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Article

A new class of endoplasmic reticulum export signal PhiXPhiXPhi for transmembrane proteins and its selective interaction with Sec24C.

The Journal of biological chemistry - 21 Jun 2013

Otsu Wataru, Kurooka Takao, Otsuka Yayoi, Sato Kota, Inaba Mutsumi

Abstract excerpt

Protein export from the endoplasmic reticulum (ER) depends on the interaction between a signal motif on the cargo and a cargo recognition site on the coatomer protein complex II. A hydrophobic sequence in the N terminus of the bovine anion exchanger 1 (AE1) anion exchanger facilitated the ER export of human AE1Δ11, an ER-retained AE1 mutant, through interaction with a specific Sec24 isoform. The cell surface...

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Share to Amino Acid Motifs
Share to Anion Exchange Protein 1, Erythrocyte

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Endoplasmic Reticulum

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Share to Microscopy, Confocal

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Source

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Identifiers

PMID: 23658022
DOI: 10.1074/jbc.M112.443325
PMCID: PMC3689993

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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