Premium
Mg 2+ ‐free ATP regulates the processivity of native cytoplasmic dynein
Author(s) -
Behrens Vincent A.,
Walter Wilhelm J.,
Peters Carsten,
Wang Tianbang,
Brenner Bernhard,
Geeves Michael A.,
Scholz Tim,
Steffen Walter
Publication year - 2019
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13319
Subject(s) - dynein , processivity , dynactin , microtubule , motor protein , cytoplasm , microbiology and biotechnology , molecular motor , chemistry , function (biology) , biophysics , biology , biochemistry , gene , dna replication
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 Mg 2+ 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 Mg 2+ ‐free ATP to Mg. ATP as the regulating factor and propose a model for dynein processive stepping.