Evidence map›Paper›PMID 26023881›Full record

ArticleScientific reports2015

Structural transition in Bcl-xL and its potential association with mitochondrial calcium ion transport.

Sreekanth Rajan, Minjoo Choi, Quoc Toan Nguyen, Hong Ye, Wei Liu, Hui Ting Toh, CongBao Kang, Neelagandan Kamariah, Chi Li, Huiya Huang and 4 more

Abstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
–field-weighted citation impact
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

11 citing papers in PubMed.

  1. Article
  2. ATP Synthase KFunction (Oxford, England) · 2022
    Article
  3. Article
  4. Review
  5. The Structural Biology of Bcl-xInternational journal of molecular sciences · 2019
    Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. 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

14 authors.

Sreekanth RajanSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551.
Minjoo ChoiSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551.
Quoc Toan NguyenSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551.
Hong YeSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551.
Wei LiuSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551.
Hui Ting TohSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551.
CongBao KangExperimental Therapeutics Centre, Agency for Science, Technology and Research (A*STAR), Singapore 138669.
Neelagandan KamariahBioinformatics Institute, Agency for Science, Technology and Research (A*STAR), 30 Biopolis Street, Singapore 138671.
Chi LiMolecular Targets Program, James Graham Brown Center and Department of Medicine, Pharmacology and Toxicology, University of Louisville, Louisville, KY 40202, USA.
Huiya HuangDepartment of Physiology and Biophysics, Rosalind Franklin University of Medicine and Science, 3333 Green Bay Road, North Chicago, IL 60064, USA.
Carl WhiteDepartment of Physiology and Biophysics, Rosalind Franklin University of Medicine and Science, 3333 Green Bay Road, North Chicago, IL 60064, USA.
Kwanghee BaekDepartment of Genetic Engineering, College of Life Sciences, Kyung Hee University, Yongin-si, Gyeonggi-do, 446-701, Republic of Korea.
Gerhard Grüber1] School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551 [2] Bioinformatics Institute, Agency for Science, Technology and Research (A*STAR), 30 Biopolis Street, Singapore 138671.
Ho Sup Yoon1] School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551 [2] Department of Genetic Engineering, College of Life Sciences, Kyung Hee University, Yongin-si, Gyeonggi-do, 446-701, Republic of Korea.

Funding

Activating Bax as a therapeutic strategy for lung cancerR01CA175003 · NCI · UNIVERSITY OF LOUISVILLE · PI LI, CHI · 2013 to 2017
$1.5M
NCI NIH HHS R01 CA175003
6 · The paper itself

Abstract

Bcl-2 family proteins are key regulators for cellular homeostasis in response to apoptotic stimuli. Bcl-xL, an antiapoptotic Bcl-2 family member, undergoes conformational transitions, which leads to two conformational states: the cytoplasmic and membrane-bound. Here we present the crystal and small-angle X-ray scattering (SAXS) structures of Bcl-xL treated with the mild detergent n-Octyl β-D-Maltoside (OM). The detergent-treated Bcl-xL forms a dimer through three-dimensional domain swapping (3DDS) by swapping helices α6-α8 between two monomers. Unlike Bax, a proapoptotic member of the Bcl-2 family, Bcl-xL is not converted to 3DDS homodimer upon binding BH3 peptides and ABT-737, a BH3 mimetic drug. We also designed Bcl-xL mutants which cannot dimerize and show that these mutants reduced mitochondrial calcium uptake in MEF cells. This illustrates the structural plasticity in Bcl-xL providing hints toward the probable molecular mechanism for Bcl-xL to play a regulatory role in mitochondrial calcium ion transport.

Indexed as

Molecular ConformationAnimalsbcl-2-Associated X Proteinbcl-X ProteinCalciumIon TransportMiceMitochondriaModels, MolecularMutationPeptide FragmentsProtein BindingProtein Interaction Domains and MotifsProtein MultimerizationProto-Oncogene ProteinsScattering, Small AngleBax protein (53-86)bcl-2-Associated X Proteinbcl-X ProteinCalciumPeptide FragmentsProto-Oncogene Proteins

Identifiers

PMID26023881
PMCPMC4448555

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.