Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Roles of microtubules and LIS1 in dynein transport machinery assembly.
Journal, issue, pages	Nature, Year 2026
Publish date	Feb 18, 2026
Authors	Qinhui Rao / Jun Yang / Pengxin Chai / Steven Markus / Kai Zhang /
PubMed Abstract	Cytoplasmic dynein-1, a microtubule (MT)-based motor protein, requires dynactin and a coiled-coil adaptor to form the processive dynein-dynactin-adaptor (DDA) complex. The roles of MTs and dynein ...Cytoplasmic dynein-1, a microtubule (MT)-based motor protein, requires dynactin and a coiled-coil adaptor to form the processive dynein-dynactin-adaptor (DDA) complex. The roles of MTs and dynein regulator lissencephaly-1 (LIS1) in DDA assembly have remained elusive. Here we use cryo-electron microscopy to determine the structural basis of MT- and LIS1-mediated DDA assembly. We show that an adaptor-independent dynein-dynactin complex spontaneously forms on MTs with an intrinsic 2:1 stoichiometry in a highly efficient manner, driven by parallel alignment of dynein tails upon MT binding. Adaptors can wedge into and exchange within the assembled MT-bound dynein-dynactin complex; these processes are enabled by relative rotations between dynein and dynactin and facilitated by the dynein light-intermediate chains that assist the adaptor 'search' mechanism. Although LIS1 is dispensable for efficient DD(A)-MT assembly, its presence expands the conformational landscape of DD(A) assemblies on MTs. Cryo-electron microscopy reveals that LIS1 bridges dynactin p150 and dynein in both the closed Phi-like and open prepowerstroke states, stabilizing low-MT-affinity intermediates that tether dynein molecules in proximity to MTs and prime them for subsequent DD(A) assembly through alternative pathways. These findings demonstrate the dynamic adaptability of the dynein transport machinery and the coordinated roles of MTs and LIS1 in DDA assembly.
External links	Nature / PubMed:41708859
Methods	EM (single particle)
Resolution	3.5 - 15.0 Å
Structure data	46843 9dgp EMDB-46843, PDB-9dgp: Motor domain of dynein-1 complex on microtubules Method: EM (single particle) / Resolution: 3.5 Å 46844 9dgq EMDB-46844, PDB-9dgq: Structure of dynein-1 on microtubules Method: EM (single particle) / Resolution: 11.0 Å 46845 9dgr EMDB-46845, PDB-9dgr: Composite structure of dynein-dynactin on microtubules Method: EM (single particle) / Resolution: 15.0 Å 46846 9dgs EMDB-46846, PDB-9dgs: Dynactin and dynein tail region of dynein-dynactin complex on microtubules Method: EM (single particle) / Resolution: 3.9 Å 46847 9dgt EMDB-46847, PDB-9dgt: structure of dynactin, dynein tail with one BICDR from dynein-dynactin-BICDR on microtubules Method: EM (single particle) / Resolution: 7.2 Å 46848 9dgu EMDB-46848, PDB-9dgu: structure of dynactin, dynein tail with two BICDR from dynein-dynactin-BICDR on microtubules Method: EM (single particle) / Resolution: 7.1 Å 46849 9dgv EMDB-46849, PDB-9dgv: structure of dynactin, dynein tail with TRAK2 from dynein-dynactin-TRAK2 on microtubules Method: EM (single particle) / Resolution: 8.8 Å EMDB-47061: Consensus map of dynein-dynactin on microtubules Method: EM (single particle) / Resolution: 12.0 Å 73173 9ync EMDB-73173, PDB-9ync: Motor domains of phi-like human dynein-1 bound to dynactin-p150glued and LIS1 Method: EM (single particle) / Resolution: 3.93 Å 73174 9ynd EMDB-73174, PDB-9ynd: Motor domain of human dynein-1 in pre-power stroke bound to dynactin-p150glued-CC1B and LIS1 Method: EM (single particle) / Resolution: 4.26 Å 73175 9yne EMDB-73175, PDB-9yne: Motor domain of human dynein-1 in pre-power stroke bound to dynactin-p150glued-CC1B-ICD and LIS1 Method: EM (single particle) / Resolution: 8.46 Å 73176 9ynf EMDB-73176, PDB-9ynf: Motor domain of human dynein-1 in post1 state Method: EM (single particle) / Resolution: 3.92 Å 73178 9yng EMDB-73178, PDB-9yng: Dynactin and dynein-1 tail region of dynein-dynactin complex on microtubule in the presence of LIS1 Method: EM (single particle) / Resolution: 4.07 Å 73179 9ynh EMDB-73179, PDB-9ynh: Full-length human cytoplasmic dynein-1 in phi-like state bound to dynactin-p150glued and LIS1 Method: EM (single particle) / Resolution: 5.5 Å
Chemicals	ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM ChemComp-ANP: PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogueYM ChemComp-MG: Unknown entry ChemComp-ZN*: Unknown entry
Source	sus scrofa (pig) mus musculus (house mouse) homo sapiens (human)
Keywords	MOTOR PROTEIN / dynein / microtubule / dynactin / BICDR / TRAK2 / Dynein-1 / phi-like conformation / Lis1 / p150glued / p150