 Current Address: Rockefeller University and Howard Hughes Medical Institute Laboratory of Mammalian Cell Biology and Development, 1230 York Avenue, Box 300, New York, NY. 10021-6399, USA
BMC Cell Biology 2003, 4:5 doi:10.1186/1471-2121-4-5Published: 3 June 2003
2,3-Butanedione monoxime (BDM) has been widely used as a non-muscle myosin inhibitor to investigate the role of non-muscle myosinII in the process of actin retrograde flow and other actin cytoskeletal processes. Recent reports show that BDM does not inhibit any non-muscle myosins so far tested, including nm-myosinII, prompting the question, how were these process affected in BDM studies?
We have found that treatment of mammalian cells with BDM for only 1 min blocks actin incorporation at the leading edge in a permeabilized cell system. We show that inhibition of actin incorporation occurs through de-localization of leading edge proteins involved in actin polymerization – the Arp2/3 complex, WAVE, and VASP – that de-localize concomitantly with the leading edge actin network.
De-localization of actin leading edge components by BDM treatment is a newly described effect of this compound. It may explain many of the results previously ascribed to inhibition of non-muscle myosinII by BDM, particularly in studies of leading edge dynamics. Though this effect of BDM is intriguing, future studies probing actin dynamics at the leading edge should use more potent and specific inhibitors.