ArticleThe Journal of cell biology2021
Phosphorylation and Pin1 binding to the LIC1 subunit selectively regulate mitotic dynein functions.
Article in The Journal of cell biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Phosphorylation in the dynein light intermediate chain 2 isoform enables Pin1 binding and modulates cargo-adaptor interactions.Journal of structural biology: X · 2026Article
- Morphological map of under- and overexpression of genes in human cells.Nature methods · 2025Article
- Quantitative Analysis of Kinetochore Protein Levels and Inter-Kinetochore Distances in Mammalian Cells During Mitosis.Bio-protocol · 2024Article
- PEP-1-PIN1 Promotes Hippocampal Neuronal Cell Survival by Inhibiting Cellular ROS and MAPK Phosphorylation.Biomedicines · 2024Article
- Pin1-catalyzed conformational regulation after phosphorylation: A distinct checkpoint in cell signaling and drug discovery.Science signaling · 2024Review
- Solution NMR Backbone Assignment of the C-Terminal Region of Human Dynein Light Intermediate Chain 2 (LIC2-C) Unveils Structural Resemblance with Its Homologue LIC1-C.Magnetochemistry (Basel, Switzerland) · 2023Article
- The meiotic LINC complex component KASH5 is an activating adaptor for cytoplasmic dynein.The Journal of cell biology · 2023Article
- Article
- The regulatory role of Pin1 in neuronal death.Neural regeneration research · 2023Review
- A bibliometric analysis of PIN1 and cell death.Frontiers in cell and developmental biology · 2022Article
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The dynein motor performs multiple functions in mitosis by engaging with a wide cargo spectrum. One way to regulate dynein's cargo-binding selectivity is through the C-terminal domain (CTD) of its light intermediate chain 1 subunit (LIC1), which binds directly with cargo adaptors. Here we show that mitotic phosphorylation of LIC1-CTD at its three cdk1 sites is required for proper mitotic progression, for dynein loading onto prometaphase kinetochores, and for spindle assembly checkpoint inactivation in human cells. Mitotic LIC1-CTD phosphorylation also engages the prolyl isomerase Pin1 predominantly to Hook2-dynein-Nde1-Lis1 complexes, but not to dynein-spindly-dynactin complexes. LIC1-CTD dephosphorylation abrogates dynein-Pin1 binding, promotes prophase centrosome-nuclear envelope detachment, and impairs metaphase chromosome congression and mitotic Golgi fragmentation, without affecting interphase membrane transport. Phosphomutation of a conserved LIC1-CTD SP site in zebrafish leads to early developmental defects. Our work reveals that LIC1-CTD phosphorylation differentially regulates distinct mitotic dynein pools and suggests the evolutionary conservation of this phosphoregulation.
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