Literature summary for 7.2.2.9 extracted from

Jain, S.; Farias, G.G.; Bonifacino, J.S.
Polarized sorting of the copper transporter ATP7B in neurons mediated by recognition of a dileucine signal by AP-1 (2015), Mol. Biol. Cell, 26, 218-228.

Search for more literature for 7.2.2.9

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
trans-Golgi network	polarized sorting of the Cu2+ transporter ATP7B to the somatodendritic domain of rat hippocampal neurons is mediated by recognition of dileucine-based signals in the cytosolic domains of the proteins by the sigma1 subunit of the clathrin adaptor AP-1. Under basal Cu2+ conditions, ATP7B is localized to the trans-Golgi network and the plasma membrane of the soma and dendrites but not the axon. Mutation of a dileucine-based signal in ATP7B or overexpression of a dominant-negative sigma1 mutant results in nonpolarized distribution of ATP7B between the somatodendritic and axonal domains. Addition of high Cu2+ concentrations causes loss of trans-Golgi network localization and somatodendritic polarity of ATP7B	Rattus norvegicus	5802	-

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
neuron	polarized sorting of the Cu2+ transporter ATP7B to the somatodendritic domain of rat hippocampal neurons is mediated by recognition of dileucine-based signals in the cytosolic domains of the proteins by the sigma1 subunit of the clathrin adaptor AP-1. Under basal Cu2+ conditions, ATP7B is localized to the trans-Golgi network and the plasma membrane of the soma and dendrites but not the axon. Mutation of a dileucine-based signal in ATP7B or overexpression of a dominant-negative sigma1 mutant results in nonpolarized distribution of ATP7B between the somatodendritic and axonal domains. Addition of high Cu2+ concentrations causes loss of trans-Golgi network localization and somatodendritic polarity of ATP7B	Rattus norvegicus	-

Synonyms

Synonyms	Comment	Organism
ATP7B	-	Rattus norvegicus

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Release 2023.1 (January 2023)