2014
DOI: 10.1074/jbc.m114.588764
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Lipase Maturation Factor 1 (Lmf1) Is Induced by Endoplasmic Reticulum Stress Through Activating Transcription Factor 6α (Atf6α) Signaling

Abstract: Background: Lipase maturation factor 1 (Lmf1) plays an important role in plasma lipid metabolism, but its regulation remains uncharacterized. Results: Endoplasmic reticulum (ER) stress induces Lmf1 expression in cell lines and mouse liver. Atf6␣ deficiency abolishes, whereas active Atf6␣ stimulates this response. Conclusion: Lmf1 is an unfolded protein response (UPR) target through Atf6␣ signaling. Significance: Lmf1 regulation by the UPR suggests a possible role in ER homeostasis.

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Cited by 13 publications
(4 citation statements)
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“…Endoplasmic reticulum is the main storage site of Ca 2+ , and any disruption in its accumulation can also promote ER stress. Studies of the relationship between calcium homeostasis and UPR activation using molecules that modify Ca 2+ storage, such as thapsigargin and tunicamycin, reveal that interference with the cation homeostasis induces the UPR response . Calcium concentrations are controlled by three transmembrane channels: Sarco (endo)plasmic reticulum Ca(2+)‐ATPase (SERCA) pumps, responsible for the influx of Ca 2+ from cytosol, ryanodine receptors (RyR), important in skeletal muscle cells, and inositol‐1,4,5‐triphosphate receptor (IP 3 R), both in charge of the cation efflux.…”
Section: The Endoplasmic Reticulum Stressmentioning
confidence: 99%
“…Endoplasmic reticulum is the main storage site of Ca 2+ , and any disruption in its accumulation can also promote ER stress. Studies of the relationship between calcium homeostasis and UPR activation using molecules that modify Ca 2+ storage, such as thapsigargin and tunicamycin, reveal that interference with the cation homeostasis induces the UPR response . Calcium concentrations are controlled by three transmembrane channels: Sarco (endo)plasmic reticulum Ca(2+)‐ATPase (SERCA) pumps, responsible for the influx of Ca 2+ from cytosol, ryanodine receptors (RyR), important in skeletal muscle cells, and inositol‐1,4,5‐triphosphate receptor (IP 3 R), both in charge of the cation efflux.…”
Section: The Endoplasmic Reticulum Stressmentioning
confidence: 99%
“…Specifically, Fam173a encodes a mitochondrial lysine-specific methyltransferase that targets adenine nucleotide translocase ( Małecki et al, 2019 ), and NADH dehydrogenase (ubiquinone) 1 beta subcomplex 10 ( Ndufb10 ) is an accessory subunit of respiratory complex I important for complex assembly ( Friederich et al, 2017 ). Lmf1 (lipase maturation factor 1) is important for regulating plasma lipid levels and responds to redox stress on the endoplasmic reticulum (ER) ( Mao et al, 2014 ). It functions as a molecular chaperone enabling proper folding and activity of ER membrane proteins.…”
Section: Resultsmentioning
confidence: 99%
“…When LMF1 expresses an unfolded protein of the response target gene, it is sufficient and necessary to activate the LMF1 promoter through activating transcription factor 6 (Atf6) signaling. Most importantly, induction of LMF1 appears not restricted to lipase-expressing cells but to be a common phenomenon caused by ER stress [ 21 ]. ER stress has a synergistic contribution to EGFR inhibitor gefitinib-induced apoptosis in glioma.…”
Section: Resultsmentioning
confidence: 99%