The cell surface trafficking of PDIA1, PDIA3, and PDIA6 is dependent on KDELR1, which travels in a dynamic manner to the cell surface. This transport is assumed to result in PDI cell surface association, which differs from PDI inducible secretion into the extracellular space.
Data show that Golgi-based, KDEL receptor-dependent signalling promotes lysosome repositioning to the perinuclear area, involving a complex process intertwined to autophagy, lipid-droplet turnover and Golgi-mediated secretion.
KDELR protein mediated the intracellular trafficking of Japanese encephalitis virus particles.
A Golgi-based KDELR-dependent signalling pathway controls invadopodia-dependent extracellular matrix degradation.
We propose a model whereby in analogy to previous findings (e.g., the RAS-RAF signalling pathway), PHB can act as a signalling scaffold protein to assist in KDELR-dependent Src activation
It discuss the particular role of KDEL receptor signaling in the regulation of important pathways involved in the maintenance of the homeostasis of the transport apparatus, and in particular, of the Golgi complex.
KDEL receptor activates CREB1 and other transcription factors that upregulate transport-related genes
These findings reveal an unexpected GPCR-like mode of action of the KDEL-R and shed light on a core molecular control mechanism of intra-Golgi traffic.
our data provide evidence that KDELR, as a novel inducer of autophagy, participates in the degradation of misfolded neurodegenerative disease-related proteins.
Cystinosin, MPDU1, SWEETs and KDELR belong to a well-defined protein family with putative function of cargo receptors.
the KDEL receptor participates in the ER stress response not only by its retrieval ability but also by modulating MAP kinase signaling
Src relocated the KDEL receptor (KDEL-R) from the Golgi apparatus to the endoplasmic reticulum
In a mouse line having nonfunctional KDELR1, polyclonal naive T cells show excessive integrated stress responses, which are rescued by strong TCR-mediated signaling
regulates naive T-cell homeostasis by controlling integrated stress responses
present a recessive mouse missense allele of the prototypical mammalian KDEL receptor, KDEL ER protein retention receptor 1 (KDELR1). Kdelr1 homozygous mutants were mildly lymphopenic, as were mice with a CRISPR/Cas9-engineered frameshift allele
dilated cardiomyopathy found in the mutant KDEL receptor transgenic mice is associated with ER stress
Retention of resident soluble proteins in the lumen of the endoplasmic reticulum (ER) is achieved in both yeast and animal cells by their continual retrieval from the cis-Golgi, or a pre-Golgi compartment. Sorting of these proteins is dependent on a C-terminal tetrapeptide signal, usually lys-asp-glu-leu (KDEL) in animal cells, and his-asp-glu-leu (HDEL) in S. cerevisiae. This process is mediated by a receptor that recognizes, and binds the tetrapeptide-containing protein, and returns it to the ER. In yeast, the sorting receptor encoded by a single gene, ERD2, which is a seven-transmembrane protein. Unlike yeast, several human homologs of the ERD2 gene, constituting the KDEL receptor gene family, have been described. The protein encoded by this gene was the first member of the family to be identified, and it encodes a protein structurally and functionally similar to the yeast ERD2 gene product.
ER lumen protein retaining receptor 1
, KDEL endoplasmic reticulum protein retention receptor 1
, KDEL receptor 1
, putative MAPK-activating protein PM23