Ask about this productRelated genes to: STK38 antibody
- Gene:
- STK38 NIH gene
- Name:
- serine/threonine kinase 38
- Previous symbol:
- -
- Synonyms:
- NDR, NDR1
- Chromosome:
- 6p21.31
- Locus Type:
- gene with protein product
- Date approved:
- 2001-12-19
- Date modifiied:
- 2018-05-17
Related products to: STK38 antibody
Related articles to: STK38 antibody
- The cellular response to environmental fluctuations, such as increased temperature, is crucial in promoting cell survival and plays an increasingly recognized role in cancer biology. Important cellular functions altered by heat stress are cell polarization and protein translation. Previous studies have shown that heat stress alters the dynamics of Cdc42, a key regulator of cell polarization in eukaryotes, and promotes ribonucleoprotein (RNP) granule formation, reprogramming protein translation. The biological mechanisms underlying these vast changes are only partially known. Here, we report that the conserved NDR kinase Orb6, a homolog of mammalian STK38, responds to heat stress and regulates heat stress resilience by modulating Cdc42 dynamics and promoting RNP granule assembly in Schizosaccharomyces pombe. Also, we discovered a finely tuned mechanism whereby stress-activated mitogen-activated protein kinase (MAPK) Sty1 negatively regulates Orb6 kinase and Orb6 C-terminal phosphorylation during heat stress. Orb6 inhibition by Sty1 increases the sensitivity of the cell to heat stress in a temperature-specific manner, fostering increased stress resilience and metabolic adaptation. These observations highlight the role of NDR kinase in the process of heat adaptation and thermotolerance during environmental cell exposure to elevated temperatures. - Source: PubMed
Publication date: 2026/04/22
Doyle Laura PTams Robert NChen ChuanNuñez IllyceHaller Patrick RomanVerde Fulvia - Paligenosis is a conserved cellular plasticity program that allows mature cells to reenter the cell cycle in response to tissue injury. Paligenosis progresses via three stages: autodegradation (with dramatic increase in autophagy and lysosomes), induction of metaplastic or fetal-like genes, and cell cycle entry. Hippo signaling, particularly the downstream effector YAP1, regulates cellular plasticity, but its role in paligenosis has not been studied. Here, we examine YAP1 dynamics during paligenosis in digestive-enzyme-secreting chief cells from the mouse stomach. We identified Serine/Threonine Kinase 38 (STK38) as a noncanonical YAP1 kinase that phosphorylates and deactivates YAP1 in uninjured chief cells. During paligenosis, STK38 was degraded by autophagy in stage 1, dephosphorylating and activating YAP1. YAP1 activation was necessary and sufficient for paligenosis-driven conversion of chief cells into metaplastic, proliferating progenitors. Additionally, we show that STK38, like canonical Hippo kinases, interacts with Neurofibromatosis Type 2 (Merlin), a scaffold that recruits Hippo kinases to phosphorylate YAP1. We also observed the same pattern of YAP1 induction via autophagic destruction of STK38 in other tissues and cell types, suggesting injury-induced activation of autophagy in differentiated cells during tissue damage may be a more general feature by which Hippo effectors induce plasticity for regeneration. - Source: PubMed
Publication date: 2026/03/30
Zeng YongjiHuang Yang-ZheLi Qing KayHo RaymondBark Steven JWillet Spencer GDiPaolo Richard JMills Jason C - Glioblastoma (GBM) remains a lethal brain tumor due to therapy resistance. While autophagy contributes to temozolomide (TMZ) resistance, its regulation is incompletely understood. This study investigates the role of replication factor RFC4, which is associated with poor prognosis and TMZ resistance in GBM. Multi-omics analyses and molecular experiments reveal that TMZ-induced chromatin accessibility enables transcription factor YY1 to bind the RFC4 promoter and upregulate its expression. RFC4, in turn, stabilizes the kinase STK38, which is essential for autophagosome formation. The RFC4-STK38 interaction facilitates BECN1 recruitment, thereby activating autophagy. Phosphorylation of STK38 at T444 stabilizes this complex, whereas a phospho-deficient mutant impairs autophagy. In vivo, RFC4 overexpression confers TMZ resistance, reversible by autophagy inhibition. Thus, our findings identify the RFC4-STK38-BECN1 axis as a mechanism underlying TMZ resistance and a potential target for precision therapy in GBM. - Source: PubMed
