Kinases MINK1
- Known as:
- Kinases MINK1
- Catalog number:
- PK-MINK1-A010
- Product Quantity:
- 10
- Category:
- -
- Supplier:
- Biaffin
- Gene target:
- Kinases MINK1
Related genes to: Kinases MINK1
- Gene:
- MINK1 NIH gene
- Name:
- misshapen like kinase 1
- Previous symbol:
- -
- Synonyms:
- B55, MINK, ZC3, MAP4K6, YSK2
- Chromosome:
- 17p13.2
- Locus Type:
- gene with protein product
- Date approved:
- 2005-01-20
- Date modifiied:
- 2016-04-04
Related products to: Kinases MINK1
Adenylate kinases are involved in regulating the adenine nucleotide composition within a cell by catalyzing the reversible transfer of phosphate groups among adenine nucleotides. Three isozymes of adeAEE788 AEE788 is a novel multitargeted human epidermal receptor (HER) 1_2 and vascular endothelial growth factor receptor (VEGFR) 1_2 receptor family tyrosine kinases inhibitor with IC50 of 2, 6, 77,AK3L1 is a member of the adenylate kinase family of enzymes. The protein is localized to the mitochondrial matrix. Adenylate kinases regulate the adenine and guanine nucleotide compositions within a canti-MINK1 MAP4K6 (Internal)anti-MINK1 / MAP4K6anti-MINK1 / MAP4K6 (Internal)B55,GCK family kinase MiNK,Homo sapiens,Human,MAP4K6,MAPK_ERK kinase kinase kinase 6,MEK kinase kinase 6,MEKKK 6,MINK,MINK1,Misshapen_NIK-related kinase,Misshapen-like kinase 1,Mitogen-activated proteBLK ( B lymphoid tyrosine kinase), with 505-amino acid protein (about 56KDa), belongs to the Src non-receptor tyrosine kinases family.Different subcellular localizations of Src-family kinases may be iBLK ( B lymphoid tyrosine kinase), with 505-amino acid protein (about 56KDa), belongs to the Src non-receptor tyrosine kinases family.Different subcellular localizations of Src-family kinases may be iBLK ( B lymphoid tyrosine kinase), with 505-amino acid protein (about 56KDa), belongs to the Src non-receptor tyrosine kinases family.Different subcellular localizations of Src-family kinases may be iBos taurus,Bovine,CKS1,CKS-1,CKS1B,Cyclin-dependent kinases regulatory subunit 1Bos taurus,Bovine,CKS2,CKS-2,Cyclin-dependent kinases regulatory subunit 2Bos taurus,Bovine,NUCKS1,Nuclear ubiquitous casein and cyclin-dependent kinases substrateBovine c-Jun N-terminal kinases stress-activated protein kinase ELISABovine c-Jun N-terminal kinases/stress-activated protein kinase ELISA kit Related articles to: Kinases MINK1
- Chemotherapy-induced peripheral neuropathy (CIPN) is a major dose-limiting side effect of cancer treatment, yet the lack of predictive human models continues to hinder therapeutic progress. Here, we establish a scalable and reproducible model of paclitaxel-induced axon degeneration and neurotoxicity in human iPSC-derived sensory neurons, suitable for high-throughput identification of neuroprotective compounds. Using this platform, we screen a library of 192 kinase inhibitors and identify 19 hits that commonly inhibit three STE20 kinases-MAP4K4, MINK1, and TNIK. Genetic knockdown studies reveal that multi-kinase inhibition of these kinases is required for neuroprotection against paclitaxel. Consistently, selective pharmacological inhibition of the identified STE20 kinases rescues paclitaxel-induced axon degeneration in iPSC-derived sensory neurons and primary human dorsal root ganglia (DRG) and preserves intraepidermal nerve fiber density in a mouse model of CIPN. Together, these findings establish a translational human sensory neuron platform that enables target validation and drug discovery for CIPN. - Source: PubMed
Publication date: 2026/05/06
Petrova VeselinaMills Caitlin EHug ClemensCetinkaya-Fisgin AyselSplaine JenniferFouladzadeh SepidehHakim SaraPowell RasheenZhen ShannonChung MirraBradshaw Gary ADeng TaoSingec IlyasWang QingKawaguchi RikiJonnagaddala HarathiBarrett Lee BSmith Jennifer AKalocsay MarianGyori Benjamin MHoke AhmetSorger Peter KWoolf Clifford J - The nucleotide oligomerization domain (NOD)-like receptor protein 3 (NLRP3) inflammasome is a cytosolic multiprotein complex that can be activated by a wide variety of stimuli. However, dysregulated activation of NLRP3 is implicated in the pathogenesis of chronic inflammatory diseases. Hence, the activity of NLRP3 is intricately governed by several regulatory mechanisms. Misshapen-like kinase 1 (MINK1), a serine/threonine kinase, plays an important role in the immune cell differentiation and inflammatory response regulation in mammals; however, its regulatory function in NLRP3 inflammasome activation in fish remains poorly understood. In the present study, a homolog gene of MINK1 (MINK1) was cloned and functionally characterized in common carp ( L.). The expression profiling disclosed that was upregulated under spring viremia of carp virus (SVCV) and stimulation. Overexpression of MINK1 promoted NLRP3-mediated inflammasome activation, including apoptosis-associated speck-like protein containing a CARD (ASC) oligomerization, speck formation, cysteine-requiring aspartate protease A/B (Caspase-A/B) enzyme activity and interleukin-1β (IL-1β) cleavage. Mechanistically, MINK1 interacted with NLRP3 via its S_TKC domain and facilitated NLRP3 phosphorylation, thereby promoting its aggregation and activation. Collectively, these discoveries unveil a novel regulatory mechanism that governs the functional regulation of NLRP3 and fine-tuning innate immune responses in teleost. - Source: PubMed
