Evidence map›Paper›PMID 19808674›Full record

ArticleThe Journal of biological chemistry2009

Mechanism for amyloid precursor-like protein 2 enhancement of major histocompatibility complex class I molecule degradation.

Amit Tuli, Mahak Sharma, Haley L Capek, Naava Naslavsky, Steve Caplan, Joyce C Solheim

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
0.7field-weighted citation impact, top 33% 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

23 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
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  3. Review
  4. Article
  5. Article
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  7. Bispecific antibody drug conjugates: Making 1+1>2.Acta pharmaceutica Sinica. B · 2024
    Review
  8. Exploring the next generation of antibody-drug conjugates.Nature reviews. Clinical oncology · 2024
    Review
  9. Review
  10. Observational
  11. Article
  12. Article
  13. APP, APLP2 and LRP1 interact with PCSK9 but are not required for PCSK9-mediated degradation of the LDLR in vivo.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2017
    Article
  14. Review
  15. Article
  16. Article
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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 1 institution in 1 country.

Amit TuliDepartment of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, Nebraska 68198-6805, USA.
Mahak Sharma
Haley L Capek
Naava Naslavsky
Steve Caplan
Joyce C Solheim
University of Nebraska Medical Center · US

Funding

UNMC/EPPLEY CANCER CENTER SUPPORT GRANTP30CA036727 · NCI · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI Apar Kishor Ganti · 1985 to 2026
$55.0M
Molecular Mechanisms Controlling Endocytic RecyclingR01GM074876 · NIGMS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI CAPLAN, STEVEN H · 2006 to 2015
$2.6M
ER PROTEINS EFFECT ON CLASS I MHC ASSEMBLYR01GM057428 · NIGMS · UNIVERSITY OF SOUTH DAKOTA · PI SOLHEIM, JOYCE C · 1998 to 2009
$1.5M
NCI NIH HHS P30 CA036727NCI NIH HHS P30CA036727NIGMS NIH HHS GM57428NIGMS NIH HHS GM74876NIGMS NIH HHS R01 GM057428NIGMS NIH HHS R01 GM074876
6 · The paper itself

Abstract

Earlier studies have demonstrated interaction of the murine major histocompatibility complex (MHC) class I molecule K(d) with amyloid precursor-like protein 2 (APLP2), a ubiquitously expressed member of the amyloid precursor protein family. Our current findings indicate that APLP2 is internalized in a clathrin-dependent manner, as shown by utilization of inhibitors of the clathrin pathway. Furthermore, we demonstrated that APLP2 and K(d) bind at the cell surface and are internalized together. The APLP2 cytoplasmic tail contains two overlapping consensus motifs for binding to the adaptor protein-2 complex, and mutation of a tyrosine shared by both motifs severely impaired APLP2 internalization and ability to promote K(d) endocytosis. Upon increased expression of wild type APLP2, K(d) molecules were predominantly directed to the lysosomes rather than recycled to the plasma membrane. These findings suggest a model in which APLP2 binds K(d) at the plasma membrane, facilitates uptake of K(d) in a clathrin-dependent manner, and routes the endocytosed K(d) to the lysosomal degradation pathway. Thus, APLP2 has a multistep trafficking function that influences the expression of major histocompatibility complex class I molecules at the plasma membrane.

Indexed as

Major Histocompatibility ComplexAmino Acid MotifsAmyloid beta-Protein PrecursorAntibodies, MonoclonalCell MembraneCytoplasmDynaminsEndocytosisGreen Fluorescent ProteinsHeLa CellsHumansLysosomesModels, BiologicalMutationNerve Tissue ProteinsProtein BindingAmyloid beta-Protein PrecursorAntibodies, MonoclonalAPLP2 protein, humanDynaminsGreen Fluorescent ProteinsNerve Tissue Proteins

Identifiers

PMID19808674
PMCPMC2797198
OpenAlexW1967040338

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.