Document Type: Article All Authors / Contributors: Hnia K.; Laporte J.; Vaccari I.; Bolino A. ISSN:1471-4914 Language Note: English Unique Identifier: 795791921 Awards:
| Title | : | Myotubularin phosphoinositide phosphatases: Cellular functions and disease pathophysiology |
| Author | : | Hnia K.; Laporte J.; Vaccari I.; Bolino A. |
| Language | : | en |
| Rating | : | 4.90 out of 5 stars |
| Type | : | PDF, ePub, Kindle |
| Uploaded | : | Apr 12, 2021 |
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Mar 9, 2018 we recently identified myotubularin related protein-2 (mtmr2), a phosphoinositide (pi) phosphatase, in the native piezo2 interactome of murine.
Oct 11, 2012 myotubularin mtm1 is a phosphoinositide (ppin) 3-phosphatase mutated in x- linked centronuclear myopathy (xlcnm; myotubular myopathy).
Myotubularin removes phosphate groups from two molecules called phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-biphosphate. These molecules are found within cell membranes and are likely involved in transporting molecules within cells.
Apr 24, 2007 loss of endosomal phosphatidylinositol 3-phosphate [pi(3)p] upon overex- pression of wild-type mtm1, but not a phosphatase-dead.
The myotubularin family is a large eukaryotic group within the tyrosine/dual-specificity phosphatase super-family (ptp/dsp). Among the 14 human members, three are mutated in genetic diseases: myotubular myopathy and two forms of charcot–marie–tooth neuropathy. We present an analysis of the myotubularin family in sequenced genomes.
From wikipedia, the free encyclopedia myotubularin domain represents a region within eukaryotic myotubularin-related proteins that is sometimes found with the gram domain interpro ipr004182. Myotubularin is a dual-specific lipid phosphatase that dephosphorylates phosphatidylinositol 3-phosphate and phosphatidylinositol (3,5)-bi-phosphate.
Phosphoinositide 3-kinases and 3-phosphatases have received a special focus in volume i, and recent therapeutic developments in human disease are presented along with a historical perspective illustrating the impressive progress in the field. Volume ii extends into the role of phosphoinositides in membrane organization and vesicular traffic.
Mtm1, the gene encoding myotubularin (mtm1), is mutated in the x-linked myotubular myopathy (xlmtm), a severe genetic muscular disorder. Mtm1 is a phosphoinositide phosphatase hydrolyzing phosphatidylinositol 3-phosphate (ptdins(3)p) in yeast and in vitro. Because this lipid is implicated in the regulation of vesicular trafficking, we used established cell lines from xlmtm patients to evaluate.
Myotubularin domain represents a region within eukaryotic myotubularin-related proteins that is sometimes found with the gram domain interpro: ipr004182. Myotubularin is a dual-specific lipid phosphatase that dephosphorylates phosphatidylinositol 3-phosphate and phosphatidylinositol (3,5)-bi-phosphate.
Myotubularin-related protein 14 (mtmr14) is a novel phosphoinositide phosphatase with roles in the maintenance of normal muscle performance, autophagy, and aging in mice.
Myotubularin, a protein tyrosine phosphatase mutated in myotubular myopathy, dephosphorylates the lipid second messenger, phosphatidylinositol.
The requirement of vps34p, the sole phosphatidylinositol (pi) 3-kinase in saccharomyces cerevisiae, for protein sorting to the vacuole in yeast has exemplified.
Myotubularin-related protein 2 (mtmr2) is a member of the myotubularin family of phosphoinositide lipid phosphatases. Mtmr possesses phosphatase activity towards phosphatidylinositol-3-phosphate and phosphatidylinositol-3,5-bisphosphate.
Laporte j, blondeau f, buj-bello a, mandel jl (2001) the myotubularin family: from genetic disease to phosphoinositide metabolism. Trends genet 17:221–228 pubmed google scholar laporte j, blondeau f, gansmuller a, lutz y, vonesch jl, mandel jl (2002) the ptdins3p phosphatase myotubularin is a cytoplasmic protein that also localizes to rac1.
^ myotubularin phosphoinositide phosphatases: cellular functions and disease pathophysiology. Trends mol med 18, 317-27, (2012) view article pmid: 22578719.
Phosphatidylinositol 5-phosphate (ptdins5p) is a phosphoinositide, one of the phosphorylated derivatives of phosphatidylinositol (ptdins), that are well-established membrane-anchored regulatory molecules. Phosphoinositides participate in signaling events that control cytoskeletal dynamics, intracellular membrane trafficking, cell proliferation.
Summary the sarcoplasmic reticulum (sr) is a specialized form of endoplasmic reticulum (er) in skeletal muscle and is essential for calcium homeostasis. The mechanisms involved in sr remodeling and maintenance of sr subdomains are elusive. In this study, we identified myotubularin (mtm1), a phosphoinositide phosphatase mutated in x-linked centronuclear myopathy (xlcnm, or myotubular myopathy.
The myotubularin family of phosphoinositide phosphatases includes several members mutated in neuromuscular diseases or associated with metabolic syndrome, obesity, and cancer. Catalytically dead phosphatases regulate their active homologs by heterodimerization and potentially represent key players in the phosphatase–kinase balance.
