The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The requested protein is correctly identified as Pac1 from Saccharomyces cerevisiae S288c, encoded by PAC1/YOR269W and represented by UniProt P39946. It is the budding-yeast homolog of LIS1/NudF and belongs to the conserved WD-repeat LIS1 family. The literature-supported architecture—an N-terminal dimerization/coiled-coil region followed by seven WD40 repeats forming β-propeller domains—matches the supplied domain annotations. This report excludes unrelated genes named PAC1 in other organisms. (lee2003theroleof pages 8-9, gillies2022structuralbasisfor pages 1-2)
Pac1 is not an enzyme, transporter, or structural microtubule component. Its primary function is that of a non-catalytic, dimeric regulator of cytoplasmic dynein. It binds directly to the Dyn1 motor domain, promotes an open or activation-competent dynein conformation, supports delivery and retention of dynein at cytoplasmic-microtubule plus ends, and regulates the transition from a targeted motor complex to an active cortical force generator. This pathway positions the mitotic spindle and moves the nucleus through the mother–bud neck. (lee2003theroleof pages 1-1, gillies2022structuralbasisfor pages 1-2, gillies2022structuralbasisfor pages 16-17, karasmanis2023lis1relievescytoplasmic pages 1-2)
The identity criteria are internally consistent:
Thus, the supplied PAC1–P39946–YOR269W assignment is biologically coherent. Reports about mammalian PAC1 receptors, phosphatases, or unrelated PAC1 genes were not treated as evidence for this protein.
Pac1 binds directly to the motor domain of the dynein heavy chain Dyn1. Structural work identifies two principal interfaces: a ring site near AAA3/AAA4 in dynein’s AAA+ motor ring and a stalk site near the stalk emerging from AAA4. Pac1 dimerization and the integrity of both interfaces are important for dynein localization and function in yeast. A 3.1-Å cryo-EM structure resolved these contacts at high resolution. (gillies2022structuralbasisfor pages 1-2, gillies2022structuralbasisfor pages 16-17)
Pac1 should therefore be annotated as a dynein-activating and targeting cofactor. It does not supply ATPase activity; ATP hydrolysis and force production reside in Dyn1. Pac1 instead controls dynein’s conformational ensemble and mechanochemistry. Its binding at the motor ring is sterically incompatible with dynein’s compact autoinhibited “Phi” state, favoring an open state that can proceed toward active assemblies. However, Pac1 has additional effects beyond simply breaking Phi autoinhibition, because mutations at its ring and stalk interfaces continue to affect cortical targeting and spindle positioning even in some dynein backgrounds with weakened Phi autoinhibition. (gillies2022structuralbasisfor pages 16-17, gillies2022structuralbasisfor pages 11-13)
Structure-guided endogenous mutations strengthen this assignment. Pac1 E253A/H254A at the ring-associated interface substantially reduced dynein foci at spindle-pole bodies, microtubule plus ends, and the cortex. Pac1 S248Q at the stalk-associated interface produced a partial separation-of-function phenotype that preserved plus-end localization better than subsequent cortical localization. Mutations F185D/I189D/R494A affecting the Pac1–Pac1 interface also impaired localization or function, supporting an important role for Pac1 dimerization. (gillies2022structuralbasisfor pages 11-13)
Pac1 acts principally in the cytoplasm at three connected sites: cytoplasmic-microtubule plus ends, spindle-pole-body-associated microtubules, and the bud cortex during dynein offloading or activation.
