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Structure paper

TitleCryo-EM shows how dynactin recruits two dyneins for faster movement.
Journal, issue, pagesNature, Vol. 554, Issue 7691, Page 202-206, Year 2018
Publish dateFeb 7, 2018
AuthorsLinas Urnavicius / Clinton K Lau / Mohamed M Elshenawy / Edgar Morales-Rios / Carina Motz / Ahmet Yildiz / Andrew P Carter /
PubMed AbstractDynein and its cofactor dynactin form a highly processive microtubule motor in the presence of an activating adaptor, such as BICD2. Different adaptors link dynein and dynactin to distinct cargoes. ...Dynein and its cofactor dynactin form a highly processive microtubule motor in the presence of an activating adaptor, such as BICD2. Different adaptors link dynein and dynactin to distinct cargoes. Here we use electron microscopy and single-molecule studies to show that adaptors can recruit a second dynein to dynactin. Whereas BICD2 is biased towards recruiting a single dynein, the adaptors BICDR1 and HOOK3 predominantly recruit two dyneins. We find that the shift towards a double dynein complex increases both the force and speed of the microtubule motor. Our 3.5 Å resolution cryo-electron microscopy reconstruction of a dynein tail-dynactin-BICDR1 complex reveals how dynactin can act as a scaffold to coordinate two dyneins side-by-side. Our work provides a structural basis for understanding how diverse adaptors recruit different numbers of dyneins and regulate the motile properties of the dynein-dynactin transport machine.
External linksNature / PubMed:29420470 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.79 - 8.2 Å
Structure data

4168

6f1t

EMDB-4168, PDB-6f1t:
Cryo-EM structure of two dynein tail domains bound to dynactin and BICDR1
Method: EM (single particle) / Resolution: 3.5 Å

4169

6f1u

EMDB-4169, PDB-6f1u:
N terminal region of dynein tail domains in complex with dynactin filament and BICDR-1
Method: EM (single particle) / Resolution: 3.4 Å

4170

6f1v

EMDB-4170, PDB-6f1v:
C terminal region of the dynein heavy chains in the dynein tail/dynactin/BICDR1 complex
Method: EM (single particle) / Resolution: 3.4 Å

4171

6f1y

EMDB-4171, PDB-6f1y:
Dynein light intermediate chain region of the dynein tail/dynactin/BICDR1 complex
Method: EM (single particle) / Resolution: 3.4 Å

4172

6f1z

EMDB-4172, PDB-6f1z:
Roadblock-1 region of the dynein tail/dynactin/BICDR1 complex
Method: EM (single particle) / Resolution: 3.4 Å

4177

6f38

EMDB-4177, PDB-6f38:
Cryo-EM structure of two dynein tail domains bound to dynactin and HOOK3
Method: EM (single particle) / Resolution: 6.7 Å

PDB-5owo:
Human cytoplasmic Dynein N-Terminus dimerization domain at 1.8 Angstrom resolution
Method: X-RAY DIFFRACTION / Resolution: 1.79 Å

PDB-6f3a:
Cryo-EM structure of a single dynein tail domain bound to dynactin and BICD2N
Method: ELECTRON MICROSCOPY / Resolution: 8.2 Å

Chemicals

ChemComp-GOL:
GLYCEROL / Glycerol

ChemComp-MG:
Unknown entry

ChemComp-CA:
Unknown entry

ChemComp-NA:
Unknown entry

ChemComp-K:
Unknown entry

ChemComp-HOH:
WATER / Water

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM / Adenosine triphosphate

Source
  • mus musculus (house mouse)
  • homo sapiens (human)
  • sus scrofa (pig)
  • Pig (pig)
KeywordsMOTOR PROTEIN / Dynein / Heavy chain / Dimerization domain / Cryo-EM / Complex / dynein/dynactin/BICDR / TDR / Cargo adaptor / TDH / DDH / dynein/dynactin/HOOK3 / TDB / dynein/dynactin/BICD2

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