Evidence map›Paper›PMID 23530051›Full record

ArticleThe Journal of biological chemistry2013

Serines in the intracellular tail of podoplanin (PDPN) regulate cell motility.

Harini Krishnan, Jhon A Ochoa-Alvarez, Yongquan Shen, Evan Nevel, Meenakshi Lakshminarayanan, Mary C Williams, Maria I Ramirez, W Todd Miller, Gary S Goldberg

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. 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
3.8field-weighted citation impact, top 6% 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, 65 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Podoplanin in Inflammation and Cancer.International journal of molecular sciences · 2019
    Review
  19. Review
  20. 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

9 authors at 2 institutions in 1 country.

Harini KrishnanGraduate School of Biomedical Sciences and Department of Molecular Biology, School of Osteopathic Medicine, University of Medicine and Dentistry of New Jersey, Stratford, New Jersey 08084, USA.
Jhon A Ochoa-Alvarez
Yongquan Shen
Evan Nevel
Meenakshi Lakshminarayanan
Mary C Williams
Maria I Ramirez
W Todd Miller
Gary S Goldberg
Boston University · USStony Brook University · US

Funding

SUSTRATE SPECIFICITY OF NONRECEPTOR TYROSINE KINASER01CA058530 · NCI · STATE UNIVERSITY NEW YORK STONY BROOK · PI MILLER, W TODD · 1999 to 2018
$3.7M
LUNG ALVEOLAR TYPE 1 CELL MORPHOGENESISR01HL083034 · NHLBI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI RAMIREZ, MARIA ISABEL · 2006 to 2010
$2.3M
SUBSTRATE SPECIFICITY OF NONRECEPTOR TYROSINE KINASESR29CA058530 · NCI · STATE UNIVERSITY NEW YORK STONY BROOK · PI MILLER, W TODD · 1993 to 1997
–
NCI NIH HHS CA58530NCI NIH HHS R01 CA058530NHLBI NIH HHS HL083034NHLBI NIH HHS R01 HL083034
6 · The paper itself

Abstract

Podoplanin (PDPN) is a transmembrane receptor that affects the activities of Rho, ezrin, and other proteins to promote tumor cell motility, invasion, and metastasis. PDPN is found in many types of cancer and may serve as a tumor biomarker and chemotherapeutic target. The intracellular region of PDPN contains only two serines, and these are conserved in mammals including mice and humans. We generated cells from the embryos of homozygous null Pdpn knock-out mice to investigate the relevance of these serines to cell growth and migration on a clear (PDPN-free) background. We report here that one or both of these serines can be phosphorylated by PKA (protein kinase A). We also report that conversion of these serines to nonphosphorylatable alanine residues enhances cell migration, whereas their conversion to phosphomimetic aspartate residues decreases cell migration. These results indicate that PKA can phosphorylate PDPN to decrease cell migration. In addition, we report that PDPN expression in fibroblasts causes them to facilitate the motility and viability of neighboring melanoma cells in coculture. These findings shed new light on how PDPN promotes cell motility, its role in tumorigenesis, and its utility as a functionally relevant biomarker and chemotherapeutic target.

Indexed as

Cell MovementAnimalsCell Line, TumorCoculture TechniquesCyclic AMP-Dependent Protein KinasesFibroblastsMelanomaMembrane GlycoproteinsMiceMice, KnockoutNeoplasm ProteinsPhosphorylationPodoplaninSerineCyclic AMP-Dependent Protein KinasesMembrane GlycoproteinsNeoplasm ProteinsPdpn protein, mousePodoplaninSerine

Identifiers

PMID23530051
PMCPMC3636905
OpenAlexW2033001098

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.