Pac1 and Dyn1 form a complex before or during recruitment to plus ends decorated by Bik1, the yeast CLIP-170 homolog. Pac1 and Dyn1 depend reciprocally on one another and on Bik1 for efficient plus-end localization, whereas Bik1 localization is comparatively independent of Pac1 and Dyn1. Quantitative imaging and purification suggested approximately coordinated, near-1:1 loading of Pac1 and Dyn1; increasing Bik1 recruited roughly equal additional amounts of each. Kinesin Kip2 contributes to transport toward plus ends, although cytosolic recruitment also occurs. (markus2011quantitativeanalysisof pages 1-2, gillies2022structuralbasisfor pages 16-17)
Pac1 is necessary for productive Dyn1 accumulation at distal cytoplasmic-microtubule tips. Early imaging found that Pac1 tip localization could occur independently of Dyn1, whereas subsequent quantitative work showed reciprocal dependence under other assay conditions; the combined evidence supports a cooperative targeting system rather than Pac1 functioning merely as a passive dynein cargo. (lee2003theroleof pages 8-9, markus2011quantitativeanalysisof pages 1-2, lee2003theroleof pages 1-1)
Plus ends probe the bud cortex. At Num1-containing cortical sites, dynein and associated factors are transferred or “offloaded” from the microtubule tip to the cortex. Dynactin acts downstream of initial Pac1-dependent tip targeting, contributing to cortical capture, anchoring, activation, and force production. Pac1 and Dyn1 accumulate at plus ends when Num1 or dynactin is absent, supporting this ordering. (lee2003theroleof pages 8-9, lee2003theroleof pages 1-1)
Pac1 must then relinquish dynein for sustained active movement. Recent structural work indicates that dynein’s transition into a microtubule-bound conformation lowers Pac1 affinity. Microtubule binding remodels the AAA5-loop, AAA4-helix, and AAA3-loop region and distorts the Pac1-binding geometry by approximately 3.2 Å. This provides an allosteric mechanism for Pac1 release before sustained cortical or cargo-associated transport. The precise temporal sequence among microtubule binding, Num1 engagement, dynactin assembly, and complete Pac1 dissociation remains an active mechanistic question rather than a fully resolved linear pathway. (ton2022microtubulebindinginducedallostery pages 14-15)
Once anchored at cortical Num1 sites and associated with dynactin, dynein pulls on cytoplasmic microtubules through lateral sliding and end-capture/shrinkage mechanisms. These forces draw the spindle and nucleus toward and through the mother–bud neck. Pac1 is thus upstream of force production but essential for placing dynein into the correct spatial and conformational state. (lee2003theroleof pages 8-9, lee2003theroleof pages 1-1)
The best-defined biological role is the dynein-dependent phase of mitotic nuclear migration and spindle positioning. Cells lacking functional Pac1 lose productive microtubule sliding along the bud cortex and exhibit defective spindle movement and nuclear segregation. In one quantitative analysis, approximately 83% of an elongating spindle could remain on the mother-cell side. Some mutant microtubules became laterally plastered against the bud cortex but failed to slide and detached after roughly 10 seconds. (lee2003theroleof pages 1-1, lee2003theroleof pages 2-3)
These defects are not explained by a general collapse of microtubule dynamics. Reported growth rates were similar in pac1 and wild type—4.92 versus 4.67 µm min⁻¹—and shrinkage rates were 5.59 versus 4.91 µm min⁻¹, with no major qualitative change in catastrophe or rescue. Pac1 therefore regulates productive dynein targeting and force generation rather than serving as a general controller of microtubule polymerization. (lee2003theroleof pages 2-3)
| Topic | Conclusion | Location / partners | Strongest evidence type | Key quantitative result or caveat |
|---|---|---|---|---|
| Identity and architecture | PAC1 encodes budding-yeast Pac1, the conserved LIS1/nudF-family dynein regulator matching P39946/YOR269W. It has an N-terminal dimerization/coiled-coil region and seven C-terminal WD40 repeats forming β-propellers. | S. cerevisiae S288c cytoplasm; Pac1 homodimer; Dyn1 dynein | Yeast genetics, domain analysis, and structural biology (lee2003theroleof pages 8-9, gillies2022structuralbasisfor pages 1-2) | Direct yeast evidence supports the identity and seven-WD-repeat architecture. Same-symbol genes in other organisms are not interchangeable with this target. |
| Primary molecular function | Pac1 is a nonenzymatic dynein cofactor, not an enzyme or transporter. It directly binds the Dyn1 motor domain, regulates dynein mechanochemistry, favors an activation-competent state, and enables correct motor targeting. | Dyn1 AAA+ ring and stalk; Pac1–Pac1 interface | Biochemistry, structure-guided mutagenesis, live-cell imaging, and yeast genetics (gillies2022structuralbasisfor pages 1-2, gillies2022structuralbasisfor pages 16-17) | Ring-, stalk-, and dimer-interface mutations impair cortical dynein delivery and spindle positioning. Pac1 is an established direct motor-domain-binding dynein regulator. |
