Evidence map›Paper›PMID 17762858›Full record

ArticleThe Journal of investigative dermatology2008

Localization of the TIG3 transglutaminase interaction domain and demonstration that the amino-terminal region is required for TIG3 function as a keratinocyte differentiation regulator.

Ralph Jans, Michael T Sturniolo, Richard L Eckert

RetractedOpen access · bronzeAbstract readRetracted Publication
PubMed Publisher
In one paragraph

Article in The Journal of investigative dermatology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.2field-weighted citation impact, top 20% 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

21 citing papers in PubMed, 34 citations in OpenAlex.

  1. The Phospholipase AJournal of lipid and atherosclerosis · 2026
    Review
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  3. Article
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  8. The HRASLS (PLA/AT) subfamily of enzymes.Journal of biomedical science · 2015
    Review
  9. Article
  10. TIG3: an important regulator of keratinocyte proliferation and survival.The Journal of investigative dermatology · 2014
    Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Ralph JansDepartment of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, Maryland 21201, USA.
Michael T Sturniolo
Richard L Eckert
University of Maryland, Baltimore · US

Funding

UNIVERSITY OF MARYLAND GREENEBAUM CANCER CENTERSUPPORT GRANTP30CA134274 · NCI · UNIVERSITY OF MARYLAND BALTIMORE · PI FEYRUZ VIRGILIA RASSOOL · 2008 to 2026
$51.0M
Vitamin D endocrine system and Protection Against Skin TumorlgenesisP30AR039750 · NIAMS · CASE WESTERN RESERVE UNIVERSITY · PI COOPER, KEVIN D · 1988 to 2015
$9.1M
NCI NIH HHS P30 CA134274NIAMS NIH HHS AR39750
6 · The paper itself

Abstract

Tazarotene-induced gene 3 (TIG3) regulates keratinocyte terminal differentiation by activating type I transglutaminase (TG1). TIG3 consists of an amino-terminal (N-terminal) segment, that encodes several conserved motifs, and a carboxy-terminal (C-terminal) membrane-anchoring domain. By producing a series of truncation mutants that remove segments of the N-terminal region, and monitoring the ability of each mutant to co-precipitate TG1, function as a TG1 substrate, or functionally localize with TG1 in cells, we show that the TIG3 domain that interacts with TG1 is located within a TIG3 segment spanning amino acids 112-164. Although they bind TG1, TIG3 mutants lacking the conserved N-terminal region drive apoptosis-like cell death characterized by cell rounding, membrane blebbing, cytochrome c release, procaspase-3 and poly(ADP-ribose)polymerase (PARP) cleavage, and reduced p53 and p21 levels. Compared with TIG3, these truncated mutants have an increased tendency to associate with membranes. A mutant lacking the C-terminal membrane-anchoring domain is inactive. These findings suggest that TIG3 interaction with TG1 does not require the N-terminal conserved domains, that the TIG3 N-terminal region is required for TIG3-dependent keratinocyte differentiation, that its removal converts TIG3 into a proapoptotic protein, and that this change in action of TIG3 is associated with an intracellular redistribution.

Indexed as

AcyltransferasesAnimalsApoptosisCadaverineCell DifferentiationCells, CulturedChlorocebus aethiopsCOS CellsCytochromes cEpidermal CellsFluorescenceHumansKeratinocytesLipoylationMolecular WeightMutagenesisAcyltransferasesCadaverineCytochromes clecithin-retinol acyltransferasePLAAT4 protein, humanReceptors, Retinoic Acidtransglutaminase 1Transglutaminases

Identifiers

PMID17762858
OpenAlexW2001362516

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.