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Title 

Interleukin-32α modulates promyelocytic leukemia zinc finger gene activity by inhibiting protein kinase C?-dependent sumoylation

Authors 

Y S ParkJ W KangD H LeeM S KimY BakY YangHee Gu LeeJ HongD Y Yoon

Publisher 

Elsevier

Issue Date 

2014

Citation 

International Journal of Biochemistry & Cell Biology, vol. 55, no. C, pp. 136-143

Keywords 

Interleukin 32αPromyelocytic leukemia zinc finger proteinSmall ubiquitin-like modifier-2

Abstract 

Interleukin-32 (IL-32) is a proinflammatory cytokine. However, there is growing evidence that IL-32 also plays a mediatory role intracellularly. In this study, we present evidence that IL-32α modifies and inhibits promyelocytic leukemia zinc finger (PLZF), a sequence-specific transcriptional regulator that regulates the expression of a subset of interferon (IFN)-stimulated genes (ISGs). We screened IL-32α-interacting proteins in a human spleen cDNA library using the yeast two-hybrid assay, and investigated the functional relevance of the interaction between IL-32α and PLZF. We demonstrated that IL-32α interacts with protein kinase C (PKC)δ and PKCε in a phorbol 12-myristate 13-acetate (PMA) dependent way, and that PKCε regulates the interaction of IL-32α with PLZF. We verified the involvement of PKCε in the interaction between these proteins by using various PKC inhibitors. PLZF is known to be modified by small ubiquitin-like modifier (SUMO)-1, but it is unclear whether SUMO-2 conjugation of PLZF occurs. We showed that IL-32α inhibited SUMO-2-conjugation of PLZF. Further, we demonstrated that sumoylated PLZF decreased when IL-32α was co-expressed. PKCε affected the sumoylation of PLZF only in the presence of IL-32α because PKC inhibitor treatment did not reduce PLZF sumoylation in the absence of IL-32α. We finally investigated whether IL-32α-mediated inhibition of PLZF sumoylation affected the transcriptional activity of PLZF, and demonstrated that the inhibition of sumoylation of PLZF by IL-32α down-regulated ISGs induced by PLZF. Together, our data suggest that IL-32α associates with PLZF and PKCε, and then inhibits PLZF sumoylation, resulting in suppression of the transcriptional activity of PLZF.

ISSN 

1357-2725

Link 

http://dx.doi.org/10.1016/j.biocel.2014.08.018

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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