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

Studies on endocytic mechanisms of the Menkes copper-translocating P-type ATPase (ATP7A; MNK). Endocytosis of the Menkes protein.

Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine - 1 Feb 2004

Lane Cinnamon, Petris Michael J, Benmerah Alexandre, Greenough Mark, Camakaris James

Abstract excerpt

The human X-linked recessive copper deficiency disorder, Menkes disease, is caused by mutations in the ATP7A (MNK) gene, which encodes a transmembrane copper-transporting P-type ATPase (MNK). The MNK protein is localised to the Golgi apparatus and relocalises to the plasma membrane when copper levels are elevated. Previous studies have identified a C-terminal di-leucine endocytic motif (L1487L1488) in MNK,...

Read the complete abstract on PubMed

Topics

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

Share to Calcium-Binding Proteins
Share to Cation Transport Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Clathrin

Share to Copper

Share to Copper-Transporting ATPases

Share to Endocytosis

Share to Leucine

Share to Lysine

Source

Identifiers

PMID: 14977365
DOI: 10.1023/a:1024413631537

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

Studies on endocytic mechanisms of the Menkes copper-translocating P-type ATPase (ATP7A; MNK). Endocytosis of the Menkes protein.PMID 14977365Read ↗

The Menkes disease ATPase (ATP7A) is internalized via a Rac1-regulated, clathrin- and caveolae-independent pathway.Semantic proximity Read ↗

A C-terminal di-leucine is required for localization of the Menkes protein in the trans-Golgi network.Semantic proximity Read ↗

Signals regulating trafficking of Menkes (MNK; ATP7A) copper-translocating P-type ATPase in polarized MDCK cells.Semantic proximity Read ↗

Trafficking of the copper-ATPases, ATP7A and ATP7B: role in copper homeostasis.Semantic proximity Read ↗

Characterization of the Menkes protein copper-binding domains and their role in copper-induced protein relocalization.Semantic proximity Read ↗

Menkes disease.Semantic proximity Read ↗

The Menkes copper transporter is required for the activation of tyrosinase.Semantic proximity Read ↗

Characterization of ATP7A missense mutants suggests a correlation between intracellular trafficking and severity of Menkes disease.Semantic proximity Read ↗

Protein kinase-dependent phosphorylation of the Menkes copper P-type ATPase.Semantic proximity Read ↗

Wilson disease protein ATP7B utilizes lysosomal exocytosis to maintain copper homeostasis.Semantic proximity Read ↗

A conditional mutation affecting localization of the Menkes disease copper ATPase. Suppression by copper supplementation.Semantic proximity Read ↗

Mutation in the CPC motif-containing 6th transmembrane domain affects intracellular localization, trafficking and copper transport efficiency of ATP7A protein in mosaic mutant mice--an animal model of Menkes disease.Semantic proximity Read ↗

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