Molecular mechanism of dynein-dynactin complex assembly by LIS1

K Singh, CK Lau, G Manigrasso, JB Gama… - Science, 2024 - science.org
Cytoplasmic dynein is a microtubule motor vital for cellular organization and division. It
functions as a~ 4-megadalton complex containing its cofactor dynactin and a cargo-specific …

[HTML][HTML] Nde1 promotes Lis1-mediated activation of dynein

Y Zhao, S Oten, A Yildiz - Nature Communications, 2023 - nature.com
Cytoplasmic dynein drives the motility and force generation functions towards the
microtubule minus end. The assembly of dynein with dynactin and a cargo adaptor in an …

Microtubule-binding-induced allostery triggers LIS1 dissociation from dynein prior to cargo transport

WD Ton, Y Wang, P Chai… - Nature structural & …, 2023 - nature.com
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) …

[HTML][HTML] Lis1 relieves cytoplasmic dynein-1 autoinhibition by acting as a molecular wedge

EP Karasmanis, JM Reimer, AA Kendrick… - Nature Structural & …, 2023 - nature.com
Cytoplasmic dynein-1 transports intracellular cargo towards microtubule minus ends. Dynein
is autoinhibited and undergoes conformational changes to form an active complex that …

[HTML][HTML] Ndel1 disfavors dynein–dynactin–adaptor complex formation in two distinct ways

SR Garrott, JP Gillies, A Siva, SR Little… - Journal of Biological …, 2023 - ASBMB
Dynein is the primary minus-end-directed microtubule motor protein. To achieve activation,
dynein binds to the dynactin complex and an adaptor to form the" activated dynein complex." …

Kinesin-1 autoinhibition facilitates the initiation of dynein cargo transport

R Qiu, J Zhang, X Xiang - Journal of Cell Biology, 2022 - rupress.org
The functional significance of Kinesin-1 autoinhibition has been unclear. Kinesin-1
transports multiple cargoes including cytoplasmic dynein to microtubule plus ends. From a …

Lis1 slows force-induced detachment of cytoplasmic dynein from microtubules

E Kusakci, ZM Htet, Y Zhao, JP Gillies… - Nature Chemical …, 2024 - nature.com
Lis1 is a key cofactor for the assembly of active cytoplasmic dynein complexes that transport
cargo along microtubules. Lis1 binds to the AAA+ ring and stalk of dynein and slows dynein …

Molecular mechanism of dynein-dynactin activation by JIP3 and LIS1

K Singh, C Lau, G Manigrasso, JB Gama, R Gassmann… - bioRxiv, 2022 - biorxiv.org
Microtubule motors, like cytoplasmic dynein-1, are tightly regulated to prevent inappropriate
activity in cells. Dynein functions as a~ 4 MDa complex containing its cofactor dynactin and a …

New pieces for the Lis1–dynein puzzle

CK Lau - nature structural & molecular biology, 2023 - nature.com
The microtubule motor dynein is regulated by lissencephaly-1 (Lis1) at several points during
its complex activation process. Two papers reveal the molecular mechanism for two steps …

[HTML][HTML] Patient-specific mutation of Dync1h1 in mice causes brain and behavioral deficits

RL Ramos, MMB De Heredia, Y Zhang, RF Stout… - Neurobiology of …, 2024 - Elsevier
Aims Cytoplasmic dynein heavy chain (DYNC1H1) is a multi-subunit protein complex that
provides motor force for movement of cargo on microtubules and traffics them back to the …