Evidence map›Paper›PMID 16384915›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2006

Regulation of tyrosinase trafficking and processing by presenilins: partial loss of function by familial Alzheimer's disease mutation.

Runsheng Wang, Phuong Tang, Pei Wang, Raymond E Boissy, Hui Zheng

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
3.1field-weighted citation impact, top 9% 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

46 citing papers in PubMed, 91 citations in OpenAlex.

  1. Review
  2. Article
  3. Anti-Melanogenic Effects ofPlants (Basel, Switzerland) · 2023
    Article
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  9. Essential requirement for nicastrin in marginal zone and B-1 B cell development.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
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  19. Review
  20. The γ-secretase complex: from structure to function.Frontiers in cellular neuroscience · 2014
    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

5 authors at 2 institutions in 1 country.

Runsheng WangHuffington Center on Aging and Departments of Molecular and Human Genetics and Molecular and Cellular Biology, Baylor College of Medicine, Houston, TX 77030, USA.
Phuong Tang
Pei Wang
Raymond E Boissy
Hui Zheng
Baylor College of Medicine · USUniversity of Cincinnati Medical Center · US

Funding

Knockin Mouse Models of Alzheimers DiseaseR01AG020670 · NIA · BAYLOR COLLEGE OF MEDICINE · PI Hui Zheng · 2002 to 2026
$9.1M
CELL &MOLECULAR BIOLOGY OF AGINGT32AG000183 · NIA · BAYLOR COLLEGE OF MEDICINE · PI DONEHOWER, LAWRENCE A. · 1989 to 2015
$3.7M
Presenilins in tumorigenesis and neurodegenerationR01NS040039 · NINDS · BAYLOR COLLEGE OF MEDICINE · PI ZHENG, HUI · 2000 to 2007
$2.6M
Knockin mouse models of Alzheimer's DiseaseRF1AG020670 · NIA · BAYLOR COLLEGE OF MEDICINE · PI ZHENG, HUI · 2022 to 2022
$2.3M
ON THE ROLE OF THE HPS GENE PRODUCT IN MELANOCYTESR01AR045429 · NIAMS · UNIVERSITY OF CINCINNATI · PI BOISSY, RAYMOND E · 1999 to 2002
$629k
NIAMS NIH HHS AR45429NIAMS NIH HHS R01 AR045429NIA NIH HHS AG20670NIA NIH HHS R01 AG020670NIA NIH HHS RF1 AG020670NIA NIH HHS T32 AG000183NINDS NIH HHS NS40039NINDS NIH HHS R01 NS040039
6 · The paper itself

Abstract

Presenilins (PS) are required for gamma-secretase cleavage of multiple type I membrane proteins including the amyloid precursor protein and Notch and also have been implicated in regulating intracellular protein trafficking and turnover. Using genetic and pharmacological approaches, we reveal here a unique function of PS in the pigmentation of retinal pigment epithelium and epidermal melanocytes. PS deficiency leads to aberrant accumulation of tyrosinase (Tyr)-containing 50-nm post-Golgi vesicles that are normally destined to melanosomes. This trafficking is gamma-secretase-dependent, and abnormal localization of Tyr in the absence of PS is accompanied by the simultaneous accumulation of its C-terminal fragment. Furthermore, we show that the PS1M146V familial Alzheimer's disease mutation exhibits a partial loss-of-function in pigment synthesis. Our results identify Tyr and related proteins as physiological substrates of PS and link gamma-secretase activity with intracellular protein transport.

Indexed as

Alzheimer DiseaseAnimalsEmbryo, MammalianEpitheliumGolgi ApparatusMelaninsMelanocytesMembrane ProteinsMiceMice, Inbred C57BLMice, KnockoutMicroscopy, Electron, TransmissionMonophenol MonooxygenaseMutationPigmentationPresenilin-1MelaninsMembrane ProteinsMonophenol MonooxygenasePresenilin-1Presenilin-2Tyrosine

Identifiers

PMID16384915
PMCPMC1326180
OpenAlexW2068896977

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.