MTMR8 antibody
- Known as:
- MTMR8 (anti-)
- Catalog number:
- orb101222
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Biorbyt biorb
- Gene target:
- MTMR8 antibody
Related genes to: MTMR8 antibody
- Gene:
- MTMR8 NIH gene
- Name:
- myotubularin related protein 8
- Previous symbol:
- -
- Synonyms:
- FLJ20126
- Chromosome:
- Xq11.2
- Locus Type:
- gene with protein product
- Date approved:
- 2002-09-05
- Date modifiied:
- 2015-09-04
- Gene:
- MTMR9 NIH gene
- Name:
- myotubularin related protein 9
- Previous symbol:
- C8orf9, MTMR8
- Synonyms:
- DKFZp434K171, LIP-STYX
- Chromosome:
- 8p23.1
- Locus Type:
- gene with protein product
- Date approved:
- 2001-02-14
- Date modifiied:
- 2016-10-05
Related products to: MTMR8 antibody
Related articles to: MTMR8 antibody
- Regulation of phosphatidylinositol phosphates plays a crucial role in signal transduction, membrane trafficking or autophagy. Members of the myotubularin family of lipid phosphatases contribute to phosphoinositide metabolism by counteracting the activity of phosphoinositide kinases. The mechanisms determining their subcellular localization and targeting to specific membrane compartments are still poorly understood. We show here that the inactive phosphatase MTMR9 localizes to the intermediate compartment and to the Golgi apparatus and is able to recruit its active phosphatase partners MTMR6 and MTMR8 to these locations. Furthermore, MTMR8 and MTMR9 co-localize with the small GTPase RAB1A and regulate its localization. Loss of MTMR9 expression compromises the integrity of the Golgi apparatus and results in altered distribution of RAB1A and actin nucleation-promoting factor WHAMM. Loss or overexpression of MTMR9 leads to decreased rate of protein secretion. We demonstrate that secretion of physiologically relevant cargo exemplified by the WNT3A protein is affected after perturbation of MTMR9 levels. - Source: PubMed
Publication date: 2019/11/06
Doubravská LenkaDostál VojtěchKnop FilipLibusová LenkaMacůrková Marie - The myotubularins are a large family of inositol polyphosphate 3-phosphatases that, despite having common substrates, subsume unique functions in cells that are disparate. The myotubularin family consists of 16 different proteins, 9 members of which possess catalytic activity, dephosphorylating phosphatidylinositol 3-phosphate [PtdIns(3)P] and phosphatidylinositol 3,5-bisphosphate [PtdIns(3,5)P(2)] at the D-3 position. Seven members are inactive because they lack the conserved cysteine residue in the CX(5)R motif required for activity. We studied a subfamily of homologous myotubularins, including myotubularin-related protein 6 (MTMR6), MTMR7, and MTMR8, all of which dimerize with the catalytically inactive MTMR9. Complex formation between the active myotubularins and MTMR9 increases their catalytic activity and alters their substrate specificity, wherein the MTMR6/R9 complex prefers PtdIns(3,5)P(2) as substrate; the MTMR8/R9 complex prefers PtdIns(3)P. MTMR9 increased the enzymatic activity of MTMR6 toward PtdIns(3,5)P(2) by over 30-fold, and enhanced the activity toward PtdIns(3)P by only 2-fold. In contrast, MTMR9 increased the activity of MTMR8 by 1.4-fold and 4-fold toward PtdIns(3,5)P(2) and PtdIns(3)P, respectively. In cells, the MTMR6/R9 complex significantly increases the cellular levels of PtdIns(5)P, the product of PI(3,5)P(2) dephosphorylation, whereas the MTMR8/R9 complex reduces cellular PtdIns(3)P levels. Consequentially, the MTMR6/R9 complex serves to inhibit stress-induced apoptosis and the MTMR8/R9 complex inhibits autophagy. - Source: PubMed
Publication date: 2012/05/30
Zou JunZhang ChunfenMarjanovic JasnaKisseleva Marina VMajerus Philip WWilson Monita P - The myotubularins are a large family of lipid phosphatases with specificity towards PtdIns3P and PtdIns(3,5)P(2). Each of the 14 family members bears a signature phosphatase domain, which is inactive in six cases due to amino acid changes at the catalytic site. Fragmentary data have indicated heteromeric interactions between myotubularins, which have hitherto paired an active family member with an inactive one. In this study we have conducted a largescale analysis of potential associations within the human myotubularin family, through directed two-hybrid screening and immunoprecipitation of epitope-tagged proteins. We have confirmed all previously reported combinations and identified novel heteromeric interactions: MTMR8 with MTMR9, and MTMR3 with MTMR4, the first such combination of enzymatically active MTMs. We also report the capacity of several family members to self-associate, including MTMR3 and MTMR4. Subcellular localisation studies reveal a unique distribution of MTMR4 to endosomal structures, the major site of substrate lipid accumulation. All active MTMs we have tested (MTM1, MTMR2-MTMR4) reduce endosomal PtdIns3P levels upon overexpression. Despite this, only MTMR4 exerts any effect on EGF receptor trafficking and degradation, which is more pronounced with a phosphatase inactive form of MTMR4 and requires an intact FYVE domain. - Source: PubMed
Publication date: 2006/06/20
Lorenzo OscarUrbé SylvieClague Michael J - Myotubularin and myotubularin-related proteins are dual-specificity phosphatases. Several myotubularin-related proteins have been identified in humans and mice. The members of the myotubularin protein family are highly conserved, from humans to yeast. Mutations in the human myotubularin gene (MTM1) lead to X-linked myotubular myopathy. Here we isolate and localize a novel putative myotubularin-related protein gene (MTMR8) on chromosome 8p22--p23,between the markers D8S550 and D8S265, by exon-trapping experiments and RT-PCR. Genomic sequencing revealed that the gene consists of 10 exons and spans approximately 43 kb. The corresponding cDNA is 7081 bp. The open reading frame predicts a protein of 549 amino acids and a calculated molecular mass of 63 kDa. Like myotubularin-related protein-5, MTMR8 has no dual-specificity phosphatase domain. It contains a double-helical motif similar to the SET interaction domain, which is thought to have a role in the control of cell proliferation. - Source: PubMed
Appel SReichwald KZimmermann WReis ARosenthal AHennies H C