Evidence map›Paper›PMID 15772161›Full record

ArticleMolecular biology of the cell2005

CART: an Hrs/actinin-4/BERP/myosin V protein complex required for efficient receptor recycling.

Qing Yan, Wei Sun, Pekka Kujala, Yasmin Lotfi, Thomas A Vida, Andrew J Bean

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

60 citing papers in PubMed, 126 citations in OpenAlex.

  1. Article
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  5. Molecular Mechanisms of AMPA Receptor Trafficking in the Nervous System.International journal of molecular sciences · 2023
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  8. Article
  9. Article
  10. The journal of venomous animals and toxins including tropical diseases · 2021
    Article
  11. Ubiquitination of TLR3 by TRIM3 signals its ESCRT-mediated trafficking to the endolysosomes for innate antiviral response.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  12. Spatial control of membrane traffic in neuronal dendrites.Molecular and cellular neurosciences · 2020
    Review
  13. Journal of cell science · 2020
    Article
  14. The many functions of ESCRTs.Nature reviews. Molecular cell biology · 2020
    Review
  15. Roles of Myosin-Mediated Membrane Trafficking in TGF-β Signaling.International journal of molecular sciences · 2019
    Review
  16. Article
  17. Article
  18. Review
  19. The Autoimmune Disorder Susceptibility GeneFrontiers in immunology · 2019
    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

6 authors at 2 institutions in 2 countries.

Qing YanDepartment of Neurobiology and Anatomy, University of Texas Medical School, Houston, TX 77030, USA.
Wei Sun
Pekka Kujala
Yasmin Lotfi
Thomas A Vida
Andrew J Bean
The University of Texas at Austin · USThe Netherlands Cancer Institute · NL

Funding

MOLECULAR MECHANISMS OF NEUROTRANSMITTER SECRETIONR01MH058920 · NIMH · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI BEAN, ANDREW J · 1998 to 2010
$2.9M
MECHANISMS OF ENDOSOME TO LYSOSOME TRANSPORT IN YEASTR01GM052092 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI VIDA, THOMAS A · 1995 to 2005
$947k
NIGMS NIH HHS GM-052092NIGMS NIH HHS R01 GM052092NIMH NIH HHS MH-58920NIMH NIH HHS R01 MH058920
6 · The paper itself

Abstract

Altering the number of surface receptors can rapidly modulate cellular responses to extracellular signals. Some receptors, like the transferrin receptor (TfR), are constitutively internalized and recycled to the plasma membrane. Other receptors, like the epidermal growth factor receptor (EGFR), are internalized after ligand binding and then ultimately degraded in the lysosome. Routing internalized receptors to different destinations suggests that distinct molecular mechanisms may direct their movement. Here, we report that the endosome-associated protein hrs is a subunit of a protein complex containing actinin-4, BERP, and myosin V that is necessary for efficient TfR recycling but not for EGFR degradation. The hrs/actinin-4/BERP/myosin V (CART [cytoskeleton-associated recycling or transport]) complex assembles in a linear manner and interrupting binding of any member to its neighbor produces an inhibition of transferrin recycling rate. Disrupting the CART complex results in shunting receptors to a slower recycling pathway that involves the recycling endosome. The novel CART complex may provide a molecular mechanism for the actin-dependence of rapid recycling of constitutively recycled plasma membrane receptors.

Indexed as

ActininBase SequenceCarrier ProteinsCytoskeletonDNAEndosomal Sorting Complexes Required for TransportEndosomesErbB ReceptorsHeLa CellsHumansIn Vitro TechniquesMicrofilament ProteinsMicroscopy, ImmunoelectronModels, BiologicalMultiprotein ComplexesMyosin Type VActininACTN4 protein, humanCarrier ProteinsDNAEndosomal Sorting Complexes Required for TransportErbB Receptorshepatocyte growth factor-regulated tyrosine kinase substrateMicrofilament ProteinsMultiprotein ComplexesMyosin Type VPhosphoproteinsReceptors, Cell SurfaceReceptors, TransferrinRecombinant ProteinsTRIM3 protein, human

Identifiers

PMID15772161
PMCPMC1087250
OpenAlexW2110616259

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.