Ask about this productRelated genes to: MTMR4 antibody
- Gene:
- MTMR4 NIH gene
- Name:
- myotubularin related protein 4
- Previous symbol:
- -
- Synonyms:
- KIAA0647, ZFYVE11
- Chromosome:
- 17q22
- Locus Type:
- gene with protein product
- Date approved:
- 1999-02-05
- Date modifiied:
- 2014-12-02
Related products to: MTMR4 antibody
Related articles to: MTMR4 antibody
- Lung adenocarcinoma (LUAD) shows high recurrence rate and poor prognosis. Genes associated with ubiquitin play a role in the onset and advancement of cancers; however, they have yet to be employed for the diagnosis and prognosis of LUAD. - Source: PubMed
Publication date: 2025/08/15
Li YueTian WeiChen ChenLiu HailinZhang ZhenfaWang Changli - Although research has increasingly been focused on pulmonary tuberculosis (PTB) in adolescents, its diagnosis remains complex and challenging. Thus, the use of host transcription markers in the diagnosis of adolescent PTB was evaluated in this study. - Source: PubMed
Publication date: 2025/07/25
Sha YuxiaZhou HaoquanYan BingdaDa XianzongShao MeilinLi YeDing Shenggang - Autophagic lysosome reformation (ALR) is crucial for lysosomal homeostasis and therefore for different autophagic processes. Despite recent advances, the signaling mechanisms regulating ALR are incompletely understood. We show that RAF1, a member of the RAS/RAF/MEK/ERK pathway initiated by growth factors, has an essential, kinase-dependent role in lysosomal biology. RAF1 ablation impairs autophagy, and a proxisome screen identifies several proteins involved in autophagic and lysosomal pathways in the RAF1 molecular space. Two of these, SPG11 and the lipid phosphatase MTMR4, are RAF1 substrates. RAF1 ablation causes the appearance of enlarged autolysosomes and alters the phosphoinositide composition of autolysosomes. RAF1 and MTMR4 colocalize on autolysosomes, and overexpression of a MTMR4 mutant mimicking phosphorylation of the RAF1-dependent site rescues the lysosomal phenotypes induced by RAF1 ablation. Our data identify an RAF1 function in lysosomal homeostasis and a substrate through which the kinase regulates phospholipid metabolism at the lysosome, ALR, and autophagy. - Source: PubMed
Publication date: 2025/04/03
Toifl StefanieDidusch SebastianEhrenreiter KarinDesideri EnricoDorard CoralieBaccarini Manuela - Pharmacologic intervention in chronic heart failure (HF) with renal insufficiency is one of the clinical challenges due to the fact that the mechanisms of cardio-renal interactions in chronic heart failure (CHF) progressing have not been fully revealed. In this paper, C57BL/6 mice were applied thoracic aortic narrowing surgery to establish pressure overload CHF model. Cardiac function, serum markers, renal pathologic changes and kidney metabolism were analyzed at 4th, 8th, 12th, and 16th week after surgery respectively to evaluate the heart-Kidney pathologic overlap. Kidney proteomic analysis was performed at 16th week after operation. As a result, renal hypofiltration and exacerbation of pathological damage was observed accompanying cardiac function deterioration after 12th week. 66 differentially expressed proteins and 13 differential metabolites were found to be involved in the cardio-renal pathological overlap. Joint proteomic and metabolomic analysis revealed that signal pathways like Phosphatidylinositol signaling system, Glucagon signaling pathway, the Glyoxylate and dicarboxylate metabolism; DEPs of Pten, Mtmr4, PLC and CPT1, differential metabolites like aspartic acid and isocitrate deserve further investigation. - Source: PubMed
Publication date: 2024/12/17
Wang ChunliuZhou JieJia PuYang YangSong RuixueZheng XiaohuiZhang HongLi Ye - Atherosclerosis (AS) is the most prevalent cardiovascular disease and remains the major contributor to death and mortality globally. Leonurine (LEO) is a unique alkaloid compound with protective effects on the cardiovascular system. However, the exact mechanisms underlying its cardiovascular-protecting action are still not fully elucidated. The methyltransferase 3 (METTL3), the catalytic core of the N6-methyladenosine modification (mA) methyltransferase complex, has been shown to inhibit autophagy and exacerbate the process of AS via regulation of mA modification of mRNA. - Source: PubMed
Publication date: 2024/08/11
Yu XinyuanZhang YaoyuanWang JuanWang XiaodanChen XuYin KaiZhu Xiao