The Cell Adhesion Molecule Retina Cognin Is a Cell Surface Protein Disulfide Isomerase That Uses Disulfide Exchange Activity to Modulate Cell Adhesion

Pariser, Harold; Zhang, Jun; Hausman, Robert E.

doi:10.1006/excr.2000.4931

Cited by 16 publications

(14 citation statements)

References 38 publications

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“…A cognin-like protein is also recruited to the membrane in the presence of 3-oxo-C 12 -HSL. This membrane protein intervenes in cell aggregation thanks to its disulfide isomerase activity, which creates temporary covalent links with membrane proteins of the other cells [50], [51]. Some data demonstrate that some sponge-associated bacteria possess proteins with eukaryotic protein-protein interaction domains [5].…”

Section: Discussionmentioning

confidence: 99%

Cellular Effects of Bacterial N-3-Oxo-Dodecanoyl-L-Homoserine Lactone on the Sponge Suberites domuncula (Olivi, 1792): Insights into an Intimate Inter-Kingdom Dialogue

et al. 2014

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Sponges and bacteria have lived together in complex consortia for 700 million years. As filter feeders, sponges prey on bacteria. Nevertheless, some bacteria are associated with sponges in symbiotic relationships. To enable this association, sponges and bacteria are likely to have developed molecular communication systems. These may include molecules such as N-acyl-L-homoserine lactones, produced by Gram-negative bacteria also within sponges. In this study, we examined the role of N-3-oxododecanoyl-L-homoserine lactone (3-oxo-C12-HSL) on the expression of immune and apoptotic genes of the host sponge Suberites domuncula. This molecule seemed to inhibit the sponge innate immune system through a decrease of the expression of genes coding for proteins sensing the bacterial membrane: a Toll-Like Receptor and a Toll-like Receptor Associated Factor 6 and for an anti-bacterial perforin-like molecule. The expression of the pro-apoptotic caspase-like 3/7 gene decreased as well, whereas the level of mRNA of anti-apoptotic genes Bcl-2 Homolog Proteins did not change. Then, we demonstrated the differential expression of proteins in presence of this 3-oxo-C12-HSL using 3D sponge cell cultures. Proteins involved in the first steps of the endocytosis process were highlighted using the 2D electrophoresis protein separation and the MALDI-TOF/TOF protein characterization: α and β subunits of the lysosomal ATPase, a cognin, cofilins-related proteins and cytoskeleton proteins actin, α tubulin and α actinin. The genetic expression of some of these proteins was subsequently followed. We propose that the 3-oxo-C12-HSL may participate in the tolerance of the sponge apoptotic and immune systems towards the presence of bacteria. Besides, the sponge may sense the 3-oxo-C12-HSL as a molecular evidence of the bacterial presence and/or density in order to regulate the populations of symbiotic bacteria in the sponge. This study is the first report of a bacterial secreted molecule acting on sponge cells and regulating the symbiotic relationship.

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Section: Discussionmentioning

confidence: 99%

Cellular Effects of Bacterial N-3-Oxo-Dodecanoyl-L-Homoserine Lactone on the Sponge Suberites domuncula (Olivi, 1792): Insights into an Intimate Inter-Kingdom Dialogue

et al. 2014

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“…A clear‐cut example of intervention of PDI in cell adhesion has been found in retina cells from chicken embryo, where a protein of the cell surface called R‐cognin, responsible for adhesion (Hausman and Moscona, 1975), was later found to be identical to PDI (Krishna Rao and Hausman, 1993; Pariser et al, 2000). Moreover, its adhesion property required the integrity of the thioredoxin‐like active site.…”

Section: Secretion and Location On Cell Surfacementioning

confidence: 99%

Proteins of the PDI family: Unpredicted non‐ER locations and functions

Turano

Coppari

Altieri

et al. 2002

Journal Cellular Physiology

474

395

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Protein disulfide isomerases (PDIs) constitute a family of structurally related enzymes which catalyze disulfide bonds formation, reduction, or isomerization of newly synthesized proteins in the lumen of the endoplasmic reticulum (ER). They act also as chaperones, and are, therefore, part of a quality-control system for the correct folding of the proteins in the same subcellular compartment. While their functions in the ER have been thoroughly studied, much less is known about their roles in non-ER locations, where, however, they have been shown to be involved in important biological processes. At least three proteins of this family from higher vertebrates have been found in unusual locations (i.e., the cell surface, the extracellular space, the cytosol, and the nucleus), reached through an export mechanism which has not yet been understood. In some cases their function in the non-ER location is clearly related to their redox properties, but in most cases their mechanism of action has still to be disclosed, although their propensity to associate with other proteins or even with DNA might be the main factor responsible for their activities.

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“…However, there is accumulating evidence that, similarly to RB60, additional PDI-like proteins might also carry out other biological functions and that they may reside in additional subcellular compartments. Regulatory roles have been proposed for PDIs on the extracellular face of a number of cell types (10)(11)(12)(13), in nuclei of maturing spermatids (14), associated with the nuclear matrix in chicken liver cells (15), and probably also in mitochondria (16). Markedly, RB60 is the sole PDI gene identified thus far in the C. reinhardtii genome (www.ncbi.nlm.nih.gov), thus raising the possibility that it might also function as the essential ER PDI.…”

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confidence: 99%

Dual targeting of the protein disulfide isomerase RB60 to the chloroplast and the endoplasmic reticulum

Levitan

Trebitsh

Kiss

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

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RB60 is an atypical protein disulfide isomerase (PDI) that functions as a member of a redox regulatory protein complex controlling translation in the chloroplast of Chlamydomonas reinhardtii, but also contains a C-terminal endoplasmic reticulum (ER) retention signal, -KDEL. Here, we show by fluorescence microscopy that RB60 resides in the chloroplast but also outside of the chloroplast colocalized with BiP, an ER marker protein. RB60 accumulates in microsomes that exhibit a typical ER magnesium-shift, and cotranslationally translocates into ER microsomes. The first 50-aa leader of RB60 is sufficient for both chloroplast and ER targeting. The leader is cleaved upon translocation into the ER, whereas it remains intact after import to the chloroplast. The leader sequence also contains an acidic domain that appears necessary for the protein's association with the thylakoid membranes. Based on these and additional results, we propose that the dual localization of RB60 occurs via the two conserved transport mechanisms, to the chloroplast and to the ER, that the chloroplast RB60 most likely carries an additional function in the ER, and that its mode of transport, including the differential cleavage of its N terminus, plays an important role in its suborganellar localization and organellarspecific function.dual subcellular localization ͉ redox-responsive regulator ͉ membrane association ͉ GFP

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The Cell Adhesion Molecule Retina Cognin Is a Cell Surface Protein Disulfide Isomerase That Uses Disulfide Exchange Activity to Modulate Cell Adhesion

Cited by 16 publications

References 38 publications

Cellular Effects of Bacterial N-3-Oxo-Dodecanoyl-L-Homoserine Lactone on the Sponge Suberites domuncula (Olivi, 1792): Insights into an Intimate Inter-Kingdom Dialogue

Cellular Effects of Bacterial N-3-Oxo-Dodecanoyl-L-Homoserine Lactone on the Sponge Suberites domuncula (Olivi, 1792): Insights into an Intimate Inter-Kingdom Dialogue

Proteins of the PDI family: Unpredicted non‐ER locations and functions

Dual targeting of the protein disulfide isomerase RB60 to the chloroplast and the endoplasmic reticulum

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