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
- Bicaudal C Homolog 1 (BICC1) is a conserved RNA-binding protein that, in mammals, has been primarily associated with polycystic kidney disease and renal organogenesis. However, its role in other disease contexts, including cancer, remains poorly understood. In this study, we characterized the BICC1 interactome, with emphasis on its dependence on RNA and the sterile alpha motif (SAM) domain, to identify novel biological processes associated with BICC1 function. Protein complexes were purified from HEK293T cells by co-immunoprecipitation and analyzed by mass spectrometry. Notably, co-immunoprecipitations performed in the presence of RNA yielded a larger number of interacting proteins, with 31 of 71 proteins (~43%) uniquely identified under RNA-preserved conditions, highlighting the critical role of RNA in mediating BICC1 protein-protein interactions. Enriched proteins were predominantly associated with mRNA splicing, the PRMT5 methylosome complex, and membraneless organelles, such as biomolecular condensates. Consistent with these findings, immunofluorescence assays performed on stressed cells revealed the co-localization of BICC1 with stress granule markers. Moreover, BICC1 interactions with PRMT5, STK38, PARP1, and IGF2BP1 were confirmed by immunoblotting. - Source: PubMed
Publication date: 2026/08/07
do Amaral-Prado Heloísa MonteiroMoreira Gabriela AlvesSantos CristianeBosso Fernando HenriqueCiamponi Felipe EduardoBarbosa Guilherme OliveiraBengtson Mario HenriqueMassirer Katlin Brauer - Although aberrant activation of autophagy is well known in triple-negative breast cancer (TNBC), its functional roles and underlying mechanisms remain largely unknown. In the present study, we found that high UBE2L6 expression was strongly associated with aggressive clinical features in TNBC. We demonstrated that UBE2L6 promoted migration, invasion, and lung metastasis of TNBC by enhancing STK38-mediated autophagy. Mechanistically, UBE2L6 stabilized STK38 by promoting its ISGylation and inhibiting its ubiquitin-proteasomal degradation. Therefore, targeting UBE2L6 and modulating the STK38 ISGylation-autophagy axis represent potential intervention points in TNBC. - Source: PubMed
Publication date: 2026/07/06
Ji LiangLi KangFeng JingYin Jun-HuiHe Yu-TingZhang Wen-JingLi Zhuo-LingGu Zi-HaoYang Na-MinQiao Yuan-QiCheng Ren-JieWang MinLiu ChangHai XinZhou Yi - Receptor-interacting protein kinase 1 (RIPK1) is a key stress sensor regulating cell death, inflammation, and tumorigenesis, yet how RIPK1 becomes activated remains unclear. Here, we identify serine/threonine kinase 38 (STK38) as a novel direct RIPK1 activator. STK38 binds to RIPK1, integrates into RIPK1-containing death complexes, and accelerates RIPK1-dependent cell death. STK38 deletion suppresses RIPK1-mediated necroptosis and apoptosis. Moreover, TNF-α stimulation triggers MEKK2-dependent STK38 activation, which in turn phosphorylates RIPK1 at serine 309, a residue conserved only in higher primates. This phosphorylation at S309 disrupts RIPK1's interaction with its inhibitory kinase MK2, thereby suppressing S320 phosphorylation and facilitating RIPK1 activation. Furthermore, colorectal cancer sample analysis revealed a positive correlation among STK38 expression, RIPK1 activation status, and favourable patient outcomes. Consistently, STK38 deficiency confers resistance to RIPK1-dependent cell death and facilitates tumour progression in a xenograft model. Our findings identify STK38 as an activator of RIPK1 and uncover a novel regulatory mechanism of RIPK1-mediated cell death in humans. - Source: PubMed
Publication date: 2026/07/01
Kim SeongmiLee Seung RiRho HyunjinKim Hye-JungKo Hyuk WanShin DonghyukHong Seung-MoKim MinjoongYu JiyoungKim KyunggonChung Joon-YongSong Jaewhan - The Hippo pathway is a key regulator of development, regeneration, tissue homeostasis, and organ size, and its dysregulation promotes tumorigenesis. However, the precise mechanisms of its regulation in both normal physiology and cancer remain incompletely understood. Here, we identify STK38 and STK38L (also known as NDR1 and NDR2), previously proposed as redundant kinases of LATS, as negative regulators of the Hippo pathway. STK38/L inhibit LATS by competitively binding to MOB1 and disrupting the LATS-MOB1 complex, a process independent of their kinase activity. This inhibitory mechanism is evolutionarily conserved, as the ortholog Tricornered similarly impairs Warts-Mats complex formation, resulting in enlarged fly wing size. Pathologically, STK38L is highly expressed in ovarian cancer and required for ovarian tumor growth, and its amplification correlates with YAP activation and increased tumor sensitivity to TEAD inhibitors. Taken together, our study reveals a conserved role of STK38/L in Hippo pathway regulation, providing new insights into Hippo-dependent growth control and cancer development. - Source: PubMed
Publication date: 2026/07/01
An JeongminHuang ZhenKizhedathu AmruthaLan TianLin TzulingJoo HyejinThilakaratne Eshan MalindaLiu YuhanXu Yun YiYang BingLara-Gonzalez PabloWarrior RahulLuo RayWang Wenqi - Alveolar type II (AT2) cells act as progenitors that sustain gas exchange and drive postinjury repair. Disruption of their proliferation-differentiation balance promotes pulmonary fibrosis and acute respiratory distress syndrome, but the core regulatory mechanisms are unclear. Serum deprivation response protein (SDPR, cavin-2), a caveolae-associated protein involved in proliferation and lipid metabolism, may modulate AT2 fate. This study investigated how the SDPR-STK38 axis regulates AT2 proliferation and differentiation and its impact on lung homeostasis and regeneration. - Source: PubMed
Publication date: 2026/05/06
Wang JieLei XuepeiHuang YiyingTang JiamingShi GuiyingLi HangBai Lin