Purification and Characterization of the Human KDEL Receptor

Scheel, Andreas A.; Pelham, Hugh R.B.

doi:10.1021/bi960807x

Cited by 48 publications

(42 citation statements)

References 29 publications

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“…D, One milligram of each extract was incubated with Con A-Sepharose, and the bound materials were eluted with ␣-methylmannoside, resolved by SDS-PAGE, and immunoblotted with anti-AIP. retained there by continuous retrieval from a post-ER compartment, which relies on a pH-dependent interaction of the retention signal with a specific receptor (15,16). Some proteins with the KDEL retention signal were reported to be exported from the ER to plasma membranes or extracellular medium under normal conditions or by an activation-dependent mechanism (17)(18)(19).…”

Section: Aip Predominantly Localizes In the Inner Cavity Of Capsule Smentioning

confidence: 99%

Purification and Cloning of an Apoptosis-Inducing Protein Derived from Fish Infected with Anisakis simplex, a Causative Nematode of Human Anisakiasis

Jung

Mai

Iwamoto³

et al. 2000

The Journal of Immunology

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While investigating the effect of marine products on cell growth, we found that visceral extracts of Chub mackerel, an ocean fish, had a powerful and dose-dependent apoptosis-inducing effect on a variety of mammalian tumor cells. This activity was strikingly dependent on infection of the C. mackerel with the larval nematode, Anisakis simplex. After purification of the protein responsible for the apoptosis-inducing activity, we cloned the corresponding gene and found it to be a flavoprotein. This protein, termed apoptosis-inducing protein (AIP), was also found to possess an endoplasmic reticulum retention signal (C-terminal KDEL sequence) and H2O2-producing activity, indicating that we had isolated a novel reticuloplasimin with potent apoptosis-inducing activity. AIP was induced in fish only after infection with larval nematode and was localized to capsules that formed around larvae to prevent their migration to host tissues. Our results suggest that AIP may function to impede nematode infection.

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Section: Aip Predominantly Localizes In the Inner Cavity Of Capsule Smentioning

confidence: 99%

Purification and Cloning of an Apoptosis-Inducing Protein Derived from Fish Infected with Anisakis simplex, a Causative Nematode of Human Anisakiasis

Jung

Mai

Iwamoto³

et al. 2000

The Journal of Immunology

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“…Microsomal membranes, prepared as described (26), were resuspended at a final protein concentration of 1.6 mg͞ml in phosphorylation buffer containing 20 mM Hepes (pH 7.4), 0.1% (mass͞vol) Triton X-100, 10 mM MgCl 2 , 2 mM MnCl 2 , 0. 4 Ci͞ l [␥-32 P]ATP (Amersham Pharmacia, specific activity: 3,000 Ci͞mmol, final concentration of radiolabeled ATP: 0.133 M), phosphatase inhibitors (10 mM NaF, 0.1 mM Na 3 VO 4 , and 1 M okadaic acid), and protease inhibitors (10 g͞ml leupeptine, 10 g͞ml aprotinine, and 1 mM PMSF) and incubated for 30 min at room temperature.…”

Section: Phosphorylation In Vitro Of Microsomal Membrane Preparationsmentioning

confidence: 99%

The integral membrane S-locus receptor kinase of Brassica has serine/threonine kinase activity in a membranous environment and spontaneously forms oligomers in planta