Publication date: 2025/10/22
Liu RongrongZhao KeyingZhao YueYang GuiwenLi Hua - Previously reported antimalarial phosphatidylinositol 4-kinase IIIβ 2,8-diaryl-1,5-naphthyridine inhibitors have shown suboptimal physicochemical and pharmacokinetic properties. A focused target-based structure-activity relationship and structure-property optimization studies identified several compounds with good target and whole-cell activities and improved physicochemical properties. A new frontrunner compound showed an improved pharmacokinetic profile and reduced parasitaemia (91% at 4 × 50 mg/kg QD doses) in the humanized NOD- mouse model of malaria. Compound poses no hERG channel inhibition at high concentrations or mammalian cytotoxicity but shows low selectivity against related human lipid kinases (PI3Kα and PI4Kβ); however, significantly higher selectivity margins were observed against the human MINK1 and MAP4K4 kinases. - Source: PubMed
Publication date: 2025/10/07
Dziwornu Godwin ASeanego DonaldFienberg StephenSypu Venkata SSalomane NicolaasKrugmann LiezlTaylor DaleMasike KeabetsweNjoroge MathewBoonyalai NonlawatLee Marcus C SGodoy Luiz CPasaje Charisse FleridaNiles Jacquin CBasarab Gregory SCoulson Lauren BGhorpade Sandeep RChibale Kelly - Circular RNA (circRNA) plays a regulatory role in cancer progression, but the role of circ_0092278 in papillary thyroid cancer (PTC) is unclear. In this research, we aimed to reveal the effect of circ_0092278 on PTC progression as well as its interaction with the eukaryotic translation initiation factor 4A3 (EIF4A3). The expression of circ_0092278 in PTC samples was analyzed using quantitative real-time polymerase chain reaction (qRT-PCR). Cell experiments were conducted to assess the effects of circ_0092278 on PTC cell viability, migration, and invasion. Furthermore, key proteins involved in the phosphatidylinositol 3-kinase/protein kinase B/mammalian target of rapamycin (PI3K/AKT/mTOR) pathway were examined using western blotting. Additionally, a xenograft model in nude mice was used to investigate the role of circ_ 0092278. The interactions between EIF4A3 and circ_0092278 were analyzed through RNA-binding protein immunoprecipitation and qRT-PCR assays. Circ_0092278, located in the cell cytoplasm, was significantly upregulated in PTC. Knockdown of circ_0092278 reduced PTC cell proliferation, migration, invasion, and tumor growth by inhibiting the PI3K/Akt/mTOR pathway. Conversely, overexpression of circ_0092278 prompted PTC cell malignancy by activating the PI3K/Akt/mTOR pathway. Additionally, EIF4A3 was found to bind to MINK1 (circ_0092278 linear gene), thereby enhancing the expression of circ_0092278. Circ_0092278, controlled by EIF4A3, promotes PTC progression by activating the PI3K/Akt/mTOR pathway. Our findings indicate that targeting the EIF4A3-circ_0092278 axis may provide a novel approach for treating PTC. - Source: PubMed
Publication date: 2025/06/19
Liu MengjiangZhang LinghuiYan Zhaodan - Capping protein regulator and myosin 1 Linker 1 (CARMIL1) is a multifunctional regulator of actin polymerization, ruffle formation, and lamellipodia development, making it essential for cell spreading and migration. While its protein-level functions are perceived, phospho-signaling of highly phosphorylated CARMIL1 remains unexplored. This study investigates CARMIL1 phosphorylation and its regulatory mechanisms. Global phosphoproteome datasets captured the most frequently detected and differentially regulated CARMIL1 phosphosites under different conditions to be in the CARMIL_C domain (T916, S968, and S1067). A coregulation-based method was employed to identify interactors and upstream kinases that are coregulated with the phosphorylation sites. These sites exhibited a consistent co-occurrence pattern including both positive and negative coregulation. The phosphosites of complex interactors showed positive and negative coregulation and were involved in cell cycle regulation and cell growth. AKT1, PAK2, and MYLK were identified as potential upstream kinases for CARMIL at S968, while WNK1 was predicted as a potential upstream kinase for S1067, suggesting distinct regulatory mechanisms for these phosphorylation sites. Phosphorylation at CDK1 S146, MAP4K2 S238, MINK1 S641, and TNIK S678 was found coregulated high with CARMIL T916 in human brain cancer. Notably, most coregulated proteins were associated with regulation of the actin cytoskeleton pathway. Our results show that phosphorylation of CARMIL1 in the C-terminal domain highly influences actin cytoskeletal organization. It offers new insights on CARMIL1-mediated cellular functions, deepening our comprehension of its involvement in cytoskeletal dynamics. - Source: PubMed
Publication date: 2025/06/16
Sheela AkhilaMahin AlthafUmmar SamseeraVattoth Nazah NaurahDcunha LeonaGopalakrishnan Athira PerunellyRaju Rajesh