Evidence map›Paper›PMID 25578910›Full record

ArticleCurrent biology : CB2015

Proteomic analysis of isolated ciliary transition zones reveals the presence of ESCRT proteins.

Dennis R Diener, Pietro Lupetti, Joel L Rosenbaum

Open access · bronzeAbstract read
In one paragraph

Article in Current biology : CB, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
7.4field-weighted citation impact, top 3% 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

57 citing papers in PubMed, 95 citations in OpenAlex.

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  14. Article
  15. Initial ciliary assembly inMolecular biology of the cell · 2023
    Article
  16. Non-classical functions of nuclear pore proteins in ciliopathy.Frontiers in molecular biosciences · 2023
    Review
  17. Article
  18. Article
  19. Review
  20. Shedding of ciliary vesicles at a glance.Journal of cell science · 2022
    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.

Dennis R DienerDepartment of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06511, USA. Electronic address: dennis.diener@yale.edu.
Pietro LupettiDepartment of Life Sciences, University of Siena, Siena 53100, Italy.
Joel L RosenbaumDepartment of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06511, USA. Electronic address: joel.rosenbaum@yale.edu.
University of Siena · IT

Funding

SYNTHESIS AND ASSEMBLY OF FLAGELLAR PROTEINSR37GM014642 · NIGMS · YALE UNIVERSITY · PI ROSENBAUM, JOEL L · 1999 to 2008
$5.6M
SYNTHESIS AND ASSEMBLY OF FLAGELLAR PROTEINSR01GM014642 · NIGMS · YALE UNIVERSITY · PI ROSENBAUM, JOEL L · 1985 to 2015
$3.7M
NIGMS NIH HHS GM014642NIGMS NIH HHS R01 GM014642NIGMS NIH HHS R37 GM014642
6 · The paper itself

Abstract

The transition zone (TZ) is a specialized region of the cilium characterized by Y-shaped connectors between the microtubules of the ciliary axoneme and the ciliary membrane [1]. Located near the base of the cilium, the TZ is in the prime location to act as a gate for proteins into and out of the ciliary compartment, a role supported by experimental evidence [2-6]. The importance of the TZ has been underscored by studies showing that mutations affecting proteins located in the TZ result in cilia-related diseases, or ciliopathies, presenting symptoms including renal cysts, retinal degeneration, and situs inversus [7-9]. Some TZ proteins have been identified and shown to interact with each other through coprecipitation studies in vertebrate cells [4, 10, 11] and genetics studies in C. elegans [3]. As a distinct approach to identify TZ proteins, we have taken advantage of the biology of Chlamydomonas to isolate TZs. Proteomic analysis identified 115 proteins, ten of which were known TZ proteins related to ciliopathies, indicating that the preparation was highly enriched for TZs. Interestingly, six proteins of the endosomal sorting complexes required for transport (ESCRT) were also associated with the TZs. Identification of these and other proteins in the TZ will provide new insights into functions of the TZ, as well as candidate ciliopathy genes.

Indexed as

ChlamydomonasCiliaEndosomal Sorting Complexes Required for TransportMicroscopy, ElectronNuclear Pore Complex ProteinsProteomeProteomicsEndosomal Sorting Complexes Required for TransportNuclear Pore Complex ProteinsProteome

Identifiers

PMID25578910
PMCPMC4318714
OpenAlexW2054954402

What OpenQuestion holds

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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.