The structure of the dynactin complex and its interaction with dynein | Zendy

L. Urnavicius | Zendy; Kai Zhang | Zendy; Aristides G. Diamant | Zendy; C. Motz | Zendy; Max A. Schlager | Zendy; Minmin Yu | Zendy; Nisha Patel | Zendy; Carol V. Robinson | Zendy; Andrew P. Carter | Zendy

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The structure of the dynactin complex and its interaction with dynein

Author(s) -

L. Urnavicius,

Kai Zhang,

Aristides G. Diamant,

C. Motz,

Max A. Schlager,

Minmin Yu,

Nisha Patel,

Carol V. Robinson,

Andrew P. Carter

Publication year - 2015

Publication title -

science

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 12.556

H-Index - 1186

eISSN - 1095-9203

pISSN - 0036-8075

DOI - 10.1126/science.aaa4080

Subject(s) - dynactin , dynein , microtubule , protein filament , protein subunit , biophysics , microbiology and biotechnology , chemistry , actin , biology , biochemistry , gene

Making a molecular motor fit for purpose Dynactin is an essential cofactor of the microtubule motor, cytoplasmic dynein. Dynactin contains 23 subunits built around a short filament of an actin-related protein (Arp1). How dynactin is assembled, how it functions with dynein, and why it is built around an actin-like filament is unclear. Urnaviciuset al. combined cryo–electron microscopy structural studies and a crystal structure to determine the three-dimensional architecture of dynactin and how it interacts with dynein.Science , this issue p.1441

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