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#KDEL signal

2 public questions tagged with this topic.

Protein Sorting and Trafficking

The ER retention signal KDEL is recognized by:

Retention and retrieval of escaped ER resident proteins depends on pH-sensitive recognition of C-terminal retention signal by cycling receptor Erd2 localized predominantly in cis-Golgi and ER-Golgi intermediate compartment but trafficking constitutively. Human KDEL receptor family comprises three isoforms KDELR1-3 sharing seven-transmembrane architecture with lumenal binding pocket formed by polar residues and conserved histidine that at acidic pH around 6.2 characteristic of Golgi protonates enhancing affinity for Lys-Asp-Glu-Leu tetrapeptide and variants HDEL, RDEL. Ligand binding induces co

Ref: Munro & Pelham, Cell 48: 1987, KDEL Receptor Erd2 Recognizing KDEL Signal.

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Protein Sorting and Trafficking

Proteins with the KDEL signal are retrieved from:

Lumenal residents of endoplasmic reticulum that perform folding, such as BiP/GRP78, protein disulfide isomerase, calreticulin and Grp94, must be retained despite continuous bulk flow to Golgi. Retention is achieved by C-terminal tetrapeptide KDEL or variants HDEL in yeast for soluble proteins and Lys-Lys-X-X or Arg-X-Arg motifs for type I membrane proteins. Escaped proteins reach cis-Golgi and ER-Golgi intermediate compartment where seven-transmembrane KDEL receptor Erd2, actually three isoforms KDELR1-3 in mammals, cycles constitutively between ER and Golgi. At mildly acidic Golgi pH near 6.2

Ref: Alberts et al., Molecular Biology of the Cell, 6th ed., Chapter 12: KDEL Retrieval via Erd2 and COPI Vesicles.

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