Evidence map›Paper›PMID 9571248›Full record

ArticleMolecular biology of the cell1998

Endocytic clathrin-coated pit formation is independent of receptor internalization signal levels.

F Santini, M S Marks, J H Keen

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

19 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Membrane Trafficking in Neuronal Development: Ins and Outs of Neural Connectivity.International review of cell and molecular biology · 2016
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. G protein-coupled receptor sorting to endosomes and lysosomes.Annual review of pharmacology and toxicology · 2008
    Review
  11. The role of cargo proteins in GGA recruitment.Traffic (Copenhagen, Denmark) · 2007
    Article
  12. Article
  13. Clathrin-dependent endocytosis.The Biochemical journal · 2004
    Review
  14. Article
  15. Article
  16. Article
  17. Acute cholesterol depletion inhibits clathrin-coated pit budding.Proceedings of the National Academy of Sciences of the United States of America · 1999
    Article
  18. Article
  19. Molecular aspects of the endocytic pathway.The Biochemical journal · 1998
    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

3 authors at 2 institutions in 1 country.

F SantiniKimmel Cancer Institute and the Departments of Microbiology and Immunology and of Biochemistry and Molecular Pharmacology, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, USA.
M S Marks
J H Keen
Thomas Jefferson University · USUniversity of Pennsylvania · US

Funding

TRAINING PROGRAMS IN MOLECULAR GENETICS OF CANCERT32CA009678 · NCI · THOMAS JEFFERSON UNIVERSITY · PI BUCHBERG, ARTHUR M. · 1992 to 2008
$2.3M
CLATHRIN AND MEMBRANE FUNCTIONR01GM028526 · NIGMS · THOMAS JEFFERSON UNIVERSITY · PI KEEN, JAMES H · 1985 to 2004
$1.2M
NCI NIH HHS 5-T32-CA09678NCI NIH HHS T32 CA009678NIGMS NIH HHS GM-28526NIGMS NIH HHS R01 GM028526
6 · The paper itself

Abstract

The mechanisms responsible for coated pit formation in cells remain unknown, but indirect evidence has argued both for and against a critical role of receptor cytoplasmic domains in the process. If the endocytic motifs of receptors are responsible for recruiting AP2 to the plasma membrane, thereby driving coated pit formation, then the level of constitutively internalized receptors at the membrane would be expected to govern the steady-state level of coated pits in cells. Here we directly test this hypothesis for broad classes of receptors containing three distinct constitutive internalization signals. Chimeric proteins consisting of an integral membrane reporter protein (Tac) coupled to cytoplasmic domains bearing tyrosine-, di-leucine-, or acidic cluster/casein kinase II-based internalization signals were overexpressed to levels that saturated the internalization pathway. Quantitative confocal immunofluorescence microscopy indicated that the number of plasma membrane clathrin-coated pits and the concentration of their structural components were invariant when comparing cells expressing saturating levels of the chimeric receptors to nonexpressing cells or to cells expressing only the Tac reporter lacking cytoplasmic internalization signals. Biochemical analysis showed that the distribution of coat proteins between assembled coated pits and soluble pools was also not altered by receptor overexpression. Finally, the cellular localizations of AP2 and AP1 were similarly unaffected. These results provide a clear indication that receptor endocytic signals do not determine coated pit levels by directly recruiting AP2 molecules. Rather, the findings support a model in which coated pit formation proceeds through recruitment and activation of AP2, likely through a limited number of regulated docking sites that act independently of endocytic signals.

Indexed as

EndocytosisSignal TransductionAdaptor Protein Complex 1Adaptor Protein Complex 2Adaptor Protein Complex alpha SubunitsAdaptor Proteins, Vesicular TransportAmino Acid SequenceAnimalsCasein Kinase IICell FractionationCell LineCell MembraneClathrinCoated Pits, Cell-MembraneHeLa CellsHumansAdaptor Protein Complex 1Adaptor Protein Complex 2Adaptor Protein Complex alpha SubunitsAdaptor Proteins, Vesicular TransportCasein Kinase IIClathrinLeucineMembrane ProteinsProtein Serine-Threonine KinasesReceptors, Cell SurfaceTyrosine

Identifiers

PMID9571248
PMCPMC25339
OpenAlexW2054977851

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.