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Last update 01 Nov 2024

STK16

Last update 01 Nov 2024

Basic Info

Synonyms

hPSK, MPSK, MPSK1

+ [10]

Introduction

Membrane-associated protein kinase that phosphorylates on serine and threonine residues. In vitro substrates include DRG1, ENO1 and EIF4EBP1. Also autophosphorylates. May be involved in secretory vesicle trafficking or intracellular signaling. May have a role in regulating stromal-epithelial interactions that occur during ductal morphogenesis in the mammary gland. May be involved in TGF-beta signaling. Able to autophosphorylate on Tyr residue; it is however unclear whether it has tyrosine-protein kinase toward other proteins.

Drugs associated with STK16

STK16-IN-1

Target

STK16

Mechanism

STK16 inhibitors

Active Org.-

Originator Org.

Chinese Academy of Sciences

Active Indication-

Inactive Indication

Neoplasms

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with STK16

100 Translational Medicine associated with STK16

0 Patents (Medical) associated with STK16

Literatures (Medical) associated with STK16

01 Dec 2024·Biochemical and Biophysical Research Communications

Decreased mitochondrial translation confers 3,3′-Diindolylmethane resistance to Schizosaccharomyces pombe

Article

Author: Wang, Kaiyu ; Rajib, Samiul Alam ; Nagai, Hideto ; Ueno, Masaru ; Satou, Yorifumi

3,3'-Diindolylmethane (DIM), a compound derived from natural fruits and vegetables, is widely recognized for its anti-cancer activity. However, its action mechanisms remain ambiguous. In this study, to study the molecular mechanism of 3,3'-Diindolylmethane, we identified a novel mutation in the gene of mitochondrial translation elongation factor EF-Ts (tsf1⁺), a key factor in mitochondrial protein translation, that conferred DIM resistance to Schizosaccharomyces pombe. The tsf1Δ also conferred DIM resistance. Decreased mitochondrial translation was found to be responsible for conferring DIM resistance to Schizosaccharomyces pombe, as the cells gained DIM resistance after treatment with chloramphenicol, a specific mitochondrial translation inhibitor. Notably, tsf1Δ conferred DIM resistance in the absence of either autophagy-related protein, Atg7, or nuclear envelope protein, Lem2, two proteins that have been reported to be required for cell survival in the presence of DIM. Overall, this study revealed novel biological functions of DIM and highlighted its potential as an anti-cancer agent.

31 Jul 2024·The FASEB Journal

Fat body‐derived juvenile hormone acid methyltransferase functions to maintain iron homeostasis in Drosophila melanogaster

Article

Author: Liu, Zhi-Hua ; Ye, Yun-Yan ; Wang, Hui-Li

AbstractIron homeostasis is of critical importance to living organisms. Drosophila melanogaster has emerged as an excellent model to study iron homeostasis, while the regulatory mechanism of iron metabolism remains poorly understood. Herein, we accidently found that knockdown of juvenile hormone (JH) acid methyltransferase (Jhamt) specifically in the fat body, a key rate‐limiting enzyme for JH synthesis, led to iron accumulation locally, resulting in serious loss and dysfunction of fat body. Jhamt knockdown‐induced phenotypes were mitigated by iron deprivation, antioxidant and Ferrostatin‐1, a well‐known inhibitor of ferroptosis, suggesting ferroptosis was involved in Jhamt knockdown‐induced defects in the fat body. Further study demonstrated that upregulation of Tsf1 and Malvolio (Mvl, homolog of mammalian DMT1), two iron importers, accounted for Jhamt knockdown‐induced iron accumulation and dysfunction of the fat body. Mechanistically, Kr‐h1, a key transcription factor of JH, acts downstream of Jhamt inhibiting Tsf1 and Mvl transcriptionally. In summary, the findings indicated that fat body‐derived Jhamt is required for the development of Drosophila by maintaining iron homeostasis in the fat body, providing unique insight into the regulatory mechanisms of iron metabolism in Drosophila.

01 Jul 2024·Biochemical Pharmacology

Serine/Threonine kinase 16 phosphorylates STAT3 and confers a JAK2-Inhibition resistance phenotype in triple-negative breast cancer

Article

Author: Chen, Chen ; Zhu, Zhenyun ; Li, Shuangqiong ; Shi, Jian ; Xiang, Qin

Although Janus kinase 2 (JAK2) plays a critical role in the progression of triple-negative breast cancer (TNBC), its inhibitors are incapable of eradicating these tumor cells, implicating drug resistance mechanisms exist. Our evidences show that TNBC cells express high level of Serine/Threonine Kinase 16 (STK16) when JAK2 signaling is blocked. Pharmacological inhibition or silencing of STK16 significantly enhances the sensitivity of TNBC cells to JAK2 inhibition, while over-expression of STK16 alleviates the anti-tumor effect of JAK2-inhibitor. Mechanistically, elevated STK16 expression rescues the phosphorylation status and transcriptional activity of STAT3, as STK16 is able to directly catalyze the phosphorylation of STAT3 at ser-727 residue. Our data indicate that upon JAK2 inhibition, TNBC cells express STK16 to maintain STAT3 transcriptional activity, dual-inhibition of JAK2/STK16 offers a potential way to treat TNBC patients.

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