ArticleThe Journal of cell biology1999
A nonerythroid isoform of protein 4.1R interacts with the nuclear mitotic apparatus (NuMA) protein.
Article in The Journal of cell biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 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
41 citing papers in PubMed.
- Alternative splicing repurposes the Drosophila mitotic regulator Mud for meiotic functions.Genetics · 2025Article
- FERM domain-containing proteins are active components of the cell nucleus.Life science alliance · 2024Review
- Cytoskeletal Protein 4.1R in Health and Diseases.Biomolecules · 2024Review
- 4.1N-Mediated Interactions and Functions in Nerve System and Cancer.Frontiers in molecular biosciences · 2021Review
- PP2A--B55γ counteracts Cdk1 and regulates proper spindle orientation through the cortical dynein adaptor NuMA.Journal of cell science · 2020Article
- NuMA1 promotes axon initial segment assembly through inhibition of endocytosis.The Journal of cell biology · 2020Article
- Epithelial-specific isoforms of protein 4.1R promote adherens junction assembly in maturing epithelia.The Journal of biological chemistry · 2020Article
- Num1 versus NuMA: insights from two functionally homologous proteins.Biophysical reviews · 2018Review
- Protein 4.1R Influences Myogenin Protein Stability and Skeletal Muscle Differentiation.The Journal of biological chemistry · 2016Article
- FRMD3 gene: its role in diabetic kidney disease. A narrative review.Diabetology & metabolic syndrome · 2015Review
- NuMA interacts with phosphoinositides and links the mitotic spindle with the plasma membrane.The EMBO journal · 2014Article
- Article
- Cortical dynein and asymmetric membrane elongation coordinately position the spindle in anaphase.Cell · 2013Article
- Activation of Stat3 in endothelial cells following hypoxia-reoxygenation is mediated by Rac1 and protein Kinase C.Biochimica et biophysica acta · 2012Article
- And the dead shall rise: actin and myosin return to the spindle.Developmental cell · 2011Review
- Structural protein 4.1R is integrally involved in nuclear envelope protein localization, centrosome-nucleus association and transcriptional signaling.Journal of cell science · 2011Article
- The spectrin-ankyrin-4.1-adducin membrane skeleton: adapting eukaryotic cells to the demands of animal life.Protoplasma · 2010Review
- NMR characterisation of the minimal interacting regions of centrosomal proteins 4.1R and NuMA1: effect of phosphorylation.BMC biochemistry · 2010Article
- Protein 4.1R links E-cadherin/beta-catenin complex to the cytoskeleton through its direct interaction with beta-catenin and modulates adherens junction integrity.Biochimica et biophysica acta · 2009Article
- Inhibition of protein 4.1 R and NuMA interaction by mutagenization of their binding-sites abrogates nuclear localization of 4.1 R.Clinical and translational science · 2009Article
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
Red blood cell protein 4.1 (4.1R) is an 80- kD erythrocyte phosphoprotein that stabilizes the spectrin/actin cytoskeleton. In nonerythroid cells, multiple 4.1R isoforms arise from a single gene by alternative splicing and predominantly code for a 135-kD isoform. This isoform contains a 209 amino acid extension at its NH2 terminus (head piece; HP). Immunoreactive epitopes specific for HP have been detected within the cell nucleus, nuclear matrix, centrosomes, and parts of the mitotic apparatus in dividing cells. Using a yeast two-hybrid system, in vitro binding assays, coimmunolocalization, and coimmunoprecipitation studies, we show that a 135-kD 4.1R isoform specifically interacts with the nuclear mitotic apparatus (NuMA) protein. NuMA and 4.1R partially colocalize in the interphase nucleus of MDCK cells and redistribute to the spindle poles early in mitosis. Protein 4.1R associates with NuMA in the interphase nucleus and forms a complex with spindle pole organizing proteins, NuMA, dynein, and dynactin during cell division. Overexpression of a 135-kD isoform of 4.1R alters the normal distribution of NuMA in the interphase nucleus. The minimal sequence sufficient for this interaction has been mapped to the amino acids encoded by exons 20 and 21 of 4.1R and residues 1788-1810 of NuMA. Our results not only suggest that 4.1R could, possibly, play an important role in organizing the nuclear architecture, mitotic spindle, and spindle poles, but also could define a novel role for its 22-24-kD domain.
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.