Rapid de-localization of actin leading edge components with BDM treatment
<p>Abstract</p> <p>Background</p> <p>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 t...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
| Published: |
BMC
2003-06-01
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| Series: | BMC Cell Biology |
| Online Access: | http://www.biomedcentral.com/1471-2121/4/5 |
| _version_ | 1818234515288489984 |
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| author | Lechler Terry Yarrow Justin C Li Rong Mitchison Timothy J |
| author_facet | Lechler Terry Yarrow Justin C Li Rong Mitchison Timothy J |
| author_sort | Lechler Terry |
| collection | DOAJ |
| description | <p>Abstract</p> <p>Background</p> <p>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?</p> <p>Results</p> <p>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.</p> <p>Conclusion</p> <p>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.</p> |
| first_indexed | 2024-12-12T11:39:18Z |
| format | Article |
| id | doaj.art-9498b901074b44ee8845e23d66cab86e |
| institution | Directory Open Access Journal |
| issn | 1471-2121 |
| language | English |
| last_indexed | 2024-12-12T11:39:18Z |
| publishDate | 2003-06-01 |
| publisher | BMC |
| record_format | Article |
| series | BMC Cell Biology |
| spelling | doaj.art-9498b901074b44ee8845e23d66cab86e2022-12-22T00:25:35ZengBMCBMC Cell Biology1471-21212003-06-0141510.1186/1471-2121-4-5Rapid de-localization of actin leading edge components with BDM treatmentLechler TerryYarrow Justin CLi RongMitchison Timothy J<p>Abstract</p> <p>Background</p> <p>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?</p> <p>Results</p> <p>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.</p> <p>Conclusion</p> <p>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.</p>http://www.biomedcentral.com/1471-2121/4/5 |
| spellingShingle | Lechler Terry Yarrow Justin C Li Rong Mitchison Timothy J Rapid de-localization of actin leading edge components with BDM treatment BMC Cell Biology |
| title | Rapid de-localization of actin leading edge components with BDM treatment |
| title_full | Rapid de-localization of actin leading edge components with BDM treatment |
| title_fullStr | Rapid de-localization of actin leading edge components with BDM treatment |
| title_full_unstemmed | Rapid de-localization of actin leading edge components with BDM treatment |
| title_short | Rapid de-localization of actin leading edge components with BDM treatment |
| title_sort | rapid de localization of actin leading edge components with bdm treatment |
| url | http://www.biomedcentral.com/1471-2121/4/5 |
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