Evidence map›Paper›PMID 18505677›Full record

ArticleBiochemical and biophysical research communications2008

Hsp70 associates with Rictor and is required for mTORC2 formation and activity.

Jheralyn Martin, Janine Masri, Andrew Bernath, Robert N Nishimura, Joseph Gera

Open access · greenAbstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2008. 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
3.2field-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

42 citing papers in PubMed, 79 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. 7,7-Bis(3-Indolyl)-Journal of microbiology and biotechnology · 2025
    Article
  5. Article
  6. Review
  7. Molecular Network Approach RevealsInternational journal of molecular sciences · 2021
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. mTOR function and therapeutic targeting in breast cancer.American journal of cancer research · 2017
    Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. Where is mTOR and what is it doing there?The Journal of cell biology · 2013
    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

5 authors at 2 institutions in 1 country.

Jheralyn MartinDepartment of Research & Development, Greater Los Angeles Veterans Affairs Healthcare System, 16111 Plummer Street (151), Building 1, Room C111A, Los Angeles, CA 91343, USA.
Janine Masri
Andrew Bernath
Robert N Nishimura
Joseph Gera
VA Greater Los Angeles Healthcare System · USUniversity of California, Los Angeles · US

Funding

Mechanisms of AKT-dependent sensitivity to rapamycinR01CA109312 · NCI · SEPULVEDA RESEARCH CORPORATION · PI GERA, JOSEPH F · 2005 to 2012
$1.6M
NCI NIH HHS CA109312NCI NIH HHS R01 CA109312
6 · The paper itself

Abstract

mTORC2 is a multiprotein kinase composed of mTOR, mLST8, PRR5, mSIN1 and Rictor. The complex is insensitive to rapamycin and has demonstrated functions controlling cell growth, motility, invasion and cytoskeletal assembly. mTORC2 is the major hydrophobic domain kinase which renders Akt fully active via phosphorylation on serine 473. We isolated Hsp70 as a putative Rictor interacting protein in a yeast two-hybrid assay and confirmed this interaction via co-immunoprecipitation and colocalization experiments. In cells expressing an antisense RNA targeting Hsp70, mTORC2 formation and activity were impaired. Moreover, in cells lacking Hsp70 expression, mTORC2 activity was inhibited following heat shock while controls demonstrated increased mTORC2 activity. These differential effects on mTORC2 activity were specific, in that mTORC1 did not demonstrate Hsp70-dependent alterations under these conditions. These data suggest that Hsp70 is a component of mTORC2 and is required for proper assembly and activity of the kinase both constitutively and following heat shock.

Indexed as

Amino Acid SequenceCarrier ProteinsCell LineDNA Mutational AnalysisDown-RegulationHSP70 Heat-Shock ProteinsHumansImmunoprecipitationMolecular Sequence DataMultienzyme ComplexesProto-Oncogene Proteins c-aktRapamycin-Insensitive Companion of mTOR ProteinRNA, AntisenseSignal TransductionTwo-Hybrid System TechniquesCarrier ProteinsHSP70 Heat-Shock ProteinsMultienzyme ComplexesProto-Oncogene Proteins c-aktRapamycin-Insensitive Companion of mTOR ProteinRICTOR protein, humanRNA, Antisense

Identifiers

PMID18505677
PMCPMC2512964
OpenAlexW1998322858

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.