Evidence map›Paper›PMID 14561217›Full record

ArticleThe Biochemical journal2004

Localization of dynein light chains 1 and 2 and their pro-apoptotic ligands.

Catherine L Day, Hamsa Puthalakath, Gretchen Skea, Andreas Strasser, Igor Barsukov, Lu-Yun Lian, David C S Huang, Mark G Hinds

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

32 citing papers in PubMed, 74 citations in OpenAlex.

  1. Review
  2. Article
  3. DYNLT1 gene expression is downregulated in whole blood of patients at different Huntington's disease stages.Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology · 2021
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Intrinsically disordered proteins in bcl-2 regulated apoptosis.International journal of molecular sciences · 2010
    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

8 authors at 2 institutions in 2 countries.

Catherine L DayDepartment of Biochemistry, University of Otago, Dunedin, New Zealand.
Hamsa Puthalakath
Gretchen Skea
Andreas Strasser
Igor Barsukov
Lu-Yun Lian
David C S Huang
Mark G Hinds
Walter and Eliza Hall Institute of Medical Research · AUUniversity of Otago · NZ

Funding

MECHANISMS IN THE REGULATION OF APOPTOSISR01CA080188 · NCI · WALTER AND ELIZA HALL INST MEDICAL RES · PI ADAMS, JERRY M · 1999 to 2006
$1.1M
NCI NIH HHS CA 80188
6 · The paper itself

Abstract

The dynein and myosin V motor complexes are multi-protein structures that function to transport molecules and organelles within the cell. DLC (dynein light-chain) proteins, found as components of both dynein and myosin V motor complexes, connect the complexes to their cargoes. One of the roles of these motor complexes is to selectively sequester the pro-apoptotic 'BH3-only' (Bcl-2 homology 3-only) proteins, Bim (Bcl-2-interacting mediator of cell death) and Bmf (Bcl-2-modifying factor), and so regulate their cell death-inducing function. In vivo DLC2 is found exclusively as a component of the myosin V motor complex and Bmf binds DLC2 selectively. On the other hand, Bim interacts with DLC1 (LC8), an integral component of the dynein motor complex. The two DLCs share 93% sequence identity yet show unambiguous in vivo specificity for their respective BH3-only ligands. To investigate this specificity the three-dimensional solution structure of DLC2 was elucidated using NMR spectroscopy. In vitro structural and mutagenesis studies show that Bmf and Bim have identical binding characteristics to recombinant DLC2 or DLC1. Thus the selectivity shown by Bmf and Bim for binding DLC1 or DLC2, respectively, does not reside in their DLC-binding domains. Remarkably, mutational analysis of DLC1 and DLC2 indicates that a single surface residue (residue 41) determines the specific localization of DLCs with their respective motor complexes. These results suggest a molecular mechanism for the specific compartmentalization of DLCs and their pro-apoptotic cargoes and implicate other protein(s) in defining the specificity between the cargoes and the DLC proteins.

Indexed as

Adaptor Proteins, Signal TransducingMembrane ProteinsProto-Oncogene ProteinsAmino AcidsAmino Acid SequenceAnimalsApoptosisApoptosis Regulatory ProteinsBcl-2-Like Protein 11Carrier ProteinsCell LineCloning, MolecularConserved SequenceDyneinsHumansKidneyAdaptor Proteins, Signal TransducingAmino AcidsApoptosis Regulatory ProteinsBCL2L11 protein, humanBcl2l11 protein, mouseBcl-2-Like Protein 11BMF protein, humanBmf protein, mouseCarrier ProteinsDyneinsLigandsMacromolecular SubstancesMembrane ProteinsMyosin Type VPeptidesProtein SubunitsProto-Oncogene Proteins

Identifiers

PMID14561217
PMCPMC1223895
OpenAlexW2157468803

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.