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Structure paper

TitleA nucleotide code governs Lis1's ability to relieve dynein autoinhibition.
Journal, issue, pagesbioRxiv, Year 2025
Publish dateJan 2, 2025
AuthorsIndigo C Geohring / Pengxin Chai / Bharat R Iyer / William D Ton / Jun Yang / Amy H Ide / Sydney C George / Jaiveer S Bagri / Samuel V Baird / Kai Zhang / Steven M Markus
PubMed AbstractDynein-1 is a microtubule motor responsible for the transport of cytoplasmic cargoes. Activation of motility requires it first overcome an autoinhibited state prior to its assembly with dynactin and ...Dynein-1 is a microtubule motor responsible for the transport of cytoplasmic cargoes. Activation of motility requires it first overcome an autoinhibited state prior to its assembly with dynactin and a cargo adaptor. Studies suggest that Lis1 may relieve dynein's autoinhibited state. However, evidence for this mechanism is lacking. We first set out to determine the rules governing dynein-Lis1 binding, which reveals that their binding affinity is regulated by the nucleotide-bound states of each of three nucleotide-binding pockets within the dynein motor domain. We also find that distinct nucleotide 'codes' coordinate dynein-Lis1 binding stoichiometry by impacting binding affinity at two different sites within the dynein motor domain. Electron microscopy reveals that a 1 Lis1:1 dynein complex directly promotes an open, uninhibited conformational state of dynein, whereas a 2:1 complex resembles the autoinhibited state. Cryo-EM analysis reveals the structural basis for Lis1 opening dynein relies on interactions with the linker domain.
External linksbioRxiv / PubMed:39803478 / PubMed Central
MethodsEM (single particle)
Resolution3.2 - 4.1 Å
Structure data

48239

9mfv

EMDB-48239, PDB-9mfv:
Motor domain with Apo AAA1 and ADP AAA3 from yeast full-length dynein-1 in 0.1 mM ATP condition
Method: EM (single particle) / Resolution: 3.3 Å

48240

9mfw

EMDB-48240, PDB-9mfw:
Motor domain with ADP AAA1 and ADP AAA3 from yeast full-length dynein-1 in 0.1 mM ATP condition
Method: EM (single particle) / Resolution: 4.1 Å

48241

9mfx

EMDB-48241, PDB-9mfx:
Motor domain alone with Apo AAA1 and ADP AAA3 from yeast full-length dynein-1 and Pac1 in 0.1 mM ATP condition
Method: EM (single particle) / Resolution: 3.2 Å

48242

9mfy

EMDB-48242, PDB-9mfy:
Motor domain-Pac1 complex with ADP AAA1 and Apo AAA3 from yeast full-length dynein-1 and Pac1 in 0.1 mM ATP condition
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

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

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

ChemComp-MG:
Unknown entry

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsMOTOR PROTEIN / dynein

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