Ask about this productRelated genes to: MCOLN3 antibody
- Gene:
- MCOLN3 NIH gene
- Name:
- mucolipin 3
- Previous symbol:
- -
- Synonyms:
- TRPML3, FLJ11006, TRP-ML3
- Chromosome:
- 1p22.3
- Locus Type:
- gene with protein product
- Date approved:
- 2003-04-04
- Date modifiied:
- 2014-11-19
Related products to: MCOLN3 antibody
Related articles to: MCOLN3 antibody
- Parkinson's disease (PD) is the second most common progressive neurodegenerative disease that severely affects the quality of life and there is an urgent need to explore unique and effective diagnostic markers. The present study aimed to develop and validate a multigene combination model for the diagnosis of PD based on autophagy-related genes (ARGs) and to discover their correlation with immune infiltrating cells. - Source: PubMed
Publication date: 2026/03/31
Dong ZiyeDai FanshuXing NaWu QiaoliGao HezhenKan PengchengHan YuanCheng XiuliWang YaruFeng XuequanZhang Biao - Mucolipidosis type IV (MLIV) is a rare autosomal recessive lysosomal storage disorder due to biallelic pathogenic variants in the gene. Its main impact is on the central nervous system, leading to severe psychomotor delays, progressive visual impairment, and characteristic brain abnormalities. - Source: PubMed
Publication date: 2025/12/22
Mohsenipour MohaddeseNejati ParhamKhosravi TeymoorAlimoradi ElhamSalehi MohammadOladnabi MortezaAlibakhshi Reza - Acquired resistance to tyrosine kinase inhibitors (TKIs), such as osimertinib, poses a major barrier to effective treatment of non-small cell lung cancer (NSCLC). Recent data suggest that lysosomal Ca signaling, particularly via transient receptor potential mucolipin 3 (TRPML3; also known as MCOLN3), contributes to TKI resistance by promoting lysosomal exocytosis and drug efflux. Here, we investigated the regulatory role of microRNA-601 (miR-601) in modulating TRPML3 expression and its impact on osimertinib resistance in NSCLC. Bioinformatic predictions using the DIANA microT-CDS algorithm identified TRPML3 as a putative target of miR-601. Luciferase reporter assays confirmed direct binding of miR-601 to the TRPML3 3'-untranslated region. Functional assays were conducted with parental and osimertinib-resistant PC9 and HCC827 cells to evaluate the effects of miR-601 on TRPML3 expression, apoptosis, cell-cycle progression, and drug sensitivity. Osimertinib treatment led to a time-dependent miR-601 downregulation in NSCLC cells, and its basal expression remained suppressed in resistant sublines. miR-601 overexpression reduced TRPML3 protein levels, enhanced poly(ADP-ribose) polymerase cleavage, induced G0/G1 cell-cycle arrest, and restored osimertinib sensitivity. Similar effects were observed upon TRPML3 knockdown, supporting a TRPML3-dependent mechanism. Thus, miR-601 negatively regulates TRPML3 and modulated TKI responses in NSCLC cells. Restoring miR-601 expression may represent a promising therapeutic strategy for overcoming acquired osimertinib resistance by targeting TRPML3-mediated lysosomal signaling. - Source: PubMed
Kim Mi SeongKim Min Seuk - Acute pancreatitis (AP) is a severe inflammatory disease. Transient receptor potential (TRP) channels have been reported to participate in various pathophysiological processes. However, the role of TRP channels in the AP remains unclear. Here, we investigated the involvement of TRP channels in AP. - Source: PubMed
Shen ShuangjunWu XiaowanCheng ZhiyuanWang RuiyanJiang JingJiang Weiliang - ATG8s are essential for autophagy as they recruit various machinery to autophagic structures. We previously reported that the intracellular Ca channel TRPML3 specifically interacts with the mammalian ATG8 homolog GATE16, but not LC3B to increase autophagy. However, the underlying mechanism and the role of this specific interaction remain unclear. Here, we report that single amino acid motifs in GATE16 and TRPML3 determine the specificity of this interaction and its function in autophagy. We also discovered that RAB33B, a Golgi-resident small GTPase, functionally interacts with TRPML3 in autophagy and contains an LC3-interacting region (LIR) motif. Surprisingly, RAB33B specifically interacted with GATE16, but not with other ATG8s through an LIR motif, and disrupting this LIR motif inhibited autophagy. Upon induction of autophagy, RAB33B was recruited from the Golgi to the phagophore in an LIR-dependent manner, enhancing the interaction between RAB33B and TRPML3 while promoting autophagy. These results suggest that specific interactions involving GATE16 play a crucial role in autophagy by recruiting TRPML3 and RAB33B, forming protein complexes at the phagophore to promote autophagosome formation. - Source: PubMed
Publication date: 2025/08/25
Park JiwooChoi AreumKwon JinChoi SuziPark Yun MinKim Hyun Jin