| Plus-end targeting | Pac1 and Dyn1 are coordinately recruited to cytoplasmic-microtubule plus ends. Pac1 is required for Dyn1 tip localization; Bik1/CLIP-170 and kinesin Kip2 contribute to delivery, while cytosolic recruitment can also occur. | Microtubule plus ends; Dyn1, Bik1, Kip2 | Endogenous fluorescence imaging, co-purification, dosage experiments, and genetics (markus2011quantitativeanalysisof pages 1-2, gillies2022structuralbasisfor pages 16-17) | Pac1 and Dyn1 were inferred to load at approximately 1:1 stoichiometry. Increasing Bik1 recruits roughly equal amounts of both, and Pac1 overexpression increases Dyn1 plus-end targeting. |
| Cortical offloading and force generation | Plus-end-associated dynein encounters cortical Num1 sites, where dynein–dynactin is captured or offloaded and activated as Pac1 is released. Active cortical dynein drives lateral microtubule sliding or end-capture/shrinkage forces. | Bud cortex; Num1, dynactin/Arp1, cytoplasmic microtubules | Live-cell imaging and yeast loss-of-function genetics (lee2003theroleof pages 8-9, lee2003theroleof pages 1-1) | Pac1 and Dyn1 accumulate at plus ends when Num1 or dynactin is absent, supporting a later role for these proteins in offloading or activation. The exact order of Pac1 release and Num1 engagement remains a dynamic mechanistic model. |
| Spindle positioning and nuclear segregation | Pac1-dependent cortical dynein pulls spindle-pole-body-associated microtubules, moving the nucleus and anaphase spindle through the mother–bud neck. Pac1 loss abolishes productive cortical sliding and disrupts spindle positioning and nuclear segregation. | Bud cortex, cytoplasmic microtubules, spindle pole bodies, mother–bud neck | Time-lapse microscopy and deletion-mutant phenotyping (lee2003theroleof pages 1-1, lee2003theroleof pages 2-3) | About 83% of spindle length could remain on the mother side in mutants; cortex-associated microtubules detached after approximately 10 s instead of sliding. Growth rates were similar in mutant and wild type, 4.92 versus 4.67 µm min⁻¹. |
| 2022 dynein–Pac1 structure | A high-resolution yeast complex established two conserved Pac1 contacts: a ring site near AAA3/AAA4 and a stalk site emerging from AAA4. Pac1 dimerization and both interfaces contribute to in-vivo dynein function. | Dyn1 AAA+ ring and stalk; paired Pac1 β-propellers | Cryo-EM and structure-guided endogenous yeast mutations (gillies2022structuralbasisfor pages 1-2, gillies2022structuralbasisfor pages 16-17, gillies2022structuralbasisfor pages 11-13) | The structure was resolved at 3.1 Å. Pac1 E253A/H254A strongly reduced dynein foci; S248Q was a partial separation-of-function mutant; F185D/I189D/R494A altered the Pac1 dimer interface. Some activation conclusions rely partly on human reconstitution. |
| 2023 Chi molecular-wedge complex | Two Pac1/Lis1 dimers wedge between two yeast dynein motor domains in the Chi intermediate, opposing the autoinhibited Phi arrangement and promoting progression toward active dynein complexes. | Between paired Dyn1 motor domains; Chi contacts | Yeast cryo-EM, structure-guided S. cerevisiae assays, and human reconstitution (karasmanis2023lis1relievescytoplasmic pages 1-2) | The observed complex contains two motor domains and two Pac1/Lis1 dimers. Chi contacts were required for Pac1 regulation in yeast; effects on dynein–dynactin–adaptor assembly were tested mainly with human proteins. |
| Microtubule-triggered Pac1 release | Dynein’s transition into its microtubule-bound conformation lowers Pac1 affinity, providing an allosteric mechanism for regulator release before sustained cortical or cargo-associated transport. | Dyn1 ring–stalk pathway; microtubule; subsequently Num1-associated dynein | Cryo-EM, conformational mutants, chromatography, and yeast cellular-focus assays (ton2022microtubulebindinginducedallostery pages 14-15) | Microtubule binding remodels the AAA5-loop, AAA4-helix, and AAA3-loop interface and distorts the Pac1-binding site by approximately 3.2 Å. Temporal coupling to Num1 in living yeast remains partly model-based. |
| 2024 force and motility mechanism | With purified yeast dynein, Pac1/Lis1 slows movement through its AAA+ ring interaction and prolongs stalls. Stalk binding reduces force-induced detachment by interfering with stalk-registry changes but does not measurably increase force generation. | Dyn1 AAA+ ring, stalk, and microtubule under assisting or hindering load | Single-molecule fluorescence and optical trapping (kusakci2024lis1slowsforceinduced pages 1-3, kusakci2023lis1bindingregulates pages 7-9, kusakci2024lis1slowsforceinduced pages 22-23) | One regulator slows dynein and increases run time; two enhance both effects. Stalk-interface mutations partly restore detachment asymmetry but not velocity. These are direct purified yeast-motor results, not whole-cell measurements. |
Table: Compact evidence map for S. cerevisiae S288c Pac1/P39946, covering identity, localization, dynein regulation, cellular function, and recent structural and biophysical advances. It distinguishes direct yeast evidence from conserved mechanisms inferred partly through mammalian LIS1 systems.
