Abstract:
:Phalloidin and fluorescently labeled phalloidin analogs are established reagents to stabilize and mark actin filaments for the investigation of acto-myosin interactions. In the present study, we employed transient and steady-state kinetic measurements as well as in vitro motility assays to show that phalloidin perturbs the productive interaction of human non-muscle myosin-2A and -2C1 with filamentous actin. Phalloidin binding to F-actin results in faster dissociation of the complex formed with non-muscle myosin-2A and -2C1, reduced actin-activated ATP turnover, and slower velocity of actin filaments in the in vitro motility assay. In contrast, phalloidin binding to F-actin does not affect the interaction with human non-muscle myosin isoform 2B and Dictyostelium myosin-2 and myosin-5b.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Diensthuber RP,Müller M,Heissler SM,Taft MH,Chizhov I,Manstein DJdoi
10.1016/j.febslet.2011.01.042subject
Has Abstractpub_date
2011-03-09 00:00:00pages
767-71issue
5eissn
0014-5793issn
1873-3468pii
S0014-5793(11)00079-2journal_volume
585pub_type
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