Abstract
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 motility, but the underlying mechanism has remained unclear. Using single-molecule imaging and optical trapping assays, we investigated how Lis1 binding affects the motility and force generation of yeast dynein in vitro. We showed that Lis1 slows motility by binding to the AAA+ ring of dynein, not by serving as a roadblock or tethering dynein to microtubules. Lis1 binding also does not affect force generation, but it induces prolonged stalls and reduces the asymmetry in the force-induced detachment of dynein from microtubules. The mutagenesis of the Lis1-binding sites on the dynein stalk partially recovers this asymmetry but does not restore dynein velocity. These results suggest that Lis1–stalk interaction slows the detachment of dynein from microtubules by interfering with the stalk sliding mechanism.
Similar content being viewed by others
Data availability
A reporting summary for this article is available as a Supplementary Information file. The main data supporting the findings of this study are available within the article and its Extended Data figures. Protocols that support the findings of this study can be found in Methods. Yeast strains and raw data will be made available by the corresponding authors upon request. Source data are provided with this paper.
Code availability
The custom code used to analyze experimental data is uploaded to the Yildiz Lab code repository (www.yildizlab.org/code_repository) and GitHub (https://github.com/Yildiz-Lab/YFIESTA).
References
Canty, J. T., Tan, R., Kusakci, E., Fernandes, J. & Yildiz, A. Structure and mechanics of dynein motors. Annu. Rev. Biophys. 50, 549–574 (2021).
Reck-Peterson, S. L., Redwine, W. B., Vale, R. D. & Carter, A. P. The cytoplasmic dynein transport machinery and its many cargoes. Nat. Rev. Mol. Cell Biol. 19, 382–398 (2018).
Guedes-Dias, P. & Holzbaur, E. L. F. Axonal transport: driving synaptic function. Science 366, eaaw9997 (2019).
Carter, A. P., Cho, C., Jin, L. & Vale, R. D. Crystal structure of the dynein motor domain. Science 331, 1159–1165 (2011).
Kon, T. et al. The 2.8 Å crystal structure of the dynein motor domain. Nature 484, 345–350 (2012).
Can, S., Lacey, S., Gur, M., Carter, A. P. & Yildiz, A. Directionality of dynein is controlled by the angle and length of its stalk. Nature 566, 407–410 (2019).
Kon, T. et al. Helix sliding in the stalk coiled coil of dynein couples ATPase and microtubule binding. Nat. Struct. Mol. Biol. 16, 325–333 (2009).
Torisawa, T. et al. Autoinhibition and cooperative activation mechanisms of cytoplasmic dynein. Nat. Cell Biol. 16, 1118–1124 (2014).
Trokter, M., Mucke, N. & Surrey, T. Reconstitution of the human cytoplasmic dynein complex. Proc. Natl Acad. Sci. USA 109, 20895–20900 (2012).
Zhang, K. et al. Cryo-EM reveals how human cytoplasmic dynein is auto-inhibited and activated. Cell 169, 1303–1314.e18 (2017).
McKenney, R. J., Huynh, W., Tanenbaum, M. E., Bhabha, G. & Vale, R. D. Activation of cytoplasmic dynein motility by dynactin-cargo adapter complexes. Science 345, 337–341 (2014).
Schlager, M. A., Hoang, H. T., Urnavicius, L., Bullock, S. L. & Carter, A. P. In vitro reconstitution of a highly processive recombinant human dynein complex. EMBO J. 33, 1855–1868 (2014).
Markus, S. M., Marzo, M. G. & McKenney, R. J. New insights into the mechanism of dynein motor regulation by lissencephaly-1. eLife 9, 59737 (2020).
Reiner, O. et al. Isolation of a Miller–Dieker lissencephaly gene containing G protein β-subunit-like repeats. Nature 364, 717–721 (1993).
Gillies, J. P. et al. Structural basis for cytoplasmic dynein-1 regulation by Lis1. eLife 11, 71229 (2022).
DeSantis, M. E. et al. Lis1 has two opposing modes of regulating cytoplasmic dynein. Cell 170, 1197–1208.e12 (2017).
Huang, J., Roberts, A. J., Leschziner, A. E. & Reck-Peterson, S. L. Lis1 acts as a ‘clutch’ between the ATPase and microtubule-binding domains of the dynein motor. Cell 150, 975–986 (2012).