Karasmanis and colleagues visualized an activation intermediate termed Chi, containing two yeast dynein motor domains and two Lis1/Pac1 dimers. The Pac1 dimers are wedged between the motor domains, preventing or resolving the autoinhibited Phi arrangement. Chi-contact mutations impaired Pac1-dependent dynein regulation in S. cerevisiae, while complementary human reconstitution showed that equivalent contacts support assembly of active dynein–dynactin–adaptor complexes. This study supplies strong direct yeast evidence for the wedge mechanism, but claims about complete cargo-adaptor complex assembly derive partly from the human system. Published online 24 August 2023 in Nature Structural & Molecular Biology; DOI: https://doi.org/10.1038/s41594-023-01069-6. (karasmanis2023lis1relievescytoplasmic pages 1-2)
Ton and colleagues showed that dynein’s microtubule-bound conformational state has lower Pac1/LIS1 affinity than its microtubule-unbound state. The work links motor-domain allostery to release of Pac1 before processive transport and explains why Pac1 can be required for targeting and activation yet absent from the final motile complex. The yeast evidence includes motor-domain conformational mutants, Pac1 binding assays, structural comparison, and cellular dynein-focus assays; the approximately 3.2-Å deformation of the binding site provides a structural basis. Peer-reviewed version: Nature Structural & Molecular Biology 30, 1365–1379; DOI: https://doi.org/10.1038/s41594-023-01010-x. (ton2022microtubulebindinginducedallostery pages 14-15)
Kusakci and colleagues used purified budding-yeast dynein with Pac1/Lis1 in single-molecule and optical-trapping experiments. Pac1 slowed movement through its interaction with the AAA+ ring rather than acting as a physical roadblock or simple microtubule tether. It prolonged stalls and reduced the normal directional asymmetry of force-induced detachment without measurably increasing dynein’s force generation. Mutating stalk contacts partly restored detachment asymmetry but did not restore velocity, separating the ring-mediated slowing effect from the stalk-mediated resistance to detachment. Experiments further indicated that one bound regulator slows dynein and increases run time, with two producing stronger effects. Published in 2024 in Nature Chemical Biology 20, 521–529; DOI: https://doi.org/10.1038/s41589-023-01464-6. (kusakci2024lis1slowsforceinduced pages 1-3, kusakci2023lis1bindingregulates pages 7-9, kusakci2024lis1slowsforceinduced pages 22-23)
Together, these recent studies reconcile apparently opposing descriptions of LIS1-family proteins as dynein activators and motility inhibitors. Pac1 is a positive regulator at the assembly and targeting stages, but persistent occupancy during movement can slow the motor and stabilize microtubule attachment. Timely dissociation is therefore part of normal activation. (ton2022microtubulebindinginducedallostery pages 14-15, kusakci2024lis1slowsforceinduced pages 1-3, karasmanis2023lis1relievescytoplasmic pages 1-2)
Pac1 has no direct industrial or clinical application in budding yeast. Its principal real-world use is as an experimentally tractable model for conserved LIS1–dynein regulation. Yeast permits endogenous mutagenesis, live-cell imaging of spindle positioning, purification of unusually stable dynein, cryo-EM, and single-molecule force measurements. These approaches have defined interfaces and conformational intermediates that are difficult to isolate in mammalian cells. (gillies2022structuralbasisfor pages 1-2, kusakci2024lis1slowsforceinduced pages 1-3, karasmanis2023lis1relievescytoplasmic pages 1-2)
