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

TRP-ML1 regulates lysosomal pH and acidic lysosomal lipid hydrolytic activity.

The Journal of biological chemistry - 17 Mar 2006

Soyombo Abigail A, Tjon-Kon-Sang Sandra, Rbaibi Youssef, Bashllari Enkelejda, Bisceglia Jill, Muallem Shmuel, Kiselyov Kirill

Abstract excerpt

Mucolipidosis type IV (MLIV) is caused by mutations in the ion channel mucolipin 1 (TRP-ML1). MLIV is typified by accumulation of lipids and membranous materials in intracellular organelles, which was hypothesized to be caused by the altered membrane fusion and fission events. How mutations in TRP-ML1 lead to aberrant lipolysis is not known. Here we present evidence that MLIV is a metabolic disorder that is not...

Read the complete abstract on PubMed

Topics

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

Share to Carboxylic Acids
Share to Chloroquine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Chromatography, Thin Layer

Share to Ionophores

Share to Lysosomal Storage Diseases

Share to Sterol Esterase

Share to Transient Receptor Potential Channels

Share to TRPM Cation Channels

Source

Identifiers

PMID: 16361256
DOI: 10.1074/jbc.M508211200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

TRP-ML1 regulates lysosomal pH and acidic lysosomal lipid hydrolytic activity.PMID 16361256Read ↗

TRPML1: an ion channel in the lysosome.Semantic proximity Read ↗

The cation channel mucolipin-1 is a bifunctional protein that facilitates membrane remodeling via its serine lipase domain.Semantic proximity Read ↗

Mucolipin-1 is a lysosomal membrane protein required for intracellular lactosylceramide traffic.Semantic proximity Read ↗

Molecular pathophysiology of mucolipidosis type IV: pH dysregulation of the mucolipin-1 cation channel.Semantic proximity Read ↗

TRP-ML1 is a lysosomal monovalent cation channel that undergoes proteolytic cleavage.Semantic proximity Read ↗

A potentially dynamic lysosomal role for the endogenous TRPML proteins.Semantic proximity Read ↗

Differential ion selectivity and disease-associated dysfunction of TRPML channels revealed by patient and engineered mutants.Semantic proximity Read ↗

Mitochondrial Aberrations in Mucolipidosis Type IVSemantic proximity Read ↗

Mucolipidosis type IV and the mucolipins.Semantic proximity Read ↗

Drosophila TRPML is required for TORC1 activation.Semantic proximity Read ↗

Up-regulation of lysosomal TRPML1 channels is essential for lysosomal adaptation to nutrient starvation.Semantic proximity Read ↗

Loss of TRPML1 promotes production of reactive oxygen species: is oxidative damage a factor in mucolipidosis type IV?Semantic proximity Read ↗

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