Evidence map›Paper›PMID 22582393›Full record

ArticleThe Journal of biological chemistry2012

Regulation of protein kinase C inactivation by Fas-associated protein with death domain.

Wei Cheng, Lu Wang, Rong Zhang, Pan Du, Bingya Yang, Hongqin Zhuang, Bo Tang, Chun Yao, Mei Yu, Yuxuan Wang and 6 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

15 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Article
  3. PKC and PKN in heart disease.Journal of molecular and cellular cardiology · 2019
    Review
  4. Article
  5. Article
  6. Article
  7. FADD is a key regulator of lipid metabolism.EMBO molecular medicine · 2016
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. 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

16 authors at 1 institution in 1 country.

Wei ChengState Key Laboratory of Pharmaceutical Biotechnology, Department of Biochemistry, Nanjing University, Nanjing 210093, China.
Lu Wang
Rong Zhang
Pan Du
Bingya Yang
Hongqin Zhuang
Bo Tang
Chun Yao
Mei Yu
Yuxuan Wang
Jing Zhang
Wu Yin
Jiahuang Li
Weijuan Zheng
Min Lu
Zichun Hua
Nanjing University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein kinase C (PKC) plays important roles in diverse cellular processes. PKC has been implicated in regulating Fas-associated protein with death domain (FADD), an important adaptor protein involved in regulating death receptor-mediated apoptosis. FADD also plays an important role in non-apoptosis processes. The functional interaction of PKC and FADD in non-apoptotic processes has not been examined. In this study, we show that FADD is involved in maintaining the phosphorylation of the turn motif and hydrophobic motif in the activated conventional PKC (cPKC). A phosphoryl-mimicking mutation (S191D) in FADD (FADD-D) abolished the function of FADD in the facilitation of the turn motif and hydrophobic motif dephosphorylation of cPKC, suggesting that phosphorylation of Ser-191 negatively regulates FADD. We show that FADD interacts with PP2A, which is a major phosphatase involved in dephosphorylation of activated cPKC and FADD deficiency abolished PP2A mediated dephosphorylation of cPKC. We show that FADD deficiency leads to increased stability and activity of cPKC, which, in turn, promotes cytoskeleton reorganization, cell motility, and chemotaxis. Collectively, these results reveal a novel function of FADD in a non-apoptotic process by modulating cPKC dephosphorylation, stability, and signaling termination.

Indexed as

Protein Processing, Post-TranslationalAmino Acid MotifsAnimalsCell MovementCytoskeletonEnzyme StabilityFas-Associated Death Domain ProteinHEK293 CellsHumansIsoenzymesMiceMice, KnockoutPhosphorylationProtein BindingProtein Kinase CProtein Phosphatase 2Fas-Associated Death Domain ProteinIsoenzymesProtein Kinase CProtein Phosphatase 2

Identifiers

PMID22582393
PMCPMC3406696
OpenAlexW2089513484

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.