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Polo-like kinase 1 (PLK1) is a novel CARD14-binding protein in keratinocytes

Stella Iliaki, Marja Kreike (UGent) , Natalia Ferreras Moreno (UGent) , Femke De Meyer (UGent) , Aigerim Aidarova (UGent) , Harald Braun (UGent) , Claude Libert (UGent) , Inna Afonina (UGent) and Rudi Beyaert (UGent)
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Abstract
Caspase recruitment domain (CARD)-containing protein 14 (CARD14) is an intracellular protein that mediates nuclear factor-kappa B (NF-ĸB) signaling and proinflammatory gene expression in skin keratinocytes. Several hyperactivating CARD14 mutations have been associated with psoriasis and other inflammatory skin diseases. CARD14-induced NF-ĸB signaling is dependent on the formation of a CARD14-BCL10-MALT1 (CBM) signaling complex, but upstream receptors and molecular mechanisms that activate and regulate CARD14 signaling are still largely unclear. Using unbiased affinity purification and mass spectrometry (AP-MS) screening, we discover polo-like kinase 1 (PLK1) as a novel CARD14-binding protein. CARD14-PLK1 binding is independent of the CARD14 CARD domain but involves a consensus phospho-dependent PLK1-binding motif in the CARD14 linker region (LR). Expression of the psoriasis-associated CARD14(E138A) variant in human keratinocytes induces the recruitment of PLK1 to CARD14-containing signalosomes in interphase cells, but does not affect the specific location of PLK1 in mitotic cells. Finally, disruption of the PLK1-binding motif in CARD14(E138A) increases CARD14-induced proinflammatory signaling and gene expression. Together, our data identify PLK1 as a novel CARD14-binding protein and indicate a negative regulatory role for PLK1 in CARD14 signaling.
Keywords
CARD14 signaling, NF-KB, PLK1, Phosphorylation, Psoriasis, Mitosis, KAPPA-B ACTIVATION, BINDING DOMAIN, PHOSPHORYLATION, IDENTIFICATION, MUTATIONS

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MLA
Iliaki, Stella, et al. “Polo-like Kinase 1 (PLK1) Is a Novel CARD14-Binding Protein in Keratinocytes.” BIOCHEMICAL PHARMACOLOGY, vol. 228, 2024, doi:10.1016/j.bcp.2024.116316.
APA
Iliaki, S., Kreike, M., Ferreras Moreno, N., De Meyer, F., Aidarova, A., Braun, H., … Beyaert, R. (2024). Polo-like kinase 1 (PLK1) is a novel CARD14-binding protein in keratinocytes. BIOCHEMICAL PHARMACOLOGY, 228. https://doi.org/10.1016/j.bcp.2024.116316
Chicago author-date
Iliaki, Stella, Marja Kreike, Natalia Ferreras Moreno, Femke De Meyer, Aigerim Aidarova, Harald Braun, Claude Libert, Inna Afonina, and Rudi Beyaert. 2024. “Polo-like Kinase 1 (PLK1) Is a Novel CARD14-Binding Protein in Keratinocytes.” BIOCHEMICAL PHARMACOLOGY 228. https://doi.org/10.1016/j.bcp.2024.116316.
Chicago author-date (all authors)
Iliaki, Stella, Marja Kreike, Natalia Ferreras Moreno, Femke De Meyer, Aigerim Aidarova, Harald Braun, Claude Libert, Inna Afonina, and Rudi Beyaert. 2024. “Polo-like Kinase 1 (PLK1) Is a Novel CARD14-Binding Protein in Keratinocytes.” BIOCHEMICAL PHARMACOLOGY 228. doi:10.1016/j.bcp.2024.116316.
Vancouver
1.
Iliaki S, Kreike M, Ferreras Moreno N, De Meyer F, Aidarova A, Braun H, et al. Polo-like kinase 1 (PLK1) is a novel CARD14-binding protein in keratinocytes. BIOCHEMICAL PHARMACOLOGY. 2024;228.
IEEE
[1]
S. Iliaki et al., “Polo-like kinase 1 (PLK1) is a novel CARD14-binding protein in keratinocytes,” BIOCHEMICAL PHARMACOLOGY, vol. 228, 2024.
@article{01J06AYCE0BGMB96YC67NV83BR,
  abstract     = {{Caspase recruitment domain (CARD)-containing protein 14 (CARD14) is an intracellular protein that mediates nuclear factor-kappa B (NF-ĸB) signaling and proinflammatory gene expression in skin keratinocytes. Several hyperactivating CARD14 mutations have been associated with psoriasis and other inflammatory skin diseases. CARD14-induced NF-ĸB signaling is dependent on the formation of a CARD14-BCL10-MALT1 (CBM) signaling complex, but upstream receptors and molecular mechanisms that activate and regulate CARD14 signaling are still largely unclear. Using unbiased affinity purification and mass spectrometry (AP-MS) screening, we discover polo-like kinase 1 (PLK1) as a novel CARD14-binding protein. CARD14-PLK1 binding is independent of the CARD14 CARD domain but involves a consensus phospho-dependent PLK1-binding motif in the CARD14 linker region (LR). Expression of the psoriasis-associated CARD14(E138A) variant in human keratinocytes induces the recruitment of PLK1 to CARD14-containing signalosomes in interphase cells, but does not affect the specific location of PLK1 in mitotic cells. Finally, disruption of the PLK1-binding motif in CARD14(E138A) increases CARD14-induced proinflammatory signaling and gene expression. Together, our data identify PLK1 as a novel CARD14-binding protein and indicate a negative regulatory role for PLK1 in CARD14 signaling.}},
  articleno    = {{116316}},
  author       = {{Iliaki, Stella and Kreike, Marja and Ferreras Moreno, Natalia and De Meyer, Femke and Aidarova, Aigerim and Braun, Harald and Libert, Claude and Afonina, Inna and Beyaert, Rudi}},
  issn         = {{0006-2952}},
  journal      = {{BIOCHEMICAL PHARMACOLOGY}},
  keywords     = {{CARD14 signaling,NF-KB,PLK1,Phosphorylation,Psoriasis,Mitosis,KAPPA-B ACTIVATION,BINDING DOMAIN,PHOSPHORYLATION,IDENTIFICATION,MUTATIONS}},
  language     = {{eng}},
  pages        = {{13}},
  title        = {{Polo-like kinase 1 (PLK1) is a novel CARD14-binding protein in keratinocytes}},
  url          = {{http://doi.org/10.1016/j.bcp.2024.116316}},
  volume       = {{228}},
  year         = {{2024}},
}

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