The translational relevance is indirect but substantial: human LIS1 insufficiency causes lissencephaly, and the dynein-binding surfaces and activation principles are strongly conserved. Nevertheless, yeast Pac1 phenotypes should not be equated directly with neuronal migration or human disease, and findings from human dynein–dynactin–adaptor reconstitution should not automatically be assigned to the simpler yeast cortical pathway. (gillies2022structuralbasisfor pages 1-2, karasmanis2023lis1relievescytoplasmic pages 1-2)
The core annotation is supported by convergent genetics, live-cell imaging, biochemistry, cryo-EM, structure-guided mutation, single-molecule imaging, and optical trapping. The strongest conclusions are that Pac1 directly binds dynein, is required for plus-end targeting and cortical delivery, and enables dynein-dependent spindle positioning. (lee2003theroleof pages 1-1, gillies2022structuralbasisfor pages 1-2, gillies2022structuralbasisfor pages 16-17)
Three issues remain less certain. First, the exact contribution of direct Pac1–microtubule binding versus recruitment through Dyn1, Bik1, or another plus-end factor remains incompletely resolved. Second, the order and kinetics of Pac1 release relative to Num1 and dynactin engagement have not been fully measured in living cells. Third, Pac1’s effects vary by state: it opens or targets dynein before activation but slows motility and detachment when it remains motor-bound. These are state-dependent functions, not contradictory annotations. (lee2003theroleof pages 8-9, ton2022microtubulebindinginducedallostery pages 14-15, kusakci2024lis1slowsforceinduced pages 1-3)
Pac1 is a dimeric WD40-repeat LIS1-family regulator of cytoplasmic dynein. It binds the Dyn1 AAA+ motor ring and stalk, promotes an open activation-competent motor state, and enables dynein recruitment to cytoplasmic-microtubule plus ends through a Bik1/Kip2-associated targeting pathway. Following cortical encounter, Pac1 dissociation permits Num1/dynactin-associated dynein to generate microtubule-sliding and pulling forces required for mitotic spindle positioning and nuclear segregation across the mother–bud neck. Pac1 has no known catalytic reaction or transported substrate.
References
(lee2003theroleof pages 8-9): Wei-Lih Lee, Jessica R. Oberle, and John A. Cooper. The role of the lissencephaly protein pac1 during nuclear migration in budding yeast. The Journal of Cell Biology, 160:355-364, Feb 2003. URL: https://doi.org/10.1083/jcb.200209022, doi:10.1083/jcb.200209022. This article has 301 citations.
(gillies2022structuralbasisfor pages 1-2): John P Gillies, Janice M Reimer, Eva P Karasmanis, Indrajit Lahiri, Zaw Min Htet, Andres E Leschziner, and Samara L Reck-Peterson. Structural basis for cytoplasmic dynein-1 regulation by lis1. Jan 2022. URL: https://doi.org/10.7554/elife.71229, doi:10.7554/elife.71229. This article has 51 citations and is from a domain leading peer-reviewed journal.
(lee2003theroleof pages 1-1): Wei-Lih Lee, Jessica R. Oberle, and John A. Cooper. The role of the lissencephaly protein pac1 during nuclear migration in budding yeast. The Journal of Cell Biology, 160:355-364, Feb 2003. URL: https://doi.org/10.1083/jcb.200209022, doi:10.1083/jcb.200209022. This article has 301 citations.
(gillies2022structuralbasisfor pages 16-17): John P Gillies, Janice M Reimer, Eva P Karasmanis, Indrajit Lahiri, Zaw Min Htet, Andres E Leschziner, and Samara L Reck-Peterson. Structural basis for cytoplasmic dynein-1 regulation by lis1. Jan 2022. URL: https://doi.org/10.7554/elife.71229, doi:10.7554/elife.71229. This article has 51 citations and is from a domain leading peer-reviewed journal.
