Evidence map›Paper›PMID 12475967›Full record

ArticleMolecular biology of the cell2002

A novel transforming growth factor-beta receptor-interacting protein that is also a light chain of the motor protein dynein.

Qian Tang, Cory M Staub, Guofeng Gao, Qunyan Jin, Zhengke Wang, Wei Ding, Rosemarie E Aurigemma, Kathleen M Mulder

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

23 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Signaling Receptors for TGF-β Family Members.Cold Spring Harbor perspectives in biology · 2016
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. A dynein motor attachment complex regulates TGFß/Smad3 signaling.International journal of biological sciences · 2013
    Article
  12. Role of km23-1 in RhoA/actin-based cell migration.Biochemical and biophysical research communications · 2012
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. 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

8 authors at 1 institution in 1 country.

Qian TangDepartment of Pharmacology, Pennsylvania State University College of Medicine, Hershey, Pennsylvania 17033, USA.
Cory M Staub
Guofeng Gao
Qunyan Jin
Zhengke Wang
Wei Ding
Rosemarie E Aurigemma
Kathleen M Mulder
Pennsylvania State University · US

Funding

Mechanisms of TGF-Beta Production in Human Cancer CellsR01CA090765 · NCI · PENNSYLVANIA STATE UNIV HERSHEY MED CTR · PI MULDER, KATHLEEN M · 2001 to 2011
$3.1M
Role of TGFBeta in Microtubule DynamicsR01CA092889 · NCI · PENNSYLVANIA STATE UNIV HERSHEY MED CTR · PI MULDER, KATHLEEN M · 2001 to 2011
$2.9M
MECHANISMS OF TGFB SIGNALING IN COLON CARCINOMA CELLSR01CA051452 · NCI · PENNSYLVANIA STATE UNIV HERSHEY MED CTR · PI MULDER, KATHLEEN M · 1995 to 2001
$550k
ROLE OF MAPK'S AND TGFBETA MEDIATED CELLULAR RESPONSESR01CA054816 · NCI · PENNSYLVANIA STATE UNIV HERSHEY MED CTR · PI MULDER, KATHLEEN M · 1992 to 1999
–
INTRACELLULAR MEDIATORS OF TGF EFFECTSR01CA068444 · NCI · PENNSYLVANIA STATE UNIV HERSHEY MED CTR · PI MULDER, KATHLEEN M · 1996 to 1999
–
MECHANISMS OF TGF-B RESISTANCE IN COLON CARCINOMA CELLSR29CA051452 · NCI · PENNSYLVANIA STATE UNIV HERSHEY MED CTR · PI MULDER, KATHLEEN M · 1990 to 1994
–
NCI NIH HHS CA-51452NCI NIH HHS CA-54816NCI NIH HHS CA-68444NCI NIH HHS CA-90765NCI NIH HHS CA-92889NCI NIH HHS R01 CA090765NCI NIH HHS R01 CA092889
6 · The paper itself

Abstract

The phosphorylated, activated cytoplasmic domains of the transforming growth factor-beta (TGFbeta) receptors were used as probes to screen an expression library that was prepared from a highly TGFbeta-responsive intestinal epithelial cell line. One of the TGFbeta receptor-interacting proteins isolated was identified to be the mammalian homologue of the LC7 family (mLC7) of dynein light chains (DLCs). This 11-kDa cytoplasmic protein interacts with the TGFbeta receptor complex intracellularly and is phosphorylated on serine residues after ligand-receptor engagement. Forced expression of mLC7-1 induces specific TGFbeta responses, including an activation of Jun N-terminal kinase (JNK), a phosphorylation of c-Jun, and an inhibition of cell growth. Furthermore, TGFbeta induces the recruitment of mLC7-1 to the intermediate chain of dynein. A kinase-deficient form of TGFbeta RII prevents both mLC7-1 phosphorylation and interaction with the dynein intermediate chain (DIC). This is the first demonstration of a link between cytoplasmic dynein and a natural growth inhibitory cytokine. Furthermore, our results suggest that TGFbeta pathway components may use a motor protein light chain as a receptor for the recruitment and transport of specific cargo along microtublules.

Indexed as

Drosophila ProteinsJNK Mitogen-Activated Protein KinasesAnimalsCarrier ProteinsCell LineCOS CellsCytoplasmDogsDyneinsGene LibraryGlutathione TransferaseHumansMAP Kinase Kinase 4Mitogen-Activated Protein Kinase KinasesPhosphorylationPlasmidsCarrier ProteinsDrosophila ProteinsDyneinsGlutathione TransferaseJNK Mitogen-Activated Protein KinasesMAP Kinase Kinase 4Mitogen-Activated Protein Kinase KinasesReceptors, Transforming Growth Factor betaTransforming Growth Factor beta

Identifiers

PMID12475967
PMCPMC138648
OpenAlexW2150645859

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.