Publication date: 2026/03/23
Mao MinJi HangYu Wen-QianGai Qu-JingSun QiangYan QianXu Sen-LinZhu Meng-LiQu Mei-HuaLiu Han-MinHugnot Jean-PhilipeHe XiWang XinWang Yan - Metastasis remains the primary driver of cancer-related mortality; therefore, deeper mechanistic insights are needed to develop effective therapeutic strategies. Cutaneous melanoma (SKCM), the most aggressive skin malignancy with increasing incidence worldwide, exemplifies this clinical challenge. Through multiomics analysis of melanoma datasets, we identify serine/threonine kinase 38 (STK38) as a critical mediator of tumor metastasis. Elevated STK38 expression correlates strongly with metastatic progression and reduced survival in melanoma patients. Functional studies demonstrate that STK38 not only regulates cell proliferation and autophagy but also drives migration and epithelial-mesenchymal transition by sensitizing melanoma cells to tumor microenvironmental cues. Transcriptomic profiling reveals that STK38 drives tumor metastasis via the Wnt/β-catenin and Hippo signaling pathways. Mechanistically, ChIP-seq data show that CCCTC-binding factor (CTCF) binds to both the promoter and the first-intron enhancer of . Disruption of these binding sites via the CRISPR/Cas9 system abolishes chromatin loop formation, suppresses promoter-enhancer functional connectivity, and downregulates STK38 expression. Our findings identify STK38 as a metastasis-promoting regulator in melanoma and suggest that its therapeutic targeting impedes metastatic dissemination. - Source: PubMed
Publication date: 2026/03/13
Cao QingYang FangfangTian YeYang QiqiCao LichaoZhao MinRen YuxinYu XinruLai MengmengLi YingchunChen MingYang JinChen Erfei - Semen cryopreservation and artificial insemination have crucial and beneficial effects on cattle breeding. The freezability of sperm, as primarily reflected by post-thaw sperm motility (PTM), is essential for evaluating semen quality. Some studies have shown notable differences in sperm freezability among various bulls. Here, we compared protein profiles of sperm cells and seminal plasma extracellular vesicles (SPEVs) in the high sperm freezability group and the low sperm freezability group of Holstein bulls to identify the important proteins and their mechanisms that affect sperm freezability. As a result, 432 and 394 differentially expressed proteins (DEPs) were identified in sperm and SPEVs between high and low freezability groups. The results of weighted correlation network analysis (WGCNA) showed that the blue module was significantly (r = 0.89, P = 9 × 10) associated with sperm freezability. In addition, the pathway analysis revealed that "Metabolic pathways" and "Oxidative phosphorylation" were the predominant biological processes represented. Furthermore, 17 DEPs were found located in the previously identified QTLs related to post-thaw sperm motility, indicating possible variation in their genes. Interestingly, the expression of 142 protein pairs in sperm were significantly (|r| >0.9, P < 0.05) correlated with their expression in SPEVs. Finally, we detected genetic variations in six important candidate genes (STK38, HSPA1A, HSP90B1, LPO, DNASE2 and CUTA), and found that a missense mutation (Chr23g. 23:27522566 A > G) in HSPA1A may affect sperm freezability by decreasing the expression of HSPA1A. Our study highlighted the different protein characteristics of sperm and SPEVs in samples with distinct sperm freezability. These proteins, together with relevant SNPs might be useful markers for selecting bulls with high sperm freezability. - Source: PubMed
Publication date: 2026/02/02
Cao JinkangLeng BingwenZhang ChunWang YachunZhang YiZheng XianruiZhang YuanpeiLi YanqinJiang Li