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Structure paper

TitleCryo-EM captures early intermediate steps in dynein activation by LIS1.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 7054, Year 2025
Publish dateAug 1, 2025
AuthorsKendrick H V Nguyen / Eva P Karasmanis / Agnieszka A Kendrick / Samara L Reck-Peterson / Andres E Leschziner /
PubMed AbstractCytoplasmic dynein-1 (dynein) is an essential molecular motor in eukaryotic cells. Dynein primarily exists in an autoinhibited Phi state and requires conformational changes to assemble with its ...Cytoplasmic dynein-1 (dynein) is an essential molecular motor in eukaryotic cells. Dynein primarily exists in an autoinhibited Phi state and requires conformational changes to assemble with its cofactors and form active transport complexes. LIS1, a key dynein regulator, enhances dynein activation and assembly. Using cryo-EM and a human dynein-LIS1 sample incubated with ATP, we map the conformational landscape of dynein activation by LIS1 and identify an early intermediate state that we propose precedes the previously identified dynein-LIS1 Chi state. Mutations that disrupt this species, which we termed "Pre-Chi", lead to motility defects in vitro, emphasizing its functional importance. Together, our findings provide insights into how LIS1 relieves dynein autoinhibition during the activation pathway.
External linksNat Commun / PubMed:40750582 / PubMed Central
MethodsEM (single particle)
Resolution2.7 - 6.2 Å
Structure data

47342

9dzy

EMDB-47342, PDB-9dzy:
Cryo-EM structure of Pre-Chi dynein bound to Lis1
Method: EM (single particle) / Resolution: 3.1 Å

47360

9e0k

EMDB-47360, PDB-9e0k:
Cryo-EM structure of human cytoplasmic dynein-1 in the presence of ATP
Method: EM (single particle) / Resolution: 3.2 Å

47370

9e0t

EMDB-47370, PDB-9e0t:
Cryo-EM structure of human cytoplasmic dynein-1 bound to LIS1 in the presence of ATP
Method: EM (single particle) / Resolution: 3.1 Å

47371

9e0u

EMDB-47371, PDB-9e0u:
Cryo-EM structure of human cytoplasmic dynein-1 in the presence of ATP
Method: EM (single particle) / Resolution: 3.4 Å

47372

9e0w

EMDB-47372, PDB-9e0w:
Cryo-EM structure of human cytoplasmic dynein-1 bound to LIS1 in the presence of ATP
Method: EM (single particle) / Resolution: 3.2 Å

47373

9e0x

EMDB-47373, PDB-9e0x:
Cryo-EM structure of Phi dynein
Method: EM (single particle) / Resolution: 2.7 Å

47377

9e0y

EMDB-47377, PDB-9e0y:
Cryo-EM structure of human cytoplasmic dynein-1 in the presence of ATP
Method: EM (single particle) / Resolution: 3.4 Å

47429

9e22

EMDB-47429, PDB-9e22:
Cryo-EM structure of human cytoplasmic dynein-1 bound to LIS1 in the presence of ATP
Method: EM (single particle) / Resolution: 3.3 Å

47430

9e23

EMDB-47430, PDB-9e23:
Cryo-EM structure of Pre-Chi dynein tail
Method: EM (single particle) / Resolution: 6.2 Å

47443

9e28

EMDB-47443, PDB-9e28:
Cryo-EM structure of Phi dynein tail
Method: EM (single particle) / Resolution: 4.4 Å

Chemicals

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

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

ChemComp-MG:
Unknown entry

Source
  • homo sapiens (human)
KeywordsMOTOR PROTEIN / Complex / Human

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