Related Experiment Video
Updated: May 22, 2026
05:58
Tissue Triage and Freezing for Models of Skeletal Muscle Disease
Published on: July 15, 2014
Myotubularin phosphoinositide phosphatases: cellular functions and disease pathophysiology
Karim Hnia1, Ilaria Vaccari, Alessandra Bolino
1Department of Translational Medicine and Neurogenetics, IGBMC (Institut de Génétique et de Biologie Moléculaire et Cellulaire), Illkirch, France.
Trends in Molecular Medicine
|May 15, 2012
Summary
Myotubularins, a family of phosphatases, are implicated in various diseases. This review highlights their diverse roles beyond membrane trafficking, including cell proliferation and cytoskeletal dynamics, offering therapeutic insights.
Area of Science:
- Biochemistry
- Cell Biology
- Molecular Medicine
Background:
- Myotubularins are phosphoinositide phosphatases linked to neuromuscular diseases, metabolic syndrome, obesity, and cancer.
- Catalytically inactive myotubularins can regulate active forms, suggesting a role in maintaining phosphatase-kinase balance.
Purpose of the Study:
- To review the diverse cellular processes regulated by myotubularins.
- To emphasize newly identified functions in physiological and pathological contexts.
- To explore potential therapeutic strategies based on myotubularin pathophysiology.
Main Methods:
- Literature review of cellular and animal models.
- Analysis of enzymatic specificity for phosphoinositides.
- Integration of findings on myotubularin functions.
Main Results:
- Myotubularins regulate endocytosis and membrane trafficking.
- Emerging roles include regulation of cell proliferation, differentiation, autophagy, cytokinesis, and cytoskeletal dynamics.
- Evidence suggests involvement in both normal physiological processes and disease states.
Conclusions:
- Myotubularins are versatile regulators of fundamental cellular processes.
- Understanding their complex roles is crucial for developing targeted therapies for associated diseases.
- Further research into myotubularin pathophysiology can unlock new treatment avenues.
More Related Videos
Related Concept Videos
02:54Protein Kinases and Phosphatases
Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
01:48ATP Synthase: Mechanism
In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased ATP...
01:22Lysosomal Hydrolases
Lysosomes are the site for the degradation of macromolecules and biological polymers released during membrane trafficking events such as secretory, endocytic, autophagic, and phagocytic pathways. The membrane-enclosed area of the lysosome, called the lumen, contains hydrolytic enzymes active in an acidic environment. These acid hydrolases are functional at a pH between 4.5 and 5 and are involved in cellular processes such as cell signaling, energy metabolism, restoration of the plasma membrane,...
01:31Types of Intermediate Filaments
The intermediate filaments are an essential component of the cytoskeleton. Presently six types of intermediate filament have been identified. Type I and II are acidic and basic keratin proteins. Type III is of mesodermal origin and comprises four proteins: vimentin, desmin, glial fibrillary acidic protein (GFAP), and peripherin. Vimentin is commonly found in mesenchymal cells, desmin in muscle cells, GFAP in astrocytes, while peripherin is found in peripheral nervous system neurons (PNS). Type...
01:22Microtubules in Signaling
The primary cilium, made up of microtubules, acts as antennae on the cell surfaces for relaying external stimuli into the cells. These fine hair-like structures are present, generally one per cell. These are non-motile cilia in a 9+0 microtubules arrangement, where the central pair of microtubules are absent. The primary cilia arise from the basal body embedded in the cell membrane. Intraflagellar transport (IFT) carries requisite proteins from the cytoplasm to the cilium because the primary...
01:24Parkinson Disease ll: Pathophysiology
Parkinson disease (PD) is a progressive neurodegenerative disorder primarily affecting movement, with additional non-motor features. Its pathophysiology involves complex interactions among genetic susceptibility, environmental exposures, and cellular dysfunction, including dopaminergic neuron loss, protein aggregation, and mitochondrial impairment.Selective NeurodegenerationA key feature is the degeneration of dopaminergic neurons in the substantia nigra pars compacta, leading to reduced...