ArticleBMB reports2017
Protein tyrosine phosphatase PTPN21 acts as a negative regulator of ICAM-1 by dephosphorylating IKKβ in TNF-α-stimulated human keratinocytes.
Article in BMB reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 10 citations in OpenAlex.
- Article
- Amniotic Fluid Extracellular Vesicle Properties Evolve With Gestational Age and Reflect Fetal Development.Journal of extracellular biology · 2025Article
- Structural analysis of the FERM domain of human protein tyrosine phosphatase non-receptor type 21.Acta crystallographica. Section F, Structural biology communications · 2024Article
- Structural analysis of PTPN21 reveals a dominant-negative effect of the FERM domain on its phosphatase activity.Science advances · 2024Article
- Molecular Analysis of the Interaction between Human PTPN21 and the Oncoprotein E7 from Human Papillomavirus Genotype 18.Molecules and cells · 2021Article
- Review
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3 authors at 1 institution in 1 country.
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Abstract
Intercellular adhesion molecule-1 (ICAM-1), which is induced by tumor necrosis factor (TNF)-α, contributes to the entry of immune cells into the site of inflammation in the skin. Here, we show that protein tyrosine phosphatase non-receptor type 21 (PTPN21) negatively regulates ICAM-1 expression in human keratinocytes. PTPN21 expression was transiently induced after stimulation with TNF-α. When overexpressed, PTPN21 inhibited the expression of ICAM-1 in HaCaT cells but PTPN21 C1108S, a phosphatase activity-inactive mutant, failed to inhibit ICAM-1 expression. Nuclear factor-κB (NF-κB), a key transcription factor of ICAM-1 gene expression, was inhibited by PTPN21, but not by PTPN21 C1108S. PTPN21 directly dephosphorylated phospho-inhibitor of κB (IκB)-kinase β (IKKβ) at Ser177/181. This dephosphorylation led to the stabilization of IκBα and inhibition of NF-κB activity. Taken together, our results suggest that PTPN21 could be a valuable molecular target for regulation of inflammation in the skin by dephosphorylating p-IKKβ and inhibiting NF-κB signaling. [BMB Reports 2017; 50(11): 584-589].
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