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TitleMicrotubule-binding-induced allostery triggers LIS1 dissociation from dynein prior to cargo transport.
Journal, issue, pagesNat Struct Mol Biol, Vol. 30, Issue 9, Page 1365-1379, Year 2023
Publish dateJun 15, 2023
AuthorsWilliam D Ton / Yue Wang / Pengxin Chai / Cisloynny Beauchamp-Perez / Nicholas T Flint / Lindsay G Lammers / Hao Xiong / Kai Zhang / Steven M Markus /
PubMed AbstractThe lissencephaly-related protein LIS1 is a critical regulator of cytoplasmic dynein that governs motor function and intracellular localization (for example, to microtubule plus-ends). Although LIS1 ...The lissencephaly-related protein LIS1 is a critical regulator of cytoplasmic dynein that governs motor function and intracellular localization (for example, to microtubule plus-ends). Although LIS1 binding is required for dynein activity, its unbinding prior to initiation of cargo transport is equally important, since preventing dissociation leads to dynein dysfunction. To understand whether and how dynein-LIS1 binding is modulated, we engineered dynein mutants locked in a microtubule-bound (MT-B) or microtubule-unbound (MT-U) state. Whereas the MT-B mutant exhibits low LIS1 affinity, the MT-U mutant binds LIS1 with high affinity, and as a consequence remains almost irreversibly associated with microtubule plus-ends. We find that a monomeric motor domain is sufficient to exhibit these opposing LIS1 affinities, and that this is evolutionarily conserved between yeast and humans. Three cryo-EM structures of human dynein with and without LIS1 reveal microtubule-binding induced conformational changes responsible for this regulation. Our work reveals key biochemical and structural insight into LIS1-mediated dynein activation.
External linksNat Struct Mol Biol / PubMed:37322240 / PubMed Central
MethodsEM (single particle)
Resolution2.9 - 3.4 Å
Structure data

28999

8fcy

EMDB-28999, PDB-8fcy:
Engineered human dynein motor domain in microtubule-bound state
Method: EM (single particle) / Resolution: 3.4 Å

29003

8fd6

EMDB-29003, PDB-8fd6:
Engineered human dynein motor domain in the microtubule-unbound state in the buffer containing ATP-Vi
Method: EM (single particle) / Resolution: 2.9 Å

29012

8fdt

EMDB-29012, PDB-8fdt:
Engineered human dynein motor domain in the microtubule-unbound state with LIS1 complex in the buffer containing ATP-Vi
Method: EM (single particle) / Resolution: 3.2 Å

29014

8fdu

EMDB-29014, PDB-8fdu:
Engineered human dynein motor domain in the microtubule-unbound state with LIS1 complex in the buffer containing ATP-Vi (local refined on AAA3-AAA5 and LIS1)
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

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

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

ChemComp-VO4:
VANADATE ION / Vanadate

ChemComp-MG:
Unknown entry

Source
  • homo sapiens (human)
  • thermus thermophilus (bacteria)
KeywordsMOTOR PROTEIN / Dynein / motor domain / microtubule-bound / microtubule-unbound / LIS1

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