TM9/Phg1 and SadA proteins control surface expression and stability of SibA adhesion molecules inDictyostelium

Froquet, Romain Bruno; Coadic, Marion Le; Perrin, Jackie; Cherix, Nathalie; Cornillon, Sophie; Cosson, Pierre

doi:10.1091/mbc.e11-04-0338

Cited by 30 publications

(48 citation statements)

References 26 publications

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“…In a recent study, we have shown that Phg1A controls the cellular amounts of SibA, a protein involved in cellular adhesion [6]. In phg1a KO cells, SibA is produced less efficiently and degraded more readily than in WT cells [6].…”

Section: Resultsmentioning

confidence: 98%

“…Remarkably, TM9 proteins also play an important role in adhesion in yeast [3] and Drosophila [4], and their overexpression in human metastatic melanoma cells conferred the pathogenic ability to engulf neighboring cells [5]. In a recent study, we showed that in Dictyostelium , Phg1A participates in cell adhesion by controlling the surface expression of SibA adhesion molecules [6].…”

Section: Introductionmentioning

confidence: 99%

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Phg1/TM9 Proteins Control Intracellular Killing of Bacteria by Determining Cellular Levels of the Kil1 Sulfotransferase in Dictyostelium

Coadic¹,

Froquet²,

Lima³

et al. 2013

PLoS ONE

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Dictyostelium discoideum has largely been used to study phagocytosis and intracellular killing of bacteria. Previous studies have shown that Phg1A, Kil1 and Kil2 proteins are necessary for efficient intracellular killing of Klebsiella bacteria. Here we show that in phg1a KO cells, cellular levels of lysosomal glycosidases and lysozyme are decreased, and lysosomal pH is increased. Surprisingly, overexpression of Kil1 restores efficient killing in phg1a KO cells without correcting these lysosomal anomalies. Conversely, kil1 KO cells are defective for killing, but their enzymatic content and lysosomal pH are indistinguishable from WT cells. The killing defect of phg1a KO cells can be accounted for by the observation that in these cells the stability and the cellular amount of Kil1 are markedly reduced. Since Kil1 is the only sulfotransferase characterized in Dictyostelium, an (unidentified) sulfated factor, defective in both phg1a and kil1 KO cells, may play a key role in intracellular killing of Klebsiella bacteria. In addition, Phg1B plays a redundant role with Phg1A in controlling cellular amounts of Kil1 and intracellular killing. Finally, cellular levels of Kil1 are unaffected in kil2 KO cells, and Kil1 overexpression does not correct the killing defect of kil2 KO cells, suggesting that Kil2 plays a distinct role in intracellular killing.

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Section: Resultsmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

Phg1/TM9 Proteins Control Intracellular Killing of Bacteria by Determining Cellular Levels of the Kil1 Sulfotransferase in Dictyostelium

Coadic¹,

Froquet²,

Lima³

et al. 2013

PLoS ONE

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“…The stability of SibA as well as its expression on the surface was found to be dependent on two other membrane proteins, SadA and Phg1A [12]. Several studies also showed that cells lacking SadA, Pgh1A and talin had reduced substratum adhesion [10]–[19].…”

Section: Introductionmentioning

confidence: 99%

Cell Substratum Adhesion during Early Development of Dictyostelium discoideum

et al. 2014

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Vegetative and developed amoebae of Dictyostelium discoideum gain traction and move rapidly on a wide range of substrata without forming focal adhesions. We used two independent assays to quantify cell-substrate adhesion in mutants and in wild-type cells as a function of development. Using a microfluidic device that generates a range of hydrodynamic shear stress, we found that substratum adhesion decreases at least 10 fold during the first 6 hr of development of wild type cells. This result was confirmed using a single-cell assay in which cells were attached to the cantilever of an atomic force probe and allowed to adhere to untreated glass surfaces before being retracted. Both of these assays showed that the decrease in substratum adhesion was dependent on the cAMP receptor CAR1 which triggers development. Vegetative cells missing talin as the result of a mutation in talA exhibited slightly reduced adhesive properties compared to vegetative wild-type cells. In sharp contrast to wild-type cells, however, these talA mutant cells did not show further reduction of adhesion during development such that after 5 hr of development they were significantly more adhesive than developed wild type cells. In addition, both assays showed that substrate adhesion was reduced in 0 hr cells when the actin cytoskeleton was disrupted by latrunculin. Consistent with previous observations, substrate adhesion was also reduced in 0 hr cells lacking the membrane proteins SadA or SibA as the result of mutations in sadA or sibA. However, there was no difference in the adhesion properties between wild type AX3 cells and these mutant cells after 6 hr of development, suggesting that neither SibA nor SadA play an essential role in substratum adhesion during aggregation. Our results provide a quantitative framework for further studies of cell substratum adhesion in Dictyostelium.

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“…In Dictyostelium, TM9SF4/Phg1A is required for the phagocytosis and killing of bacteria [16,22,23]. Moreover, the two Dictyostelium TM9 proteins Phg1A and Phg1B synergistically contribute to the expression and/or localization of transmembrane proteins [14,24]. The function of TM9SF4 in phagocytosis is conserved in human immune cells, where TM9SF4 overexpression contributes to enhanced phagocytic activity of metastatic tumour cells [13,25], and in Drosophila [15,26].…”

Section: Introductionmentioning

confidence: 99%

The Nonaspanins TM9SF2 and TM9SF4 Regulate the Plasma Membrane Localization and Signalling Activity of the Peptidoglycan Recognition Protein PGRP-LC in Drosophila

Perrin¹,

Mortier²,

Jacomin³

et al. 2014

J Innate Immun

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Transmembrane 9 (TM9) proteins, or nonaspanins, are a family of proteins conserved throughout evolution and characterized by 9 transmembrane domains. In Drosophila, TM9 superfamily protein member 4 (TM9SF4) and its closest paralogue, TM9SF2, contribute to phagocytosis of various types of particles, while TM9SF4 displays non-redundant requirement in Gram-negative bacteria engulfment. In addition, the two TM9 proteins control the actin cytoskeleton in larval haemocytes and in Drosophila S2 cells. Here, we show that TM9SF4 and TM9SF2 co-immunoprecipitate with the peptidoglycan recognition protein (PGRP)-LC, which triggers the Drosophila immune response to bacterial infection. Furthermore, both TM9 proteins co-localize with this receptor in intracellular vesicles and at the plasma membrane in Drosophila S2 cells in culture and in the fly fat body. Silencing TM9SF4 prevents plasma membrane localization of PGRP-LC, whereas silencing TM9SF2 does not, which may account for the non-redundant role of TM9SF4 in phagocytosis of Gram-negative bacteria. Finally, we provide a set of data suggesting that TM9 proteins can prevent inappropriate signalling from the unstimulated receptor.

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TM9/Phg1 and SadA proteins control surface expression and stability of SibA adhesion molecules inDictyostelium

Cited by 30 publications

References 26 publications

Phg1/TM9 Proteins Control Intracellular Killing of Bacteria by Determining Cellular Levels of the Kil1 Sulfotransferase in Dictyostelium

Phg1/TM9 Proteins Control Intracellular Killing of Bacteria by Determining Cellular Levels of the Kil1 Sulfotransferase in Dictyostelium

Cell Substratum Adhesion during Early Development of Dictyostelium discoideum

The Nonaspanins TM9SF2 and TM9SF4 Regulate the Plasma Membrane Localization and Signalling Activity of the Peptidoglycan Recognition Protein PGRP-LC in <b><i>Drosophila</i></b>

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