Evidence map›Paper›PMID 19624486›Full record

ArticleTraffic (Copenhagen, Denmark)2009

ESCRT-I function is required for Tyrp1 transport from early endosomes to the melanosome limiting membrane.

Steven T Truschel, Sabrina Simoes, Subba Rao Gangi Setty, Dawn C Harper, Danièle Tenza, Penelope C Thomas, Kathryn E Herman, Sara D Sackett, David C Cowan, Alexander C Theos and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.5field-weighted citation impact, top 12% 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

30 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Melanosome Biogenesis in the Pigmentation of Mammalian Skin.Integrative and comparative biology · 2021
    Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Melanosome transfer: it is best to give and receive.Current opinion in cell biology · 2014
    Review
  16. Article
  17. Review
  18. Review
  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

12 authors at 4 institutions in 2 countries.

Steven T TruschelDepartment of Pathology and Laboratory Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.
Sabrina Simoes
Subba Rao Gangi Setty
Dawn C Harper
Danièle Tenza
Penelope C Thomas
Kathryn E Herman
Sara D Sackett
David C Cowan
Alexander C Theos
Graça Raposo
Michael S Marks
University of Pennsylvania · USInstitut Curie · FRCentre National de la Recherche Scientifique · FRGeorgetown University · US

Funding

IMMUNOBIOLOGY OF NORMAL AND NEOPLASTIC LYMPHOCYTEST32CA009140 · NCI · UNIVERSITY OF PENNSYLVANIA · PI Malay Haldar, WARREN S PEAR · 1985 to 2026
$16.1M
Hermansky Pudlak Syndrome &melanosome formationR01EY015625 · NEI · UNIVERSITY OF PENNSYLVANIA · PI Michael S Marks · 2004 to 2026
$9.2M
NCI NIH HHS T32 CA009140NCI NIH HHS T32-CA-009140NEI NIH HHS R01 EY015625
6 · The paper itself

Abstract

Melanosomes are lysosome-related organelles that coexist with lysosomes within melanocytes. The pathways by which melanosomal proteins are diverted from endocytic organelles toward melanosomes are incompletely defined. In melanocytes from mouse models of Hermansky-Pudlak syndrome that lack BLOC-1, melanosomal proteins such as tyrosinase-related protein 1 (Tyrp1) accumulate in early endosomes. Whether this accumulation represents an anomalous pathway or an arrested normal intermediate in melanosome protein trafficking is not clear. Here, we show that early endosomes are requisite intermediates in the trafficking of Tyrp1 from the Golgi to late stage melanosomes in normal melanocytic cells. Kinetic analyses show that very little newly synthesized Tyrp1 traverses the cell surface and that internalized Tyrp1 is inefficiently sorted to melanosomes. Nevertheless, nearly all Tyrp1 traverse early endosomes since it becomes trapped within enlarged, modified endosomes upon overexpression of Hrs. Although Tyrp1 localization is not affected by Hrs depletion, depletion of the ESCRT-I component, Tsg101, or inhibition of ESCRT function by dominant-negative approaches results in a dramatic redistribution of Tyrp1 to aberrant endosomal membranes that are largely distinct from those harboring traditional ESCRT-dependent, ubiquitylated cargoes such as MART-1. The lysosomal protein content of some of these membranes and the lack of Tyrp1 recycling to the plasma membrane in Tsg101-depleted cells suggests that ESCRT-I functions downstream of BLOC-1. Our data delineate a novel pathway for Tyrp1 trafficking and illustrate a requirement for ESCRT-I function in controlling protein sorting from vacuolar endosomes to the limiting membrane of a lysosome-related organelle.

Indexed as

AnimalsCarrier ProteinsCell LineDNA-Binding ProteinsEndosomal Sorting Complexes Required for TransportEndosomesHermanski-Pudlak SyndromeHumansIntracellular MembranesIntracellular Signaling Peptides and ProteinsLectinsMelaninsMelanocytesMelanosomesMembrane GlycoproteinsMiceBloc1s6 protein, mouseCarrier ProteinsDNA-Binding ProteinsEndosomal Sorting Complexes Required for Transporthepatocyte growth factor-regulated tyrosine kinase substrateIntracellular Signaling Peptides and ProteinsLectinsMelaninsMembrane GlycoproteinsOxidoreductasesPhosphoproteinsTranscription FactorsTsg101 ProteinTyrp1 protein, mouse

Identifiers

PMID19624486
PMCPMC2747296
OpenAlexW1985826913

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.