Elshenawy, M. M. et al. Lis1 activates dynein motility by modulating its pairing with dynactin. Nat. Cell Biol. 22, 570–578 (2020).
Htet, Z. M. et al. LIS1 promotes the formation of activated cytoplasmic dynein-1 complexes. Nat. Cell Biol. 22, 518–525 (2020).
Marzo, M. G., Griswold, J. M. & Markus, S. M. Pac1/LIS1 stabilizes an uninhibited conformation of dynein to coordinate its localization and activity. Nat. Cell Biol. 22, 559–569 (2020).
Qiu, R., Zhang, J. & Xiang, X. LIS1 regulates cargo-adapter-mediated activation of dynein by overcoming its autoinhibition in vivo. J. Cell Biol. 218, 3630–3646 (2019).
Yamada, M. et al. LIS1 and NDEL1 coordinate the plus-end-directed transport of cytoplasmic dynein. EMBO J. 27, 2471–2483 (2008).
Torisawa, T. et al. Functional dissection of LIS1 and NDEL1 towards understanding the molecular mechanisms of cytoplasmic dynein regulation. J. Biol. Chem. 286, 1959–1965 (2011).
Wang, S. et al. Nudel/NudE and Lis1 promote dynein and dynactin interaction in the context of spindle morphogenesis. Mol. Biol. Cell 24, 3522–3533 (2013).
Toropova, K. et al. Lis1 regulates dynein by sterically blocking its mechanochemical cycle. eLife 3, 03372 (2014).
Baumbach, J. et al. Lissencephaly-1 is a context-dependent regulator of the human dynein complex. eLife 6, 21768 (2017).
Gutierrez, P. A., Ackermann, B. E., Vershinin, M. & McKenney, R. J. Differential effects of the dynein-regulatory factor Lissencephaly-1 on processive dynein-dynactin motility. J. Biol. Chem. 292, 12245–12255 (2017).
Muhua, L., Karpova, T. S. & Cooper, J. A. A yeast actin-related protein homologous to that in vertebrate dynactin complex is important for spindle orientation and nuclear migration. Cell 78, 669–679 (1994).
Heil-Chapdelaine, R. A., Oberle, J. R. & Cooper, J. A. The cortical protein Num1p is essential for dynein-dependent interactions of microtubules with the cortex. J. Cell Biol. 151, 1337–1344 (2000).
Reck-Peterson, S. L. et al. Single-molecule analysis of dynein processivity and stepping behavior. Cell 126, 335–348 (2006).
DeWitt, M. A., Chang, A. Y., Combs, P. A. & Yildiz, A. Cytoplasmic dynein moves through uncoordinated stepping of the AAA+ ring domains. Science 335, 221–225 (2012).
Qiu, W. et al. Dynein achieves processive motion using both stochastic and coordinated stepping. Nat. Struct. Mol. Biol. 19, 193–200 (2012).
Belyy, V. et al. The mammalian dynein-dynactin complex is a strong opponent to kinesin in a tug-of-war competition. Nat. Cell Biol. 18, 1018–1024 (2016).
Belyy, V., Hendel, N. L., Chien, A. & Yildiz, A. Cytoplasmic dynein transports cargos via load-sharing between the heads. Nat. Commun. 5, 5544 (2014).
Elshenawy, M. M. et al. Cargo adaptors regulate stepping and force generation of mammalian dynein-dynactin. Nat. Chem. Biol. 15, 1093–1101 (2019).
McKenney, R. J., Vershinin, M., Kunwar, A., Vallee, R. B. & Gross, S. P. LIS1 and NudE induce a persistent dynein force-producing state. Cell 141, 304–314 (2010).
Markus, S. M. & Lee, W. L. Regulated offloading of cytoplasmic dynein from microtubule plus ends to the cortex. Dev. Cell 20, 639–651 (2011).
Monroy, B. Y. et al. A combinatorial MAP code dictates polarized microtubule transport. Dev. Cell 53, 60–72.e4 (2020).
Ferro, L. S. et al. Structural and functional insight into regulation of kinesin-1 by microtubule-associated protein MAP7. Science 375, 326–331 (2022).
Gennerich, A., Carter, A. P., Reck-Peterson, S. L. & Vale, R. D. Force-induced bidirectional stepping of cytoplasmic dynein. Cell 131, 952–965 (2007).