(karasmanis2023lis1relievescytoplasmic pages 1-2): Eva P. Karasmanis, Janice M. Reimer, Agnieszka A. Kendrick, Kendrick H. V. Nguyen, Jennifer A. Rodriguez, Joey B. Truong, Indrajit Lahiri, Samara L. Reck-Peterson, and Andres E. Leschziner. Lis1 relieves cytoplasmic dynein-1 autoinhibition by acting as a molecular wedge. Nature Structural & Molecular Biology, 30:1357-1364, Aug 2023. URL: https://doi.org/10.1038/s41594-023-01069-6, doi:10.1038/s41594-023-01069-6. This article has 35 citations and is from a highest quality peer-reviewed journal.
(gillies2022structuralbasisfor pages 11-13): John P Gillies, Janice M Reimer, Eva P Karasmanis, Indrajit Lahiri, Zaw Min Htet, Andres E Leschziner, and Samara L Reck-Peterson. Structural basis for cytoplasmic dynein-1 regulation by lis1. Jan 2022. URL: https://doi.org/10.7554/elife.71229, doi:10.7554/elife.71229. This article has 51 citations and is from a domain leading peer-reviewed journal.
(markus2011quantitativeanalysisof pages 1-2): Steven M. Markus, Karen M. Plevock, Bryan J. St. Germain, Jesse J. Punch, Christopher W. Meaden, and Wei‐Lih Lee. Quantitative analysis of pac1/lis1‐mediated dynein targeting: implications for regulation of dynein activity in budding yeast. Cytoskeleton, 68:157-174, Mar 2011. URL: https://doi.org/10.1002/cm.20502, doi:10.1002/cm.20502. This article has 85 citations and is from a peer-reviewed journal.
(ton2022microtubulebindinginducedallostery pages 14-15): William D. Ton, Yue Wang, Pengxin Chai, Cissloyny Beauchamp-Perez, Nicholas T. Flint, Lindsay G. Lammers, Hao Xiong, Kai Zhang, and Steven M. Markus. Microtubule binding-induced allostery promotes lis1 dissociation from dynein prior to cargo transport. BioRxiv, Nov 2022. URL: https://doi.org/10.1101/2022.11.08.515461, doi:10.1101/2022.11.08.515461. This article has 5 citations.
(lee2003theroleof pages 2-3): Wei-Lih Lee, Jessica R. Oberle, and John A. Cooper. The role of the lissencephaly protein pac1 during nuclear migration in budding yeast. The Journal of Cell Biology, 160:355-364, Feb 2003. URL: https://doi.org/10.1083/jcb.200209022, doi:10.1083/jcb.200209022. This article has 301 citations.
(kusakci2024lis1slowsforceinduced pages 1-3): Emre Kusakci, Zaw Min Htet, Yuanchang Zhao, John P. Gillies, Samara L. Reck-Peterson, and Ahmet Yildiz. Lis1 slows force-induced detachment of cytoplasmic dynein from microtubules. Nature chemical biology, 20:521-529, Nov 2024. URL: https://doi.org/10.1038/s41589-023-01464-6, doi:10.1038/s41589-023-01464-6. This article has 6 citations and is from a highest quality peer-reviewed journal.
(kusakci2023lis1bindingregulates pages 7-9): Emre Kusakci, Zaw Min Htet, Yuanchang Zhao, John P. Gillies, Samara L. Reck-Peterson, and Ahmet Yildiz. Lis1 binding regulates force-induced detachment of cytoplasmic dynein from microtubules. bioRxiv, Sep 2023. URL: https://doi.org/10.1101/2022.06.02.494578, doi:10.1101/2022.06.02.494578. This article has 2 citations.
(kusakci2024lis1slowsforceinduced pages 22-23): Emre Kusakci, Zaw Min Htet, Yuanchang Zhao, John P. Gillies, Samara L. Reck-Peterson, and Ahmet Yildiz. Lis1 slows force-induced detachment of cytoplasmic dynein from microtubules. Nature chemical biology, 20:521-529, Nov 2024. URL: https://doi.org/10.1038/s41589-023-01464-6, doi:10.1038/s41589-023-01464-6. This article has 6 citations and is from a highest quality peer-reviewed journal.