Evidence map›Paper›PMID 19789182›Full record

ArticleJournal of cell science2009

Tyrosine phosphorylation of nuclear-membrane protein emerin by Src, Abl and other kinases.

Kathryn E Tifft, Katherine A Bradbury, Katherine L Wilson

Open access · greenAbstract read
In one paragraph

Article in Journal of cell science, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

42 citing papers in PubMed, 59 citations in OpenAlex.

  1. Review
  2. Article
  3. The role of inner nuclear membrane protein emerin in myogenesis.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Review
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Components and Mechanisms of Nuclear Mechanotransduction.Annual review of cell and developmental biology · 2021
    Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Nuclear Functions of the Tyrosine Kinase Src.International journal of molecular sciences · 2020
    Review
  18. RareFrontiers in cell and developmental biology · 2019
    Article
  19. Article
  20. Article
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

3 authors at 2 institutions in 1 country.

Kathryn E TifftDepartment of Cell Biology, The Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Katherine A Bradbury
Katherine L Wilson
Johns Hopkins University · USJohns Hopkins Medicine · US

Funding

REGULATION OF NUCLEAR ENVELOPE ASSEMBLY AND DISASSEMBLYR01GM048646 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI WILSON, KATHERINE L · 1994 to 2012
$4.9M
Regulation of nuclear envelope assembly and disassemblyR56GM048646 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI WILSON, KATHERINE L · 2008 to 2008
$487k
NIGMS NIH HHS GM48646
6 · The paper itself

Abstract

X-linked recessive Emery-Dreifuss muscular dystrophy (EDMD) is caused by loss of emerin, a nuclear-membrane protein with roles in nuclear architecture, gene regulation and signaling. Phosphoproteomic studies have identified 13 sites of tyrosine phosphorylation in emerin. We validated one study, confirming that emerin is hyper-tyrosine-phosphorylated in Her2-overexpressing cells. We discovered that non-receptor tyrosine kinases Src and Abl each phosphorylate emerin and a related protein, LAP2beta, directly. Src phosphorylated emerin specifically at Y59, Y74 and Y95; the corresponding triple Y-to-F (;FFF') mutation reduced tyrosine phosphorylation by approximately 70% in vitro and in vivo. Substitutions that removed a single hydroxyl moiety either decreased (Y19F, Y34, Y161F) or increased (Y4F) emerin binding to BAF in cells. Y19F, Y34F, Y161F and the FFF mutant also reduced recombinant emerin binding to BAF from HeLa lysates, demonstrating the involvement of both LEM-domain and distal phosphorylatable tyrosines in binding BAF. We conclude that emerin function is regulated by multiple tyrosine kinases, including Her2, Src and Abl, two of which (Her2, Src) regulate striated muscle. These findings suggest roles for emerin as a downstream effector and ;signal integrator' for tyrosine kinase signaling pathway(s) at the nuclear envelope.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionAnimalsErb-b2 Receptor Tyrosine KinasesHeLa CellsHumansMass SpectrometryMembrane ProteinsMiceMolecular Sequence DataMutation, MissenseNIH 3T3 CellsNuclear EnvelopeNuclear ProteinsPhosphotyrosineProto-Oncogene Proteins c-ablemerinErb-b2 Receptor Tyrosine KinasesMembrane ProteinsNuclear ProteinsPhosphotyrosineProto-Oncogene Proteins c-ablsrc-Family Kinases

Identifiers

PMID19789182
PMCPMC2758807
OpenAlexW1990929843

What OpenQuestion holds

Textmetadata
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.