Results 151 to 160 of about 2,993 (188)
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Functional Redundancy in the Myotubularin Family
Biochemical and Biophysical Research Communications, 2002Myotubularin-related genes define a novel highly conserved family of eukaryotic proteins of at least 11 human members. The hMTM1 gene that codes for myotubularin is mutated in X-linked myotubular myopathy, a severe congenital disease. Recently, we and others have characterized myotubularin as a potent and specific phosphatidylinositol 3-phosphate 3 ...
Jocelyn Laporte +2 more
exaly +3 more sources
Myotubularin Functions Through Actomyosin to Interact With the Hippo Pathway
The Hippo pathway is an evolutionarily conserved developmental pathway that controls organ size by integrating diverse regulatory inputs, including actomyosin-mediated cytoskeletal tension. Despite established connections between the actomyosin cytoskeleton and the Hippo pathway, the upstream regulation of actomyosin in the Hippo pathway is less ...
Jianzhong Yu, Yulan Xiong, Qinfang Liu
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The Myotubularin Family: Novel Phosphoinositide Regulators [PDF]
AbstractPhosphatidylinositol 3‐phosphate [PtdIns(3)P] acts as a second messenger via the recruitment of diverse signalling proteins to various cellular compartments. Recent advances have highlighted the association of human diseases with mutations in phosphatases that regulate PtdIns(3)P levels.
Harshal H, Nandurkar, Richard, Huysmans
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The Myotubularin Family: From Genetic Disease to Phosphoinositide Metabolism
Trends in Genetics, 2001The myotubularin-related genes define a large family of eukaryotic proteins, most of them initially characterized by the presence of a ten-amino acid consensus sequence related to the active sites of tyrosine phosphatases, dual-specificity protein phosphatases and the lipid phosphatase PTEN.
Jocelyn Laporte +2 more
exaly +4 more sources
The Myotubularin Family of Lipid Phosphatases
Traffic, 2005The myotubularins (MTMs) constitute a large family of phosphoinositide lipid 3‐phosphatases with specificity for PtdIns3 P and PtdIns (3,5) P 2 .
Michael J, Clague, Oscar, Lorenzo
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Implication of Phosphoinositide Phosphatases in Genetic Diseases: The Case of Myotubularin
Cellular and Molecular Life Sciences, 2003Phosphoinositides play a central role in the control of major eukaryotic cell signaling mechanisms. Accordingly, the list of phosphoinositide-metabolizing enzymes implicated in human diseases has considerably increased these last years. Here we will focus on myotubularin, the protein mutated in the X-linked myotubular myopathy (XLMTM) and the founding ...
Bernard Payrastre +2 more
exaly +3 more sources
The structure and regulation of myotubularin phosphatases
Current Opinion in Structural Biology, 2005The human neuromuscular diseases X-linked myotubular myopathy and Charcot-Marie-Tooth disease type 4B are caused by mutations in myotubularin family proteins. The myotubularins are a unique subfamily of protein tyrosine phosphatases that utilize inositol phospholipids, rather than phosphoproteins, as substrates. Recent structural studies, including the
Michael J, Begley, Jack E, Dixon
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The Myotubularin-Amphiphysin 2 Complex in Membrane Tubulation and Centronuclear Myopathies. [PDF]
Myotubularin (MTM1) and amphiphysin 2 (BIN1) are two proteins mutated in different forms of centronuclear myopathy, but the functional and pathological relationship between these two proteins was unknown. Here, we identified MTM1 as a novel binding partner of BIN1, both in vitro and endogenously in skeletal muscle. Moreover, MTM1 enhances BIN1-mediated
Karim Hnia +2 more
exaly +4 more sources
Myotubularin phosphatases: policing 3-phosphoinositides
Trends in Cell Biology, 2006In eukaryotic cells, phosphatidylinositol is subject to differential phosphorylation, resulting in the production of seven distinct phosphatidylinositol phosphates, often referred to as phosphoinositides (PIs). PIs have numerous distinct roles in cellular regulation and membrane trafficking.
Fred L, Robinson, Jack E, Dixon
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PTEN and Myotubularin: Novel Phosphoinositide Phosphatases
Annual Review of Biochemistry, 2001▪ Abstract Protein tyrosine phosphatases (PTPs) are a diverse group of enzymes that contain a highly conserved active site motif, Cys-x5-Arg (Cx5R). The PTP super-family enzymes, which include tyrosine-specific, dual specificity, low-molecular-weight, and Cdc25 phosphatases, are key mediators of a wide variety of cellular processes, including growth,
T, Maehama, G S, Taylor, J E, Dixon
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