TIG3: An Important Regulator of Keratinocyte Proliferation and Survival

Scharadin, Tiffany M.; Eckert, Richard L.

doi:10.1038/jid.2014.79

Cited by 22 publications

(23 citation statements)

References 40 publications

(127 reference statements)

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“…Eckert et al . found that PLAAT‐4 interacts with and activates type I transglutaminase to enhance keratinocyte terminal differentiation . However, it remains unclear whether these biological functions are related to its phospholipid‐metabolizing enzyme activity.…”

Section: An Overview Of Plaat Family Membersmentioning

confidence: 99%

“…The introduction of PLAAT-4 causes terminal differentiation in normal keratinocytes and apoptosis in skin cancer cells [32]. Eckert et al found that PLAAT-4 interacts with and activates type I transglutaminase to enhance keratinocyte terminal differentiation [32]. However, it remains unclear whether these biological functions are related to its phospholipid-metabolizing enzyme activity.…”

Section: Plaat-4mentioning

confidence: 99%

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An involvement of phospholipase A/acyltransferase family proteins in peroxisome regulation and plasmalogen metabolism

2017

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Edited by Wilhelm JustThe H-Ras-like suppressor (HRASLS) is a protein family consisting of five members in humans. Despite their discovery as tumor suppressors, we demonstrated that all these proteins are phospholipid-metabolizing enzymes, such as phospholipase (PL) A 1 /A 2 and acyltransferase. We thus proposed to rename HRASLS1-5 as PLA/acyltransferase (PLAAT)-1-5. Notably, PLAATs exhibit N-acyltransferase activity to biosynthesize N-acylated ethanolamine phospholipids, including N-acyl-plasmalogen, which serve as precursors of bioactive N-acylethanolamines. Furthermore, the overexpression of PLAAT-3 in animal cells causes disappearance of peroxisomes and a remarkable reduction in plasmalogen levels. This finding might be related to the inhibitory effect of PLAAT-3 on the chaperone activity of the peroxin PEX19. In this article, we will review our recent findings about PLAAT proteins, with special reference to their roles in peroxisome biogenesis and plasmalogen metabolism.

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Section: An Overview Of Plaat Family Membersmentioning

confidence: 99%

Section: Plaat-4mentioning

confidence: 99%

An involvement of phospholipase A/acyltransferase family proteins in peroxisome regulation and plasmalogen metabolism

2017

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“…H-REV107-like family is one divergence of the NlpC/P60 superfamily in eukaryotes [1]. Members of the H-REV107-like family include H-REV107, TIG3, A-C1, HRASLS2 and iNAT, and they function as class II tumor suppressors and involve in the regulation of cell proliferation [2][3][4][5][6][7][8][9]. TIG3 (also known as RIG1, HRASLS4 or RARRES3) and H-REV107 (also known as HRASLS3, H-REV107-1, AdPLA) are ubiquitously expressed in many normal tissues, but their expression levels are decreased in most cancer tissues [10][11][12].…”

Section: Introductionmentioning

confidence: 99%

Structural and functional characterization of tumor suppressors TIG3 and H‐REV107

et al. 2015

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a b s t r a c t H-REV107-like family proteins TIG3 and H-REV107 are class II tumor suppressors. Here we report that the C-terminal domains (CTDs) of TIG3 and H-REV107 can induce HeLa cell death independently. The N-terminal domain (NTD) of TIG3 enhances the cell death inducing ability of CTD, while NTD of H-REV107 plays an inhibitory role. The solution structure of TIG3 NTD is very similar to that of H-REV107 in overall fold. However, the CTD binding regions on NTD are different between TIG3 and H-REV107, which may explain their functional difference. As a result, the flexible main loop of H-REV107, but not that of TIG3, is critical for its NTD to modulate its CTD in inducing cell death.

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“…Numerous studies on normal and diseased skin in both humans and animal models have provided detailed knowledge about the molecular repertoire of the different skin cell types and enhanced our understanding of the complex cellular interactions under normal and pathological conditions (Ghadially 2012;Li et al 2014;Scharadin and Eckert 2014;Vanbokhoven et al 2011). However, the expression pattern in skin is still unknown for a large fraction of the human proteome and a readily available compilation of skin-specific gene and protein expression is lacking.…”

Section: Introductionmentioning

confidence: 99%

Expression of Human Skin-Specific Genes Defined by Transcriptomics and Antibody-Based Profiling

Edqvist

Fagerberg

Hallström

et al. 2014

J Histochem Cytochem.

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To increase our understanding of skin, it is important to define the molecular constituents of the cell types and epidermal layers that signify normal skin. We have combined a genome-wide transcriptomics analysis, using deep sequencing of mRNA from skin biopsies, with immunohistochemistry-based protein profiling to characterize the landscape of gene and protein expression in normal human skin. The transcriptomics and protein expression data of skin were compared to 26 (RNA) and 44 (protein) other normal tissue types. All 20,050 putative protein-coding genes were classified into categories based on patterns of expression. We found that 417 genes showed elevated expression in skin, with 106 genes expressed at least five-fold higher than that in other tissues. The 106 genes categorized as skin enriched encoded for well-known proteins involved in epidermal differentiation and proteins with unknown functions and expression patterns in skin, including the C1orf68 protein, which showed the highest relative enrichment in skin. In conclusion, we have applied a genome-wide analysis to identify the human skin-specific proteome and map the precise localization of the corresponding proteins in different compartments of the skin, to facilitate further functional studies to explore the molecular repertoire of normal skin and to identify biomarkers related to various skin diseases.

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TIG3: An Important Regulator of Keratinocyte Proliferation and Survival

Cited by 22 publications

References 40 publications

An involvement of phospholipase A/acyltransferase family proteins in peroxisome regulation and plasmalogen metabolism

An involvement of phospholipase A/acyltransferase family proteins in peroxisome regulation and plasmalogen metabolism

Structural and functional characterization of tumor suppressors TIG3 and H‐REV107

Expression of Human Skin-Specific Genes Defined by Transcriptomics and Antibody-Based Profiling

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