Rao, L., Berger, F., Nicholas, M. P. & Gennerich, A. Molecular mechanism of cytoplasmic dynein tension sensing. Nat. Commun. 10, 3332 (2019).
Cleary, F. B. et al. Tension on the linker gates the ATP-dependent release of dynein from microtubules. Nat. Commun. 5, 4587 (2014).
Nicholas, M. P. et al. Cytoplasmic dynein regulates its attachment to microtubules via nucleotide state-switched mechanosensing at multiple AAA domains. Proc. Natl Acad. Sci. USA 112, 6371–6376 (2015).
Ezber, Y., Belyy, V., Can, S. & Yildiz, A. Dynein harnesses active fluctuations of microtubules for faster movement. Nat. Phys. 16, 312–316 (2020).
Carter, A. P. Crystal clear insights into how the dynein motor moves. J. Cell Sci. 126, 705–713 (2013).
Reimer, J. M., DeSantis, M. E., Reck-Peterson, S. L. & Leschziner, A. E. Structures of human dynein in complex with the lissencephaly 1 protein, LIS1. eLife 12, 84302 (2023).
Kon, T., Mogami, T., Ohkura, R., Nishiura, M. & Sutoh, K. ATP hydrolysis cycle-dependent tail motions in cytoplasmic dynein. Nat. Struct. Mol. Biol. 12, 513–519 (2005).
Lee, W. L., Oberle, J. R. & Cooper, J. A. The role of the lissencephaly protein Pac1 during nuclear migration in budding yeast. J. Cell Biol. 160, 355–364 (2003).
Lenz, J. H., Schuchardt, I., Straube, A. & Steinberg, G. A dynein loading zone for retrograde endosome motility at microtubule plus-ends. EMBO J. 25, 2275–2286 (2006).
Egan, M. J., Tan, K. & Reck-Peterson, S. L. Lis1 is an initiation factor for dynein-driven organelle transport. J. Cell Biol. 197, 971–982 (2012).
Jha, R., Roostalu, J., Cade, N. I., Trokter, M. & Surrey, T. Combinatorial regulation of the balance between dynein microtubule end accumulation and initiation of directed motility. EMBO J. 36, 3387–3404 (2017).
Lammers, L. G. & Markus, S. M. The dynein cortical anchor Num1 activates dynein motility by relieving Pac1/LIS1-mediated inhibition. J. Cell Biol. 211, 309–322 (2015).
Ton, W. D. et al. Microtubule-binding-induced allostery triggers LIS1 dissociation from dynein prior to cargo transport. Nat. Struct. Mol. Biol. 30, 1365–1379 (2023).
Pecreaux, J. et al. Spindle oscillations during asymmetric cell division require a threshold number of active cortical force generators. Curr. Biol. 16, 2111–2122 (2006).
Yang, G. et al. Architectural dynamics of the meiotic spindle revealed by single-fluorophore imaging. Nat. Cell Biol. 9, 1233–1242 (2007).
Acknowledgements
We thank S. Can, M. ElShenawy, L. S. Ferro, J. T. Canty and other members of the Yildiz and Reck-Peterson laboratories for helpful discussions, and S. M. Markus for sharing the yeast strain that expresses dyneinGal. This work was supported by grants from the National Institute of General Medical Sciences (GM094522, A.Y.), the National Science Foundation (MCB-1617028 and MCB-1055017, A.Y.) and the Fellowship of the Ministry of Education of the Turkish Republic (E.K.). S.L.R.-P. is a Howard Hughes Medical Institute Investigator and is also supported by the National Institutes of Health (1R35GM141825).
Author information
Authors and Affiliations
Contributions
E.K., S.L.R.-P. and A.Y. conceived the study and designed the experiments. Z.M.H. generated the yeast constructs for dynein and Lis1. E.K. purified the proteins. E.K. and Y.Z. performed single-molecule experiments and analyzed the data. J.P.G. performed experiments on monomeric Lis1. E.K., S.L.R.-P. and A.Y. wrote the manuscript. All authors read and revised the manuscript.
Corresponding author
Ethics declarations
Competing interests
The authors declare no competing interests.
Peer review
Peer review information
Nature Chemical Biology thanks Richard McKenney and the other, anonymous, reviewer(s) for their contribution to the peer review of this work.
Additional information
Publisher’s note Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.
