Evidence map›Paper›PMID 11818572›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2002

Uncoating ATPase Hsc70 is recruited by invariant chain and controls the size of endocytic compartments.

Cécile Lagaudrière-Gesbert, Sherri L Newmyer, Tone F Gregers, Oddmund Bakke, Hidde L Ploegh

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

22 citing papers in PubMed, 45 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. The Hsp70-Chaperone Machines in Bacteria.Frontiers in molecular biosciences · 2021
    Review
  6. Article
  7. Review
  8. Article
  9. Perspective: Reaches of chemical physics in biology.The Journal of chemical physics · 2013
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Hsp70 and its molecular role in nervous system diseases.Biochemistry research international · 2011
    Article
  16. Heat shock protein 70 (hsp70) as an emerging drug target.Journal of medicinal chemistry · 2010
    Review
  17. Review
  18. Article
  19. 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

5 authors at 2 institutions in 2 countries.

Cécile Lagaudrière-GesbertDepartment of Pathology, Harvard Medical School, Boston, MA 02115, USA.
Sherri L Newmyer
Tone F Gregers
Oddmund Bakke
Hidde L Ploegh
Scripps Research Institute · USHarvard University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Targeting of class II major histocompatibility complex molecules to endocytic compartments is mediated by their association with the invariant chain (Ii). Although the identity of certain sorting signals located in Ii's cytoplasmic tail is known, proteins that interact with Ii's cytoplasmic tail in living cells remain to be identified. Synthesis of a biotinylated trimeric Ii cytoplasmic tail allowed the retrieval of two proteins that interact with this domain. We identify one of them as the 70-kDa heat-shock cognate protein (hsc70), the uncoating ATPase of clathrin-coated vesicles, and the other as its mitochondrial homologue, the glucose-regulated protein grp75. Expression of Ii in COS cells results in the formation of large endocytic compartments. We observe extensive colocalization of hsc70 with Ii in these macrosomes. Expression of a dominant-negative (K71M) green fluorescent protein-tagged version of hsc70 counteracted the ability of Ii to modify the endocytic pathway, demonstrating an interaction in vivo of Ii with hsc70 as part of the machinery responsible for macrosome formation.

Indexed as

Amino Acid SequenceAnimalsAntibodiesAntigens, CDAntigens, Differentiation, B-LymphocyteCarrier ProteinsCell LineChlorocebus aethiopsCOS CellsEndocytosisGenes, ReporterGreen Fluorescent ProteinsHistocompatibility Antigens Class IIHLA-D AntigensHSC70 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsAntibodiesAntigens, CDAntigens, Differentiation, B-LymphocyteCarrier ProteinsGreen Fluorescent ProteinsHistocompatibility Antigens Class IIHLA-D AntigensHSC70 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsHSPA8 protein, humaninvariant chainLuminescent Proteins

Identifiers

PMID11818572
PMCPMC122222
OpenAlexW2033551445

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.