Evidence map›Paper›PMID 21650223›Full record

ArticleBiochemistry2011

Protein interactions among Fe65, the low-density lipoprotein receptor-related protein, and the amyloid precursor protein.

Melinda M Mulvihill, Miklos Guttman, Elizabeth A Komives

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.9field-weighted citation impact, top 28% 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

8 citing papers in PubMed, 8 citations in OpenAlex.

  1. Review
  2. Functional importance of stripping in NFκB signaling revealed by a stripping-impaired IκBα mutant.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  3. Article
  4. Article
  5. FE65 interacts with ADP-ribosylation factor 6 to promote neurite outgrowth.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2014
    Article
  6. Article
  7. Review
  8. 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

3 authors at 1 institution in 1 country.

Melinda M MulvihillDepartment of Chemistry and Biochemistry, University of California, San Diego, La Jolla, California 92093-0378, United States.
Miklos Guttman
Elizabeth A Komives
University of California, San Diego · US

Funding

HEMOGLOBIN AND BLOOD PROTEIN CHEMISTRYT32DK007233 · NIDDK · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI KOMIVES, ELIZABETH A. · 1986 to 2012
$4.6M
Directed Proteomics of Alzheimer's Related ProteinsR01AG025343 · NIA · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI KOMIVES, ELIZABETH A. · 2004 to 2008
$1.5M
NIA NIH HHS R01 AG025343NIA NIH HHS R01-AG025343NIDDK NIH HHS 5T32DK007233NIDDK NIH HHS T32 DK007233
6 · The paper itself

Abstract

The adapter protein Fe65 has been proposed to be the link between the intracellular domains of the amyloid precursor protein, APP (AICD), and the low-density lipoprotein receptor-related protein (LRP-CT). Functional linkage between these two proteins has been established, and mutations within LRP-CT affect the amount of Aβ produced from APP. Previous work showed that AICD binds to protein interaction domain 2 (PID2) of Fe65. Although the structure of PID1 was determined recently, all attempts to demonstrate LRP-CT binding to this domain failed. We used biophysical experiments and binding studies to investigate the binding among these three proteins. Full-length Fe65 bound more weakly to AICD than did N-terminally truncated forms; however, the intramolecular domain-domain interactions that had been proposed to inhibit binding could not be observed using amide H-D exchange. Surprisingly, when LRP-CT is phosphorylated at Tyr4507, it bound to Fe65 PID1 despite the fact that this domain belongs to the Dab-like subclass of PIDs that are not supposed to be phosphorylation-dependent. Mutation of a critical arginine abolished binding, providing further proof of the phosphorylation dependence. Fe65 PID1 thus provides a link between the Dab-like class and the IRS-like class of PIDs and is the first Dab-like family member to show phosphorylation-dependent binding.

Indexed as

Amino Acid SequenceAmyloid beta-Protein PrecursorBinding, CompetitiveCrystallography, X-RayHumansMolecular Sequence DataNerve Tissue ProteinsNuclear ProteinsPhosphorylationPhosphotyrosineProtein BindingProtein Interaction MappingProtein Structure, TertiaryReceptors, LDLAmyloid beta-Protein PrecursorAPBB1 protein, humanAPLP1 protein, humanNerve Tissue ProteinsNuclear ProteinsPhosphotyrosineReceptors, LDL

Identifiers

PMID21650223
PMCPMC3139566
OpenAlexW61184661

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.