Extended data
Extended Data Fig. 1 Single molecule motility of dynein in the presence of Lis1.
a) Representative kymographs of TMR-dynein with increasing concentrations of unlabeled Lis1. b) (Left) 1-CDF of run time under different Lis1 concentrations. Fitting to a double exponential decay (solid curves) reveals the weighted average of run time in each condition. (Right) The weighted average of run time under increasing Lis1 concentrations (± s.e.; N = 861, 534, and 312 from left to right). c) (Left) 1-CDF of run length under different Lis1 concentrations. Solid curves represent a fit to a double exponential decay. (Right) The weighted average of run length in each condition (bar graphs, ± s.e.; N = 861, 534, and 312 from left to right). d) An example kymograph shows that the transient binding of Lis1 slows whereas the subsequent release of Lis1 restores the velocity (arrowheads). In b and c, P values were calculated by the two-tailed Kolmogorov-Smirnov test.
Extended Data Fig. 2 Lis1 interacts with the microtubule lattice through its dynein binding site in vitro.
a) Microtubule co-pelleting assay with Lis1WT and Lis15A (mean ±s.e.m., three replicates per condition). The solid curve represents a fit to a binding isotherm to determine KD (±s.e.; N.D.: not determined). The statistical analysis was performed using an extra sum-of-squares F test (p = 10−4). b) The subtilisin treatment of microtubules reduces the molecular weight of tubulin in a denaturing gel (three independent experiments). c) The structure of Lis1 bound to the AAA ring with the five residues mutated in Lis15A are shown as spheres and all lysine and arginine residues are in blue (Protein Data Bank: 7MGM15). d) Representative kymographs of dynein in the presence and absence of Lis15A. Assays were performed in 50 mM KAc. e) The velocity, run time, and run length of dynein in the presence and absence of Lis15A (N = 326, 534, and 336 from left to right). The center line and whiskers represent the mean and s.d., respectively. P values were calculated by a two-tailed t-test with Welch correction for velocity and by the two-tailed Kolmogorov-Smirnov test for run time and run length. f) Surface-immobilized microtubules were decorated by 100 nM TMR-Lis1 before and after removing unbound Lis1 in the flow chamber. The assay was performed in the absence of added salt to maximize the Lis1-microtubule interaction. Washing the chamber with buffer and introducing dynein reduces 92% of the Lis1 signal on microtubules (three independent experiments).
Extended Data Fig. 3 Motility of dyneinGal in the presence of unlabeled Lis1.
a) Representative kymographs of dyneinGal with increasing concentrations of unlabeled Lis1. Assays were performed in 1 mM ATP and 150 mM KAc. b) The velocity of dyneinGal under different Lis1 concentrations (mean ± s.e.m.; N = 611, 694, 230, 260, 251, and 852 from left to right; two biological replicates). c) 1-CDF of run time and run length of dyneinGal under different Lis1 concentrations. Fitting to a double exponential decay (solid curves) reveals the weighted average of run time and run length of the motor in each condition (bar graphs, ± s.e.; N = 611, 694, and 852 from left to right). d) Representative kymographs of dyneinGal in the presence or absence of 1,000 nM unlabeled Lis15A. e) The velocity, run time, and run length of dyneinGal in the presence or absence of 1,000 nM Lis15A (N = 610 and 209 from left to right). The center line and whiskers represent the mean and s.d., respectively. In c and e, P values were calculated by a two-tailed t-test with Welch correction for velocity and by the two-tailed Kolmogorov-Smirnov test for run time and run length.
Extended Data Fig. 4 Motility of dyneinGal in the presence of fluorescently-labeled Lis1.
a) Representative kymographs of two-color imaging of LD655-labeled dyneinGal and LD555-labeled Lis1 under different Lis1 concentrations. b) The velocity, run time, and run length distributions of dyneinGal under different concentrations of Lis1 (N = 611, 526, 168, 233, 175, 55, 69, 126, and 145 from left to right). c) The fraction of LD655-dyneinGal that colocalizes with LD555-Lis1 under different Lis1 concentrations. A fit to a binding isotherm function (solid curve, see Methods) reveals KD (±s.e.). d) The velocity distribution of dyneinGal in the absence of Lis1 compared to the motors that do not colocalize with Lis1 when fluorescently labeled Lis1 is present in the chamber (N = 611 and 233 from left to right). e) Representative kymographs show colocalization of 5 nM TMR-labeled and 5 nM Cy5-labeled Lis1 to unlabeled dyneinGal. f) Velocity, run length, and run time distributions of dyneinGal in the absence (light gray) and presence of Lis1 (N = 287, 233, 175, and 274 from left to right). DyneinGal motors that colocalize with 0, 1, or 2 colors of Lis1 were analyzed separately. In b, d, and f, the center line and whiskers represent the mean and s.d., respectively. P values were calculated by two-tailed t-tests with Welch correction for velocity and by the two-tailed Kolmogorov-Smirnov test for run time and run-length measurements.
