Evidence map›Paper›PMID 20335502›Full record

ArticleMolecular biology of the cell2010

Inside-out regulation of L1 conformation, integrin binding, proteolysis, and concomitant cell migration.

Maxine M Chen, Chia-Yao Lee, Hyuma A Leland, Grace Y Lin, Anthony M Montgomery, Steve Silletti

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.9field-weighted citation impact, top 28% 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

12 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. L1 coupling to ankyrin and the spectrin-actin cytoskeleton modulates ethanol inhibition of L1 adhesion and ethanol teratogenesis.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018
    Article
  6. Article
  7. Article
  8. Article
  9. Mitogen-activated protein kinase modulates ethanol inhibition of cell adhesion mediated by the L1 neural cell adhesion molecule.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  10. Article
  11. Modification of the L1-CAM carboxy-terminus in pancreatic adenocarcinoma cells.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2011
    Article
  12. 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

6 authors at 2 institutions in 1 country.

Maxine M ChenMoores Cancer Center and Department of Pathology, University of California, San Diego, La Jolla, CA 92093, USA.
Chia-Yao Lee
Hyuma A Leland
Grace Y Lin
Anthony M Montgomery
Steve Silletti
Moores Cancer CenterUniversity of California San Diego · US

Funding

VIRAL MALIGNANCYP30CA023100 · NCI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI DIANE M SIMEONE · 1985 to 2026
$124.9M
Traget-Driven Identification of Diagnostic Patterns in Pancreatic AdenocarcinomaR03CA130104 · NCI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI SILLETTI, STEVEN A · 2007 to 2008
$155k
Potential Role of pp72syk in Pancreatic AdenocarcinomaR03CA109956 · NCI · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI SILLETTI, STEVEN A · 2004 to 2005
$154k
NCI NIH HHS CA-109956NCI NIH HHS CA-130104NCI NIH HHS P30 CA023100NCI NIH HHS P30 CA-23100NCI NIH HHS R03 CA109956NCI NIH HHS R03 CA130104
6 · The paper itself

Abstract

Previous reports on the expression of the cell adhesion molecule L1 in pancreatic ductal adenocarcinoma (PDAC) cells range from absent to high. Our data demonstrate that L1 is expressed in poorly differentiated PDAC cells in situ and that threonine-1172 (T1172) in the L1 cytoplasmic domain exhibits steady-state saturated phosphorylation in PDAC cells in vitro and in situ. In vitro studies support roles for casein kinase II and PKC in this modification, consistent with our prior studies using recombinant proteins. Importantly, T1172 phosphorylation drives, or is associated with, a change in the extracellular structure of L1, consistent with a potential role in regulating the shift between the closed conformation and the open, multimerized conformation of L1. We further demonstrate that these distinct conformations exhibit differential binding to integrins alphavbeta3 and alphavbeta5 and that T1172 regulates cell migration in a matrix-specific manner and is required for a disintegrin and metalloproteinase-mediated shedding of the L1 ectodomain that has been shown to regulate cell migration. These data define a specific role for T1172 of L1 in regulating aspects of pancreatic adenocarcinoma cell phenotype and suggest the need for further studies to elucidate the specific ramifications of L1 expression and T1172 phosphorylation in the pathobiology of pancreatic cancer.

Indexed as

AnimalsCasein Kinase IICell MovementCricetinaeDisintegrinsHydrolysisIntegrin alphaVbeta3IntegrinsMolecular ConformationNeural Cell Adhesion Molecule L1PhosphorylationProtein BindingProtein Kinase CRecombinant ProteinsThreonineCasein Kinase IIDisintegrinsIntegrin alphaVbeta3IntegrinsNeural Cell Adhesion Molecule L1Protein Kinase CRecombinant ProteinsThreonine

Identifiers

PMID20335502
PMCPMC2869374
OpenAlexW2094940109

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.