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1.
iScience ; 26(7): 107250, 2023 Jul 21.
Artigo em Inglês | MEDLINE | ID: mdl-37485344

RESUMO

The giant clam Tridacna crocea thrives in poorly nourished coral reef water by forming a holobiont with zooxanthellae and utilizing photosynthetic products of the symbiont. However, detailed metabolic crosstalk between clams and symbionts is elusive. Here, we discovered that the nonphosphorous microalgal betaine lipid DGCC (diacylglycerylcarboxy-hydroxymethylcholine) and its deacylated derivative GCC are present in all tissues and organs, including algae-free sperm and eggs, and are metabolized. Colocalization of DGCC and PC (phosphatidylcholine) evidenced by MS imaging suggested that DGCC functions as a PC substitute. The high content of GCC in digestive diverticula (DD) suggests that the algal DGCC was digested in DD for further utilization. Lipidomics analysis showing the organ-specific distribution pattern of DGCC species suggests active utilization of DGCC as membrane lipids in the clam. Thus, the utilization of zooxanthellal DGCC in animal cells is a unique evolutionary outcome in phosphorous-deficient coral reef waters.

2.
Genes Cells ; 18(9): 798-809, 2013 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-23803178

RESUMO

The unfolded protein response (UPR) is an adaptive stress response that responds to the accumulation of unfolded proteins in the lumen of the endoplasmic reticulum (ER) and that adjusts the protein-folding capacity to the needs of the cell. Perturbation of cellular lipids also activates the UPR. Lipid-induced UPR has attracted much attention because it is associated with the pathology of some metabolic diseases. However, how the lipid-induced UPR is activated remains unclear. We previously showed that palmitic acid treatment or knockdown of stearoyl-CoA desaturase in HeLa cells promotes membrane lipid saturation and activates the UPR. In this study, we compared UPR activation by membrane lipid saturation with UPR activation by conventional ER stressors that cause the accumulation of unfolded proteins such as tunicamycin and thapsigargin. Membrane lipid saturation induced autophosphorylation of inositol-requiring 1α (IRE1α) and protein kinase RNA-like ER kinase, but not the conversion of activating transcription factor-6α to the active form. A conventional ER stressor induced clustering of fluorescently tagged IRE1α fusion protein, but palmitic acid treatment did not, suggesting that IRE1α was activated without large cluster formation by membrane lipid saturation. Together, these results suggest membrane lipid saturation, and unfolded proteins activate the UPR through different mechanisms.


Assuntos
Endorribonucleases/metabolismo , Lipídeos de Membrana/metabolismo , Proteínas de Membrana/metabolismo , Proteínas Serina-Treonina Quinases/metabolismo , Resposta a Proteínas não Dobradas , Fator 6 Ativador da Transcrição/metabolismo , Estresse do Retículo Endoplasmático , Células HeLa , Humanos , Ácido Palmítico/farmacologia , Desdobramento de Proteína/efeitos dos fármacos , Tapsigargina/farmacologia , Tunicamicina/farmacologia , eIF-2 Quinase/metabolismo
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