Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The PtdIns3-phosphatase MTMR3 interacts with mTORC1 and suppresses its activity.

FEBS letters - 1 Jan 2016

Hao Feike, Itoh Takashi, Morita Eiji, Shirahama-Noda Kanae, Yoshimori Tamotsu, Noda Takeshi

Abstract excerpt

Macroautophagy is a major intracellular degradation system. We previously reported that overexpression of phosphatase-deficient MTMR3, a member of the myotubularin phosphatidylinositol (PI) 3-phosphatase family, leads to induction of autophagy. In this study, we found that MTMR3 interacted with mTORC1, an evolutionarily conserved serine/threonine kinase complex, which regulates cell growth and autophagy in...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Autophagy
Share to Catalytic Domain
Share to Embryo, Mammalian

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mechanistic Target of Rapamycin Complex 1

Share to Multiprotein Complexes

Share to Protein Interaction Domains and Motifs

Share to Protein Tyrosine Phosphatases, Non-Receptor

Share to TOR Serine-Threonine Kinases

Source

Open in PubMed Open full text

Identifiers

PMID: 26787466
DOI: 10.1002/1873-3468.12048
PMCID: PMC5064752

Genes

MTMR3

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The PtdIns3-phosphatase MTMR3 interacts with mTORC1 and suppresses its activity.PMID 26787466Read ↗

Rab35-regulated lipid turnover by myotubularins represses mTORC1 activity and controls myelin growth.Semantic proximity Read ↗

Phosphatidylinositol 3-phosphatase myotubularin-related protein 6 (MTMR6) is regulated by small GTPase Rab1B in the early secretory and autophagic pathways.Semantic proximity Read ↗

The CMT4B disease-causing phosphatases Mtmr2 and Mtmr13 localize to the Schwann cell cytoplasm and endomembrane compartments, where they depend upon each other to achieve wild-type levels of protein expression.Semantic proximity Read ↗

Phosphatidylinositol-5-phosphate activation and conserved substrate specificity of the myotubularin phosphatidylinositol 3-phosphatases.Semantic proximity Read ↗

Analysis of phosphoinositide binding domain properties within the myotubularin-related protein MTMR3.Semantic proximity Read ↗

Myotubularin and MTMR2, phosphatidylinositol 3-phosphatases mutated in myotubular myopathy and type 4B Charcot-Marie-Tooth disease.Semantic proximity Read ↗

The PTEN and Myotubularin phosphoinositide 3-phosphatases: linking lipid signalling to human disease.Semantic proximity Read ↗

MTMR regulates KRAS function by controlling plasma membrane levels of phospholipidsSemantic proximity Read ↗

PIP4kγ is a substrate for mTORC1 that maintains basal mTORC1 signaling during starvation.Semantic proximity Read ↗

Loss of phosphatase activity in myotubularin-related protein 2 is associated with Charcot-Marie-Tooth disease type 4B1.Semantic proximity Read ↗

Phosphatidylinositol 4-kinases are required for autophagic membrane trafficking.Semantic proximity Read ↗

Differential phosphorylation of the phosphoinositide 3-phosphatase MTMR2 regulates its association with early endosomal subtypes.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.