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Structure paper

TitleStructural basis for tunable control of actin dynamics by myosin-15 in mechanosensory stereocilia.
Journal, issue, pagesSci Adv, Vol. 8, Issue 29, Page eabl4733, Year 2022
Publish dateJul 22, 2022
AuthorsRui Gong / Fangfang Jiang / Zane G Moreland / Matthew J Reynolds / Santiago Espinosa de Los Reyes / Pinar Gurel / Arik Shams / James B Heidings / Michael R Bowl / Jonathan E Bird / Gregory M Alushin /
PubMed AbstractThe motor protein myosin-15 is necessary for the development and maintenance of mechanosensory stereocilia, and mutations in myosin-15 cause hereditary deafness. In addition to transporting actin ...The motor protein myosin-15 is necessary for the development and maintenance of mechanosensory stereocilia, and mutations in myosin-15 cause hereditary deafness. In addition to transporting actin regulatory machinery to stereocilia tips, myosin-15 directly nucleates actin filament ("F-actin") assembly, which is disrupted by a progressive hearing loss mutation (p.D1647G, ""). Here, we present cryo-electron microscopy structures of myosin-15 bound to F-actin, providing a framework for interpreting the impacts of deafness mutations on motor activity and actin nucleation. Rigor myosin-15 evokes conformational changes in F-actin yet maintains flexibility in actin's D-loop, which mediates inter-subunit contacts, while the mutant locks the D-loop in a single conformation. Adenosine diphosphate-bound myosin-15 also locks the D-loop, which correspondingly blunts actin-polymerization stimulation. We propose myosin-15 enhances polymerization by bridging actin protomers, regulating nucleation efficiency by modulating actin's structural plasticity in a myosin nucleotide state-dependent manner. This tunable regulation of actin polymerization could be harnessed to precisely control stereocilium height.
External linksSci Adv / PubMed:35857845 / PubMed Central
MethodsEM (helical sym.) / EM (single particle)
Resolution2.62 - 4.18 Å
Structure data

24321

7r8v

EMDB-24321, PDB-7r8v:
Cryo-EM structure of the ADP state actin filament
Method: EM (helical sym.) / Resolution: 2.82 Å

24322

7r91

EMDB-24322, PDB-7r91:
cryo-EM structure of the rigor state wild type myosin-15-F-actin complex
Method: EM (helical sym.) / Resolution: 2.83 Å

24399

7rb8

EMDB-24399, PDB-7rb8:
cryo-EM structure of the ADP state wild type myosin-15-F-actin complex
Method: EM (helical sym.) / Resolution: 3.63 Å

24400

7rb9

EMDB-24400, PDB-7rb9:
Cryo-EM structure of the rigor state Jordan myosin-15-F-actin complex
Method: EM (helical sym.) / Resolution: 3.76 Å

26459

7udt

EMDB-26459, PDB-7udt:
cryo-EM structure of the rigor state wild type myosin-15-F-actin complex (symmetry expansion and re-centering)
Method: EM (single particle) / Resolution: 3.17 Å

26460

7udu

EMDB-26460, PDB-7udu:
cryo-EM structure of the ADP state wild type myosin-15-F-actin complex (symmetry expansion and re-centering)
Method: EM (single particle) / Resolution: 4.15 Å

EMDB-26461: cryo-EM structure of the ADP state wild type myosin-15-F-actin complex (symmetry expansion)
Method: EM (single particle) / Resolution: 3.9 Å

EMDB-26462: cryo-EM structure of the rigor state wild type myosin-15-F-actin complex (symmetry expansion)
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-26463: cryo-EM structure of the ADP state actin filament (symmetry expansion)
Method: EM (single particle) / Resolution: 2.62 Å

EMDB-26464: Cryo-EM structure of the rigor state Jordan myosin-15-F-actin complex (symmetry expansion)
Method: EM (single particle) / Resolution: 4.18 Å

Chemicals

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

ChemComp-MG:
Unknown entry

Source
  • gallus gallus (chicken)
  • chicken (chicken)
  • mus musculus (house mouse)
KeywordsCELL ADHESION / filamentous actin / cytoskeleton / adhesion / contractility / MOTOR PROTEIN / myosin motor proteins / actin cytoskeleton / stereocilia / deafness / MOTOR PROTEIN/ATP Binding Protein / MOTOR PROTEIN-ATP Binding Protein complex

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