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

I-proteins - a proposed switch in myotubularin function.

Trends in biochemical sciences - 1 Feb 2004

Clague Michael J, Dove Stephen K, Barr Francis A

Abstract excerpt

In this article, we consider the functions of the myotubularins - a large family of phosphoinositide 3-phosphatases. By analogy with the phosphatidylinositol 3-phosphatase PTEN (phosphatase and tensin homolog deleted in chromosome ten) and many protein phosphatases, it has been proposed that the primary function of this protein family is to regulate substrate levels, in this case phosphatidylinositol...

Read the complete abstract on PubMed

Topics

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

Share to Endocytosis
Share to Enzyme Activation
Share to Feedback, Physiological

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Phosphatidylinositol Phosphates

Share to Phosphoric Monoester Hydrolases

Share to Protein Tyrosine Phosphatases

Share to Protein Tyrosine Phosphatases, Non-Receptor

Share to Tumor Suppressor Proteins

Source

Identifiers

PMID: 15102431
DOI: 10.1016/j.tibs.2003.12.005

Genes

PTEN

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

I-proteins - a proposed switch in myotubularin function.PMID 15102431Read ↗

The myotubularin family: novel phosphoinositide regulators.Semantic proximity Read ↗

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

The myotubularin family: from genetic disease to phosphoinositide metabolism.Semantic proximity Read ↗

Interplay between myotubularins and Ca2+ homeostasis.Semantic proximity Read ↗

The structure and regulation of myotubularin phosphatases.Semantic proximity Read ↗

PTEN and Myotubularin: Novel Phosphoinositide PhosphatasesSemantic proximity Read ↗

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

The role of PTEN as a PI(3,4)P2 lipid phosphatase in Class I phosphoinositide 3-kinase signallingSemantic proximity Read ↗

Phosphatidylinositol-3,5-bisphosphate: metabolism and physiological functions.Semantic proximity Read ↗

Identification of myotubularin as the lipid phosphatase catalytic subunit associated with the 3-phosphatase adapter protein, 3-PAP.Semantic proximity Read ↗

The PtdIns3P phosphatase myotubularin is a cytoplasmic protein that also localizes to Rac1-inducible plasma membrane ruffles.Semantic proximity Read ↗

The Genetic Background of Abnormalities in Metabolic Pathways of Phosphoinositides and Their Linkage with the Myotubular Myopathies, Neurodegenerative Disorders, and CarcinogenesisSemantic proximity Read ↗

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