Ask about this productRelated genes to: MTMR12 antibody
- Gene:
- MTMR12 NIH gene
- Name:
- myotubularin related protein 12
- Previous symbol:
- PIP3AP
- Synonyms:
- 3-PAP, FLJ20476, KIAA1682, 3PAP
- Chromosome:
- 5p13.3
- Locus Type:
- gene with protein product
- Date approved:
- 2003-09-26
- Date modifiied:
- 2016-10-05
Related products to: MTMR12 antibody
Related articles to: MTMR12 antibody
- Kidney function decline is associated with cardiovascular disease and various other morbidities. Previous studies regarding polygenic risk scores of estimated glomerular filtration rate (eGFR) change were generally based on individuals of European ancestry and not validated on populations of East Asian ancestry. - Source: PubMed
Publication date: 2025/09/04
Chuang Gwo-TsannHsiung Chia-NiChe Tony Pan-HouOh Kook-HwanPark Sue KMoon SungjiLee SangjunRobinson-Cohen CassianneHung Adriana MLi Wen-YiChang Yi-Cheng - In the classical form of α1-antitrypsin deficiency, a misfolded variant α1-antitrypsin Z accumulates in the endoplasmic reticulum of liver cells and causes liver cell injury by gain-of-function proteotoxicity in a sub-group of affected homozygotes but relatively little is known about putative modifiers. Here, we carried out genomic sequencing in a uniquely affected family with an index case of liver failure and 2 homozygous siblings with minimal or no liver disease. Their sequences were compared to sequences in well-characterized cohorts of homozygotes with or without liver disease, and then candidate sequence variants were tested for changes in the kinetics of α1-antitrypsin variant Z degradation in iPS-derived hepatocyte-like cells derived from the affected siblings themselves. - Source: PubMed
Publication date: 2024/04/01
Tafaleng Edgar NLi JieWang YanHidvegi TundaSoto-Gutierrez AlexLocke Adam ENicholas Thomas JWang Yung-ChunPak StephenCho Michael HSilverman Edwin KSilverman Gary AJin Sheng ChihFox Ira JPerlmutter David H - This article has been withdrawn as it was submitted without the knowledge of several co-authors. Under journal policies, all listed authors must have provided final approval of the submitted manuscript and the Corresponding Author is asked to confirm this approval during the submission process. Several of the listed co-authors have stated that they were not involved in the drafting of the manuscript and were not made aware of their inclusion as authors. Therefore they have been removed from this record. The Publisher apologizes for any inconvenience this may cause. The full Elsevier Policy on Article Withdrawal can be found at https://www.elsevier.com/about/our-business/policies/article-withdrawal. - Source: PubMed
Publication date: 2018/06/12
Lei Yang - X-linked myotubular myopathy (XLMTM) is a congenital disorder caused by mutations of the myotubularin gene, MTM1. Myotubularin belongs to a large family of conserved lipid phosphatases that include both catalytically active and inactive myotubularin-related proteins (i.e., "MTMRs"). Biochemically, catalytically inactive MTMRs have been shown to form heteroligomers with active members within the myotubularin family through protein-protein interactions. However, the pathophysiological significance of catalytically inactive MTMRs remains unknown in muscle. By in vitro as well as in vivo studies, we have identified that catalytically inactive myotubularin-related protein 12 (MTMR12) binds to myotubularin in skeletal muscle. Knockdown of the mtmr12 gene in zebrafish resulted in skeletal muscle defects and impaired motor function. Analysis of mtmr12 morphant fish showed pathological changes with central nucleation, disorganized Triads, myofiber hypotrophy and whorled membrane structures similar to those seen in X-linked myotubular myopathy. Biochemical studies showed that deficiency of MTMR12 results in reduced levels of myotubularin protein in zebrafish and mammalian C2C12 cells. Loss of myotubularin also resulted in reduction of MTMR12 protein in C2C12 cells, mice and humans. Moreover, XLMTM mutations within the myotubularin interaction domain disrupted binding to MTMR12 in cell culture. Analysis of human XLMTM patient myotubes showed that mutations that disrupt the interaction between myotubularin and MTMR12 proteins result in reduction of both myotubularin and MTMR12. These studies strongly support the concept that interactions between myotubularin and MTMR12 are required for the stability of their functional protein complex in normal skeletal muscles. This work highlights an important physiological function of catalytically inactive phosphatases in the pathophysiology of myotubular myopathy and suggests a novel therapeutic approach through identification of drugs that could stabilize the myotubularin-MTMR12 complex and hence ameliorate this disorder. - Source: PubMed
Publication date: 2013/06/20
Gupta Vandana AHnia KarimSmith Laura LGundry Stacey RMcIntire Jessica EShimazu JunkoBass Jessica RTalbot Ethan AAmoasii LeonelaGoldman Nathaniel ELaporte JocelynBeggs Alan H - The central portion of the short arm of chromosome 5 is unusual in that large, cytogenetically visible interstitial deletions segregate in families with and without phenotypic consequences. Here we present a family in which a transmitted interstitial deletion of 5p13.3 to 5p14.3 co-segregated with learning and/or behavioral difficulties in six family members. Facial dysmorphism was not striking but a father and daughter both had lacrimal fistulae. The deletion was 12.23 Mb in size (chr5:20,352,535-32,825,775) and contained fifteen known protein coding genes. Five of these (GOLPH3; MTMR12; ZFR; SUB1; and NPR3) and an ultra-conserved microRNA (hsa-miR-579) were present in an 883 kb candidate gene region in 5p13.3 that was deleted in the present family but not in previously reported overlapping benign deletions. Members of the cadherin precursor gene cluster, with brain specific expression, were deleted in both affected and benign deletion families. The candidate genes in 5p13.3 may be sufficient to account for the consistent presence or absence of phenotype in medial 5p deletions. However, we consider the possibility of position effects in which CDH6, and/or other cadherin genes, become penetrant when adjacent genes, or modifiers of gene expression, are also deleted. This could account for the absence of intellectual disability in benign deletions of the cadherin cluster, the cognitive phenotype in medial 5p deletion syndrome and the greater severity of intellectual disability in patients with cri-du-chat syndrome and deletions of 5p15 that extend into the region deleted in the present family. - Source: PubMed
Publication date: 2011/09/30
Barber John C KHuang ShuwenBateman Mark SCollins Amanda L