Evidence map›Paper›PMID 27582497›Full record

ArticleThe Biochemical journal2016

The Charcot Marie Tooth disease protein LITAF is a zinc-binding monotopic membrane protein.

Wenxia Qin, Lydia Wunderley, Anne L Barrett, Stephen High, Philip G Woodman

Open access · hybridAbstract read
In one paragraph

Article in The Biochemical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

17 citing papers in PubMed, 21 citations in OpenAlex.

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  4. MicroMagnify: A Multiplexed Expansion Microscopy Method for Pathogens and Infected Tissues.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
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  16. Nerve enlargement in an unusual case of inflammatory neuropathy and new gene mutation-morphology is the key.Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology · 2017
    Article
  17. 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

5 authors at 1 institution in 1 country.

Wenxia QinFaculty of Biology Medicine and Health, University of Manchester, Manchester M13 9PT, U.K.
Lydia WunderleyFaculty of Biology Medicine and Health, University of Manchester, Manchester M13 9PT, U.K.
Anne L BarrettFaculty of Biology Medicine and Health, University of Manchester, Manchester M13 9PT, U.K.
Stephen HighFaculty of Biology Medicine and Health, University of Manchester, Manchester M13 9PT, U.K.
Philip G WoodmanFaculty of Biology Medicine and Health, University of Manchester, Manchester M13 9PT, U.K.
University of Manchester · GB

Funding

Medical Research Council G0701140
6 · The paper itself

Abstract

LITAF (LPS-induced TNF-activating factor) is an endosome-associated integral membrane protein important for multivesicular body sorting. Several mutations in LITAF cause autosomal-dominant Charcot Marie Tooth disease type 1C. These mutations map to a highly conserved C-terminal region, termed the LITAF domain, which includes a 22 residue hydrophobic sequence and flanking cysteine-rich regions that contain peptide motifs found in zinc fingers. Although the LITAF domain is thought to be responsible for membrane integration, the membrane topology of LITAF has not been established. Here, we have investigated whether LITAF is a tail-anchored (TA) membrane-spanning protein or monotopic membrane protein. When translated in vitro, LITAF integrates poorly into ER-derived microsomes compared with Sec61β, a bona fide TA protein. Furthermore, introduction of N-linked glycosylation reporters shows that neither the N-terminal nor C-terminal domains of LITAF translocate into the ER lumen. Expression in cells of an LITAF construct containing C-terminal glycosylation sites confirms that LITAF is not a TA protein in cells. Finally, an immunofluorescence-based latency assay showed that both the N- and C-termini of LITAF are exposed to the cytoplasm. Recombinant LITAF contains 1 mol/mol zinc, while mutation of predicted zinc-binding residues disrupts LITAF membrane association. Hence, we conclude that LITAF is a monotopic membrane protein whose membrane integration is stabilised by a zinc finger. The related human protein, CDIP1 (cell death involved p53 target 1), displays identical membrane topology, suggesting that this mode of membrane integration is conserved in LITAF family proteins.

Indexed as

Amino Acid MotifsAmino Acid SequenceApoptosis Regulatory ProteinsCarrier ProteinsCell LineCharcot-Marie-Tooth DiseaseHeLa CellsHumansMembrane ProteinsMicrosomesMolecular Sequence DataNuclear ProteinsProtein TransportTranscription FactorsApoptosis Regulatory ProteinsCarrier ProteinsCDIP1 protein, humanLITAF protein, humanMembrane ProteinsNuclear ProteinsTranscription Factorszinc-binding proteinCDIP1endosomeESCRTmembrane integration

Identifiers

PMID27582497
PMCPMC5095921
OpenAlexW2513957285

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.