Evidence map›Paper›PMID 24109598›Full record

ArticleMolecular biology of the cell2013

NuMA localization, stability, and function in spindle orientation involve 4.1 and Cdk1 interactions.

Lindsey Seldin, Nicholas D Poulson, Henry P Foote, Terry Lechler

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
3.4field-weighted citation impact, top 8% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

58 citing papers in PubMed, 91 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Torques within and outside the human spindle balance twist at anaphase.bioRxiv : the preprint server for biology · 2023
    Article
  7. Combined prediction and design reveals the target recognition mechanism of an intrinsically disordered protein interaction domain.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Anaphase B: Long-standing models meet new concepts.Seminars in cell & developmental biology · 2021
    Review
  19. Article
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Lindsey SeldinDepartment of Cell Biology, Duke University Medical Center, Durham, NC 27710 Department of Dermatology, Duke University Medical Center, Durham, NC 27710.
Nicholas D Poulson
Henry P Foote
Terry Lechler
Duke University · US

Funding

Training Program in Developmental & Stem Cell BiologyT32HD040372 · NICHD · DUKE UNIVERSITY · PI Terry H Lechler · 2001 to 2026
$8.9M
Role of Cell Adhesion and the Cytoskeleton in Epidermal IntegrityR01AR055926 · NIAMS · DUKE UNIVERSITY · PI LECHLER, TERRY H · 2009 to 2019
$3.7M
Mechanisms Driving Asymmetric Cell Division in the EpidermisR03AR056045 · NIAMS · DUKE UNIVERSITY · PI LECHLER, TERRY H · 2009 to 2011
$231k
NIAMS NIH HHS R01 AR055926NIAMS NIH HHS R01AR055926NIAMS NIH HHS R03 AR056045NIAMS NIH HHS R03AR056045NICHD NIH HHS T32 HD040372
6 · The paper itself

Abstract

The epidermis is a multilayered epithelium that requires asymmetric divisions for stratification. A conserved cortical protein complex, including LGN, nuclear mitotic apparatus (NuMA), and dynein/dynactin, plays a key role in establishing proper spindle orientation during asymmetric divisions. The requirements for the cortical recruitment of these proteins, however, remain unclear. In this work, we show that NuMA is required to recruit dynactin to the cell cortex of keratinocytes. NuMA's cortical recruitment requires LGN; however, LGN interactions are not sufficient for this localization. Using fluorescence recovery after photobleaching, we find that the 4.1-binding domain of NuMA is important for stabilizing its interaction with the cell cortex. This is functionally important, as loss of 4.1/NuMA interaction results in spindle orientation defects, using two distinct assays. Furthermore, we observe an increase in cortical NuMA localization as cells enter anaphase. Inhibition of Cdk1 or mutation of a single residue in NuMA mimics this effect. NuMA's anaphase localization is independent of LGN and 4.1 interactions, revealing two distinct mechanisms responsible for NuMA cortical recruitment at different stages of mitosis. This work highlights the complexity of NuMA localization and reveals the importance of NuMA cortical stability for productive force generation during spindle orientation.

Indexed as

AnaphaseAnimalsCDC2 Protein KinaseCell Cycle ProteinsCytoskeletal ProteinsDynactin ComplexDyneinsEnzyme ActivationHumansKeratinocytesMembrane ProteinsMiceMicrotubule-Associated ProteinsMultiprotein ComplexesNuclear ProteinsPhosphorylationCDC2 Protein KinaseCell Cycle ProteinsCytoskeletal ProteinsDynactin ComplexDyneinserythrocyte membrane band 4.1 proteinMembrane ProteinsMicrotubule-Associated ProteinsMultiprotein ComplexesNuclear ProteinsNuma1 protein, mouse

Identifiers

PMID24109598
PMCPMC3842992
OpenAlexW1983460993

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

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.