Extended Data Fig. 5 The addition and removal of Lis1 whilst recording dynein motility.
a) A kymograph (left) and velocity (right) of dynein before and after Lis1 was flown into the chamber (red arrowhead and a dashed line, N = 44 and 42 from left to right). b) A kymograph of dyneinGal when Lis1 was flown into the chamber (red arrowhead and a dashed line). (Middle) The velocity of the complexes that were already walking on the microtubules during Lis1 addition moved at the same velocity after flowing Lis1 (N = 26 and 26 from left to right). Only the motors that do not colocalize with Lis1 were included in the analysis. (Right) The velocity of the complexes that land onto microtubules within 4 min after Lis1 addition was analyzed (N = 122 and 84 from left to right). The motors that colocalize with Lis1 walked slower than motors that do not colocalize with Lis1. c) A kymograph (left) and velocity (right) of dyneinGal before and after washing excess Lis1 from the flow chamber (red arrowhead and a dashed line). The velocity of the motors that colocalize (+Lis1) or do not colocalize (−Lis1) with Lis1 remained unaltered by removing excess Lis1 from the chamber (N = 9, 9, 22, 22 from left to right). In a, b, and c, assays were performed in 1 mM ATP and 50 mM KAc. The center line and whiskers represent the mean and s.d., respectively. P values were calculated by a two-tailed t-test with Welch correction.
Extended Data Fig. 6 Lis1 reduces the stall force of the tail-truncated dynein.
a) Representative trajectories of beads driven by tail-truncated dynein constructs dimerized with a Glutathione S-transferase (GST) tag (GFP-GST-Dyn331kDa and GFP-GST-Dyn314kDa) in the presence and absence of 300 nM Lis1. Assays were performed in 2 mM ATP. Red arrowheads represent the detachment of the motor from the microtubule followed by the snapping back of the bead to the trap center. b) Stall force histograms of Dyn331kDa and Dyn314kDa in the presence and absence of 300 nM Lis1 (mean ± s.e.m.; p = 2 × 10−7 for Dyn331kDa and 0.006 for Dyn314kDa, two-tailed t-test). c) Stall times of Dyn331kDa and Dyn314kDa in the presence and absence of 300 nM Lis1. Fitting to a double exponential decay (solid curves) reveals the weighted average of stall time (±s.e.).
Extended Data Fig. 7 Lis1 slows the motility but does not substantially affect the stall force of dyneinEQN.
a) Representative kymographs of dyneinEQN motility under different concentrations of unlabeled Lis1. b) The velocity of dyneinEQN motility under different concentrations of unlabeled Lis1 (mean ± s.e.m.; N = 659, 283, 482, 484, 487, 610, and 132 from left to right). The fit of the dyneinEQN velocity data (solid curve) reveals KD (±s.e., see Methods). c) A representative kymograph of a three-color imaging assay shows two Lis1s bind to the same dyneinEQN motor (white arrows). d) The velocities of dyneinEQN motors not colocalizing (-Lis1) or colocalizing (+Lis1) with Lis1 (N = 98 and 92 from left to right). The center line and whiskers represent the mean and s.d., respectively. The P-value was calculated by a two-tailed t-test with Welch correction. e) Representative trajectories of beads driven by dyneinEQN in the presence or absence of 900 nM Lis1 in a fixed trapping assay. Assays were performed in 2 mM ATP. Red arrowheads represent the detachment of the motor from the microtubule followed by the snapping back of the bead to the trap center. f) Stall force histograms of dyneinEQN in the presence and absence of 900 nM Lis1 (mean ± s.e.m.; p = 10−3, two-tailed t-test). g) Stall times of dyneinEQN in the presence and absence of 900 nM Lis1. Fitting to a double exponential decay (solid curves) reveals the weighted average of stall time (±s.e.).
Extended Data Fig. 8 The comparison of the F-V behavior of dynein and dyneinEQN in the presence and absence of Lis1.