Deregulation of phosphoinositide metabolism causes human disease. Iubmb life myotubularin homology region; ptdins, phosphatidylinositol; pi(3)p, phos-.
The myotubularins are a family of phosphoinositide 3-phosphatases preferentially hydrolyzing phosphatidylinositol.
2004 - development of a cell-based model of normal muscle development used to study the effects of myotubularin loss in xlmtm.
Recently, myotubularin, a second ptp superfamily enzyme associated with human disease, has also been shown to utilize a phosphoinositide as its physiologic substrate.
Recently, myotubularin, a second ptp superfamily enzyme associated with human disease, has also been shown to utilize a phosphoinositide as its physiologic.
Cg3530 is homologous to the human mtmr6 subfamily of myotubularin-related 3-phosphatases, and therefore, we named it dmtmr6. Dmtmr6, which is required for development and viability in drosophila, functions as a regulator of autophagic flux in multiple drosophila cell types.
Myotubularin phosphoinositide phosphatases, protein phosphatases, and kinases: their roles in junction dynamics and spermatogenesis.
Myotubularin was originally characterized as a protein tyrosine phosphatase, but was subsequently found instead to function primarily as a lipid phosphatase it acts specifically to remove phosphates from the 3-position of phosphoinositide rings.
(2000) reported that myotubularin, a protein-tyrosine phosphatase required for muscle cell differentiation, is a potent phosphatidylinositol 3-phosphate (pi3p) phosphatase. They found that mutations in the mtm1 gene that cause human myotubular myopathy dramatically reduced the ability of the phosphatase to dephosphorylate pi3p.
Deregulation of phosphoinositide metabolism causes human disease. Iubmb life, 53: 37–43, 2002 keywords myopathy; myotubularin; phosphatases; phosphoinosi-tides. Introduction membrane-anchored phosphoinositides, generated by the phosphoinositide 3-kinase1 (pi 3-kinase) enzyme family, recruit key proteins to distinct subcellular compartments.
Activator and myotubularin (gram) domain is involved in the interaction with membranes through protein and lipid interactions. Indeed, the ph-gram domains of mtm1, mtmr2 the myotubularins are a family of phosphoinositide 3-phosphatases preferentially hydrolyzing phosphatidylinositol.
Besides the epinephrine signaling pathway, another important signal transduction pathway that uses the 7tm receptors (also called g-coupled protein.
Myotubularin myotubularin domain represents a region within eukaryotic myotubularin-related myotubularin phosphatases: policing 3- phosphoinositides.
The myotubularins are a family of phosphoinositide 3-phosphatases preferentially hydrolyzing phosphatidylinositol 3-monophosphate and also phosphatidylinositol (3,5) bis-phosphate, thus generating phosphatidylinositol and phosphatidylinositol 5-monophosphate, respectively.
Pten and myotubularin phosphatases: from 3-phosphoinositide dephosphorylation to disease. Trends cell biol, 12(12):579-585, 01 dec 2002 cited by 106 articles pmid: 12495846.
Such catalytic site characterizes the myotubularin 3-phosphatases that dephosphorylate ptdins3p and ptdins(3,5)p 2 and produce.
In addition, we report that a hitherto unknown arabidopsis gene, at3g10550, encodes a phosphoinositide 3'-phosphatase related to the animal myotubularins (atmtm1). Myotubularin activities in plants have not been described and herein, we identify an overlapping set of genes co-regulated by atx1 and atmtm under drought conditions.
Phosphatidylinositol-3 phosphatase myotubularin-related protein 6 negatively regulates cd4 t cells.
Myotubularin, the gene mutated in myotubular myopathy, functions as a lipid phosphatase with specificity for ptdins (3)p. It is now apparent that there is an increasing family of proteins that are defined by their significant homology with myotubularin.
Myotubularin mtm1 is a phosphoinositide (ppin) 3-phosphatase mutated in x-linked centronuclear myopathy (xlcnm; myotubular myopathy). We investigated the involvement of mtm1 enzymatic activity on xlcnm phenotypes. Exogenous expression of human mtm1 in yeast resulted in vacuolar enlargement, as a consequence of its phosphatase activity.
Myotubularin and related proteins constitute a large and highly conserved family possessing phosphoinositide 3-phosphatase activity, although not all members possess this activity.
Coordinated phosphoinositide signaling is critical both for phagocytic particle engulfment and subsequent phagosomal maturation to a degradative organelle. Phosphatidylinositol 3-phosphate (ptdins(3)p) is a phosphoinositide that is rapidly synthesized and degraded on phagosomal membranes, where it recruits fyve domain- and px motif-containing.
Pten and myotubularin phosphoinositide phosphatases: bringing bioinformatics to the lab bench. Curr opin cell biol, 13(2):172-181, 01 apr 2001 cited by 31 articles pmid: 11248551.
The myotubularin family: novel phosphoinositide regulators - pubmed phosphatidylinositol 3-phosphate [ptdins(3)p] acts as a second messenger via the recruitment of diverse signalling proteins to various cellular compartments.
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