Abstract:
:Cytoplasmic dynein, a microtubule-based motor protein, is responsible for many cellular functions ranging from cargo transport to cell division. The various functions are carried out by a single isoform of cytoplasmic dynein, thus requiring different forms of motor regulation. A possible pathway to regulate motor function was revealed in optical trap experiments. Switching motor function from single steps to processive runs could be achieved by changing Mg2+ and ATP concentrations. Here, we confirm by single molecule total internal reflection fluorescence microscopy that a native cytoplasmic dynein dimer is able to switch to processive runs of more than 680 consecutive steps or 5.5 μm. We also identified the ratio of Mg2+ -free ATP to Mg.ATP as the regulating factor and propose a model for dynein processive stepping.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Behrens VA,Walter WJ,Peters C,Wang T,Brenner B,Geeves MA,Scholz T,Steffen Wdoi
10.1002/1873-3468.13319subject
Has Abstractpub_date
2019-02-01 00:00:00pages
296-307issue
3eissn
0014-5793issn
1873-3468journal_volume
593pub_type
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