(Left) F-V measurements of dynein and dyneinEQN in the absence of Lis1 (mean ±s.e.m., from left to right, N = 41, 38, 37, 861, 27, 52, 106, 28, 51, 60, 89, 115, 124, 62, 23, 38, 40 for dynein and N = 31, 66, 62, 48, 47, 26, 42, 39, 23, 45, 33 for dyneinEQN). (Right) F-V measurements of dynein in 300 nM Lis1 compared to F-V of dyneinEQN in 900 nM Lis1 (mean ±s.e.m., from left to right, N = 34, 52, 25, 312, 33, 42, 49, 37 62, 47 33 42, 36, 29, 18 for dynein; and N = 54, 36, 61, 31, 37, 17, 54, 14, 19, 38, 26 for dyneinEQN). Dynein velocity under assisting forces is lower than that of dyneinEQN in the presence of Lis1. Assays were performed in 2 mM ATP.
Supplementary information
Supplementary Information
Supplementary Table 1: The list of S. cerevisiae strains used in this study.
Supplementary Video 1
Colocalization of two Lis1s to the same dynein dimer: The three-color video shows GFP-dynein colocalized with both LD655-Lis1 and TMR-Lis1 as it moves along the microtubule (arrows). 5 nM final concentration of dynein is incubated on ice with 2 nM TMR-Lis1 and 2 nM LD655-Lis1 for 10 min. The videos were acquired on a time-shared TIRF microscope with a 108 nm effective pixel size and 0.3 s per frame per channel. The videos were analyzed using FIJI. The assay was performed in 1 mM ATP.
Supplementary Video 2
Lis1 binding pauses dynein motility and its unbinding restores dynein velocity: The two-color video shows the binding and unbinding of TMR-Lis1 to Cy5-dynein during processive motility. The red arrows show the position of dynein, whereas the cyan arrows show the Lis1 binding. Lis1 is introduced to the imaging chamber via a microfluidic system as dynein motors walk along the microtubule. The videos were acquired on a time-shared TIRF microscope with a 160 nm effective pixel size and 0.65 s per frame per channel. The videos were analyzed using FIJI. The assay was performed in 1 mM ATP.
Supplementary Video 3
Cy5-dynein moves along the microtubules in the absence of Lis1: Cy5-dynein walking along the microtubules in 1 mM ATP. The assay was performed in the absence of added salt or Lis1. The videos were acquired on a TIRF microscope with a 160 nm effective pixel size and 0.5 s per frame channel time resolution.
Supplementary Video 4
Cy5-dynein moves on a Lis1-decorated microtubule: The two-color video shows that Cy5-dynein motility is not slowed by the presence of Lis1 on the microtubule. 100 nM TMR-Lis1 is flowed into the chamber and allowed to decorate surface-immobilized microtubules in the absence of added salt. The chamber is washed twice with the stepping buffer to remove unbound Lis1 and 5 nM Cy5-dynein was added to the chamber in 1 mM ATP without added salt. The videos were collected on a TIRF microscope with a 160 nm effective pixel size and 0.65 s per frame per channel. The videos were analyzed using FIJI.
Source data
Source Data Fig. 1
Statistical source data.
Source Data Fig. 2
Statistical source data.
Source Data Fig. 3
Statistical source data.
Source Data Fig. 4
Statistical source data.
Source Data Fig. 5
Statistical source data.
Source Data Fig. 6
Statistical source data.
Source Data Extended Data Fig. 1
Statistical source data.
Source Data Extended Data Fig. 2
Statistical source data.
Source Data Extended Data Fig. 2
Unprocessed gel.
Source Data Extended Data Fig. 3
Statistical source data.
Source Data Extended Data Fig. 4
Statistical source data.
Source Data Extended Data Fig. 5
Statistical source data.
Source Data Extended Data Fig. 6
Statistical source data.
Source Data Extended Data Fig. 7
Statistical source data.
Source Data Extended Data Fig. 8
Statistical source data.
Rights and permissions
Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.
About this article
Cite this article
Kusakci, E., Htet, Z.M., Zhao, Y. et al. Lis1 slows force-induced detachment of cytoplasmic dynein from microtubules. Nat Chem Biol 20, 521–529 (2024). https://doi.org/10.1038/s41589-023-01464-6
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1038/s41589-023-01464-6
- Springer Nature America, Inc.