ArticleThe Journal of biological chemistry2017
Differential effects of the dynein-regulatory factor Lissencephaly-1 on processive dynein-dynactin motility.
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed, 81 citations in OpenAlex.
- Synthetic cargo adaptors reveal molecular features that enhance dynein activation.Nature communications · 2026Article
- Article
- PACS1 syndrome mutation disrupts dynein-mediated cargo transport via HDAC6 and BICD2.Communications biology · 2026Article
- CCSer2 gates dynein activity at the cell periphery.The Journal of cell biology · 2025Article
- Systems mapping of bidirectional endosomal transport through the crowded cell.Current biology : CB · 2024Article
- An Arabidopsis Kinesin-14D motor is associated with midzone microtubules for spindle morphogenesis.Current biology : CB · 2024Article
- CCSer2 gates dynein activity at the cell periphery.bioRxiv : the preprint server for biology · 2024Article
- Dynein and dynactin move long-range but are delivered separately to the axon tip.The Journal of cell biology · 2024Article
- Lis1 slows force-induced detachment of cytoplasmic dynein from microtubules.Nature chemical biology · 2024Article
- Molecular mechanism of dynein-dynactin complex assembly by LIS1.Science (New York, N.Y.) · 2024Article
- Nde1 promotes Lis1-mediated activation of dynein.Nature communications · 2023Article
- Conserved roles for the dynein intermediate chain and Ndel1 in assembly and activation of dynein.Nature communications · 2023Article
- Nde1 Promotes Lis1-Mediated Activation of Dynein.bioRxiv : the preprint server for biology · 2023Article
- New pieces for the Lis1-dynein puzzle.Nature structural & molecular biology · 2023Article
- Lis1 relieves cytoplasmic dynein-1 autoinhibition by acting as a molecular wedge.Nature structural & molecular biology · 2023Article
- Microtubule-binding-induced allostery triggers LIS1 dissociation from dynein prior to cargo transport.Nature structural & molecular biology · 2023Article
- Simulations suggest robust microtubule attachment of kinesin and dynein in antagonistic pairs.Biophysical journal · 2023Article
- Ndel1 disfavors dynein-dynactin-adaptor complex formation in two distinct ways.The Journal of biological chemistry · 2023Article
- The meiotic LINC complex component KASH5 is an activating adaptor for cytoplasmic dynein.The Journal of cell biology · 2023Article
- Article
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4 authors at 2 institutions in 1 country.
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Abstract
Cytoplasmic dynein is the primary minus-end-directed microtubule motor protein in animal cells, performing a wide range of motile activities, including transport of vesicular cargos, mRNAs, viruses, and proteins. Lissencephaly-1 (LIS1) is a highly conserved dynein-regulatory factor that binds directly to the dynein motor domain, uncoupling the enzymatic and mechanical cycles of the motor and stalling dynein on the microtubule track. Dynactin, another ubiquitous dynein-regulatory factor, releases dynein from an autoinhibited state, leading to a dramatic increase in fast, processive dynein motility. How these opposing activities are integrated to control dynein motility is unknown. Here, we used fluorescence single-molecule microscopy to study the interaction of LIS1 with the processive dynein-dynactin-BicD2N (DDB) complex. Surprisingly, in contrast to the prevailing model for LIS1 function established in the context of dynein alone, we found that binding of LIS1 to DDB does not strongly disrupt processive motility. Motile DDB complexes bound up to two LIS1 dimers, and mutational analysis suggested that LIS1 binds directly to the dynein motor domains during DDB movement. Interestingly, LIS1 enhanced DDB velocity in a concentration-dependent manner, in contrast to observations of the effect of LIS1 on the motility of isolated dynein. Thus, LIS1 exerts concentration-dependent effects on dynein motility and can synergize with dynactin to enhance processive dynein movement. Our results suggest that the effect of LIS1 on dynein motility depends on both LIS1 concentration and the presence of other regulatory factors such as dynactin and may provide new insights into the mechanism of LIS1 haploinsufficiency in the neurodevelopmental disorder lissencephaly.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.