ArticleProceedings of the National Academy of Sciences of the United States of America2012
Myotubularin-related protein (MTMR) 9 determines the enzymatic activity, substrate specificity, and role in autophagy of MTMR8.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers, 2 of them syntheses that pooled it.
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Who cites it
32 citing papers in PubMed, 2 syntheses or guidelines pooled it, 62 citations in OpenAlex.
- Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)Autophagy · 2021Guideline
- Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition).Autophagy · 2016Guideline
- The multifaceted significance of phosphoinositides in endocytic trafficking.FEBS letters · 2026Review
- Mitochondrial damage triggers the concerted degradation of negative regulators of neuronal autophagy.Nature communications · 2025Article
- The Myotubularin Related Proteins and the Untapped Interaction Potential of Their Disordered C-Terminal Regions.Proteins · 2025Article
- Myotubularin 2 interacts with SEC23A and negatively regulates autophagy at ER exit sites in Arabidopsis.Autophagy · 2025Article
- HDAC1 Promotes Mitochondrial Pathway Apoptosis and Inhibits the Endoplasmic Reticulum Stress Response in High Glucose-Treated Schwann Cells via Decreased U4 Spliceosomal RNA.Neurochemical research · 2024Article
- Recent advances of myotubularin-related (MTMR) protein family in cardiovascular diseases.Frontiers in cardiovascular medicine · 2024Review
- Review
- Genome-wide association study identifies Sjögren's risk loci with functional implications in immune and glandular cells.Nature communications · 2022Article
- Activation Mechanisms of the VPS34 Complexes.Cells · 2021Review
- A conserved myotubularin-related phosphatase regulates autophagy by maintaining autophagic flux.The Journal of cell biology · 2020Article
- Myotubularin-related protein 7 activates peroxisome proliferator-activated receptor-gamma.Oncogenesis · 2020Article
- GPAT4-Generated Saturated LPAs Induce Lipotoxicity through Inhibition of Autophagy by Abnormal Formation of Omegasomes.iScience · 2020Article
- Review
- Genotype-Phenotype Correlations in Charcot-Marie-Tooth Disease Due toFrontiers in neuroscience · 2019Article
- Phosphatidylinositol Kinases and Phosphatases inFrontiers in cellular and infection microbiology · 2019Review
- Proteinaceous Regulators and Inhibitors of Protein Tyrosine Phosphatases.Molecules (Basel, Switzerland) · 2018Review
- Phosphoinositide conversion in endocytosis and the endolysosomal system.The Journal of biological chemistry · 2018Review
- High resolution chromosomal microarray analysis in paediatric obsessive-compulsive disorder.BMC medical genomics · 2017Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
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.
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