Evidence map›Paper›PMID 20919742›Full record

ArticleJournal of proteome research2010

LDL receptor-related protein 1 regulates the abundance of diverse cell-signaling proteins in the plasma membrane proteome.

Alban Gaultier, Gabriel Simon, Sherry Niessen, Melissa Dix, Shinako Takimoto, Benjamin F Cravatt, Steven L Gonias

Abstract read
In one paragraph

Article in Journal of proteome research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.9field-weighted citation impact, top 30% 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

16 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. 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

7 authors at 2 institutions in 1 country.

Alban GaultierDepartment of Pathology, University of California San Diego School of Medicine, La Jolla, California 92093, United States.
Gabriel Simon
Sherry Niessen
Melissa Dix
Shinako Takimoto
Benjamin F Cravatt
Steven L Gonias
Scripps Research Institute · USUniversity of California, San Diego · US

Funding

REGULATION OF UROKINASE RECEPTOR ACTIVITY BY LRPR01HL060551 · NHLBI · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI GONIAS, STEVEN L. · 1999 to 2014
$4.0M
Chemical Approaches for Activity-Based ProteomicsR37CA087660 · NCI · SCRIPPS RESEARCH INSTITUTE, THE · PI CRAVATT, BENJAMIN F · 2009 to 2018
$3.1M
CHEMICAL APPROACHES FOR ACTIVITY BASED PROTEOMICSR01CA087660 · NCI · SCRIPPS RESEARCH INSTITUTE, THE · PI CRAVATT, BENJAMIN F · 2000 to 2008
$2.8M
Enzymes That Regulate Fatty Acid Amide Function In VivoR01DA015197 · NIDA · SCRIPPS RESEARCH INSTITUTE, THE · PI CRAVATT, BENJAMIN F · 2002 to 2009
$2.5M
Alpha2-macroglobulin in peripheral nerve injuryR01NS054671 · NINDS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI GONIAS, STEVEN L. · 2007 to 2011
$1.7M
NCI NIH HHS R01 CA087660NCI NIH HHS R37 CA087660NHLBI NIH HHS R01 HL-060551NHLBI NIH HHS R01 HL060551NIDA NIH HHS R01 DA015197NINDS NIH HHS NS-054671NINDS NIH HHS R01 NS054671
6 · The paper itself

Abstract

LDL receptor-related protein 1 (LRP1) is an endocytic receptor, reported to regulate the abundance of other receptors in the plasma membrane, including uPAR and tissue factor. The goal of this study was to identify novel plasma membrane proteins, involved in cell-signaling, that are regulated by LRP1. Membrane protein ectodomains were prepared from RAW 264.7 cells in which LRP1 was silenced and control cells using protease K. Peptides were identified by LC-MS/MS. By analysis of spectral counts, 31 transmembrane and secreted proteins were regulated in abundance at least 2-fold when LRP1 was silenced. Validation studies confirmed that semaphorin4D (Sema4D), plexin domain-containing protein-1 (Plxdc1), and neuropilin-1 were more abundant in the membranes of LRP1 gene-silenced cells. Regulation of Plxdc1 by LRP1 was confirmed in CHO cells, as a second model system. Plxdc1 coimmunoprecipitated with LRP1 from extracts of RAW 264.7 cells and mouse liver. Although Sema4D did not coimmunoprecipitate with LRP1, the cell-surface level of Sema4D was increased by RAP, which binds to LRP1 and inhibits binding of other ligands. These studies identify Plxdc1, Sema4D, and neuropilin-1 as novel LRP1-regulated cell-signaling proteins. Overall, LRP1 emerges as a generalized regulator of the plasma membrane proteome.

Indexed as

AnimalsCell LineCell MembraneCHO CellsChromatography, LiquidCricetinaeCricetulusImmunoblottingImmunoprecipitationLiverLow Density Lipoprotein Receptor-Related Protein-1MacrophagesMass SpectrometryMembrane MicrodomainsMembrane ProteinsMiceLow Density Lipoprotein Receptor-Related Protein-1Lrp1 protein, mouseMembrane ProteinsNerve Tissue ProteinsNeuropilin-1Plxna1 protein, mouseReceptors, Cell SurfaceReceptors, LDLSema4d protein, mouseSemaphorinsTumor Suppressor Proteins

Identifiers

PMID20919742
PMCPMC2997161
OpenAlexW1991827997

What OpenQuestion holds

Textmetadata
LicenceTDM
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.