Giranton¹

2000

Proceedings of the National Academy of Sciences

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To gain further insight into the mode of action of S-locus receptor kinase (SRK), a receptor-like kinase involved in the self-incompatibility response in Brassica, different recombinant SRK proteins have been expressed in a membranous environment using the insect cell͞baculovirus system. Recombinant SRK proteins exhibited properties close to those of the endogenous stigmatic SRK protein and were found to autophosphorylate on serine and threonine residues in insect cell microsomes. Autophosphorylation was constitutive because it did not require the presence of pollen or stigma extracts in the phosphorylation buffer. Phosphorylation was shown to occur in trans, suggesting the existence of constitutive homooligomers of membrane-anchored recombinant SRK. To investigate the physiological relevance of these results, we have examined the oligomeric status of SRK in planta in cross-linking experiments and by velocity sedimentation on sucrose gradients. Our data strongly suggest that SRK is associated both with other SRK molecules and other stigma proteins in nonpollinated flowers. These findings may have important implications for our understanding of self-pollen signaling. baculovirus ͉ oligomerization ͉ sporophytic self-incompatibility I n the Brassica family, the cell-cell interaction that leads to the rejection of self-pollen at the stigmatic surface [the selfincompatibility (SI) reaction] is controlled genetically by the multiallelic S-locus (1). When the pollen parent and the stigma share common S haplotypes, pollen germination or pollen tube growth is inhibited, thereby preventing self-fertilization. Several genes have been localized at the S locus but only two, the S-locus glycoprotein (SLG) and the S-locus receptor kinase (SRK) genes, exhibit the polymorphic nature expected for genes involved in the SI response (2, 3). SLG encodes a secreted glycoprotein that accumulates in the cell wall of papillae (4), whereas SRK encodes a plasmalemma-anchored glycoprotein (5, 6). SRK is structurally analogous to animal receptor kinases and belongs to the plant receptor-like kinase (RLK) family (7). Although its membrane topology has not been experimentally defined, DNA sequence analysis predicts that SRK consists of three domains: an extracellular glycosylated N-terminal domain (the S-domain) that shares extensive homology with SLG, a membrane-spanning domain, and a cytoplasmic domain (3). The cytoplasmic domain has been shown to have serine͞threonine kinase activity when expressed in bacteria (8). In the S 3 haplotype, SRK has been shown to encode, in addition to the integral membrane SRK protein, a soluble truncated form corresponding to the S-domain of SRK, the eSRK protein (9).Although there is some controversy as to whether SLG is required for the SI response (10, 11), there is strong evidence that SRK is necessary. For example, SRK was shown to be mutated in two Brassica lines that exhibited a self-compatible phenotype (12, 13). Moreover, Stahl and coworkers (14) recently have shown that the SI phenotype was altered i...

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“…Proteins that contain the 4-residue retention signal (KDEL) are found in the ER lumen and are called reticuloplasmins (Koch 1990). These proteins are transferred into the ER with the help of their signal peptide and are retained there through an interaction of the retention signal with a specific receptor (Pelham 1990, Scheel andPelham 1996). The major reticuloplasmins described to date (calreticulin, endoplasmin, protein disulfide isomerase, and BiP;Koch 1990;Lucero 1994) are all calcium-binding proteins.…”

Section: Specific Role Of the Endoplasmic Reticulum Of The Follicle Cmentioning

confidence: 99%

windbeutel,a gene required for dorsoventral patterning inDrosophila,encodes a protein that has homologies to vertebrate proteins of the endoplasmic reticulum

Konsolaki

Schüpbach

1998

Genes Dev.

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The formation of the dorsoventral axis of the Drosophila embryo depends on cell-cell interactions that take place in the female ovary and involve the activation of transmembrane receptors by secreted ligands. The gene windbeutel functions in the somatic follicle cells of the ovary and is required for the generation of a signal that will determine the ventral side of the embryo. This signal originates in the follicle cells during oogenesis, but its actions are only manifested after fertilization, when the egg has already been laid. We have performed a molecular analysis of windbeutel. We have found that windbeutel encodes a putative resident protein of the endoplasmic reticulum, and has homologs in rats and humans. The gene is expressed for a brief period of time in the follicle cells of the ovary, at around the time when the dorsoventral axis of the egg chamber is first established. We propose that Windbeutel is responsible for the folding and/or modification of a specific factor that is secreted from the follicle cells and participates in the activation of the ventralizing signal.

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Purification and Characterization of the Human KDEL Receptor

Cited by 48 publications

References 29 publications

Purification and Cloning of an Apoptosis-Inducing Protein Derived from Fish Infected with Anisakis simplex, a Causative Nematode of Human Anisakiasis

Purification and Cloning of an Apoptosis-Inducing Protein Derived from Fish Infected with Anisakis simplex, a Causative Nematode of Human Anisakiasis

The integral membrane S-locus receptor kinase of Brassica has serine/threonine kinase activity in a membranous environment and spontaneously forms oligomers in planta

windbeutel,a gene required for dorsoventral patterning inDrosophila,encodes a protein that has homologies to vertebrate proteins of the endoplasmic reticulum

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