ArticleMolecular biology of the cell2008
Dynein light intermediate chain: an essential subunit that contributes to spindle checkpoint inactivation.
Article in Molecular biology of the cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
49 citing papers in PubMed.
- Dynein-driven regulation of postsynaptic membrane architecture and synaptic function.Journal of cell science · 2025Article
- Angiogenesis is limited by LIC1-mediated lysosomal trafficking.Angiogenesis · 2024Article
- A force-sensitive mutation reveals a non-canonical role for dynein in anaphase progression.The Journal of cell biology · 2024Article
- Ninein domains required for its localization, association with partners dynein and ensconsin, and microtubule organization.Molecular biology of the cell · 2024Article
- The dynamic duo of microtubule polymerase Mini spindles/XMAP215 and cytoplasmic dynein is essential for maintainingProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Article
- Structural and functional properties of the Kunitz-type and C-terminal domains of Amblyomin-X supporting its antitumor activity.Frontiers in molecular biosciences · 2023Article
- Conformational transitions of the Spindly adaptor underlie its interaction with Dynein and Dynactin.The Journal of cell biology · 2022Article
- Dync1li1 is required for the survival of mammalian cochlear hair cells by regulating the transportation of autophagosomes.PLoS genetics · 2022Article
- Structure of the RZZ complex and molecular basis of Spindly-driven corona assembly at human kinetochores.The EMBO journal · 2022Article
- DYNC1LI2 regulates localization of the chaperone-mediated autophagy receptor LAMP2A and improves cellular homeostasis in cystinosis.Autophagy · 2022Article
- Article
- Homozygous mutation inFrontiers in endocrinology · 2022Article
- Kinetochore assembly throughout the cell cycle.Seminars in cell & developmental biology · 2021Article
- Polarized endosome dynamics engage cytoplasmic Par-3 that recruits dynein during asymmetric cell division.Science advances · 2021Article
- Dynamics of kinetochore structure and its regulations during mitotic progression.Cellular and molecular life sciences : CMLS · 2020Review
- Cyclin B1 scaffolds MAD1 at the kinetochore corona to activate the mitotic checkpoint.The EMBO journal · 2020Article
- The centromere comes into focus: from CENP-A nucleosomes to kinetochore connections with the spindle.Open biology · 2020Review
- A transient helix in the disordered region of dynein light intermediate chain links the motor to structurally diverse adaptors for cargo transport.PLoS biology · 2019Article
- The kinetochore proteins CENP-E and CENP-F directly and specifically interact with distinct BUB mitotic checkpoint Ser/Thr kinases.The Journal of biological chemistry · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
Abstract
The dynein light intermediate chain (LIC) is a subunit unique to the cytoplasmic form of dynein, but how it contributes to dynein function is not fully understood. Previous work has established that the LIC homodimer binds directly to the dynein heavy chain and may mediate the attachment of dynein to centrosomes and other cargoes. Here, we report our characterization of the LIC in Drosophila. Unlike vertebrates, in which two Lic genes encode multiple subunit isoforms, the Drosophila LIC is encoded by a single gene. We determined that the single LIC polypeptide is phosphorylated, and that different phosphoisoforms can assemble into the dynein motor complex. Our mutational analyses demonstrate that, similar to other dynein subunits, the Drosophila LIC is required for zygotic development, germline specification of the oocyte, and mitotic cell division. We show that RNA interference depletion of LIC in Drosophila S2 cells does not block the recruitment of a dynein complex to kinetochores, but it does delay inactivation of Mad2 signaling and mitotic progression. Our observations suggest the LIC contributes to a broad range of dynein functions.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.