The DOI matches its Crossref record; 19 of the 19 references it cites were found in a registry or an index; none of the 10 sources its claims cite is checked for support yet.
Aster Proteins Regulate the Accessible Cholesterol Pool in the Plasma Membrane
Open accessAbstract
Recent studies have demonstrated the existence of a discrete pool of cholesterol in the plasma membranes (PM) of mammalian cells-referred to as the accessible cholesterol pool-that can be detected by the binding of modified versions of bacterial cytolysins (e.g., anthrolysin O). When the amount of accessible cholesterol in the PM exceeds a threshold level, the excess cholesterol moves to the endoplasmic reticulum (ER), where it regulates the SREBP2 pathway and undergoes esterification. We reported previously that the Aster/Gramd1 family of sterol transporters mediates nonvesicular movement of cholesterol from the PM to the ER in multiple mammalian cell types. Here, we investigated the PM pool of accessible cholesterol in cholesterol-loaded fibroblasts with a knockdown of Aster-A and in mouse macrophages from Aster-B and Aster-A/B-deficient mice. Nanoscale secondary ion mass spectrometry (NanoSIMS) analyses revealed expansion of the accessible cholesterol pool in cells lacking Aster expression. The increased accessible cholesterol pool in the PM was accompanied by reduced cholesterol movement to the ER, evidenced by increased expression of SREBP2-regulated genes. Cosedimentation experiments with liposomes revealed that the Aster-B GRAM domain binds to membranes in a cholesterol concentration-dependent manner and that the binding is facilitated by the presence of phosphatidylserine. These studies revealed that the Aster-mediated nonvesicular cholesterol transport pathway controls levels of accessible cholesterol in the PM, as well as the activity of the SREBP pathway.
Overview
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Written from the paper’s full text.
TL;DR
Aster/Gramd1 sterol transporters regulate the size of the accessible cholesterol pool in the plasma membrane and thereby influence SREBP2 pathway activity. Loss or knockdown of Aster-A/B expands accessible plasma membrane cholesterol and reduces cholesterol movement to the ER.
Key findings
- The Aster-B GRAM domain bound liposomes in a cholesterol-dependent manner only when phosphatidylserine was present; it did not bind pure phosphatidylcholine liposomes containing up to 50% cholesterol, but bound mixed phosphatidylcholine/phosphatidylserine liposomes containing 30% or more cholesterol.
- Aster-A knockdown in 3T3-L1 preadipocytes increased 15N-labeled ALO-D4 binding to the plasma membrane, indicating an expanded accessible cholesterol pool, while [13C]cholesterol loading was not different.
- In mouse peritoneal macrophages, Aster-B KO and Aster-A/B double-knockout (DKO) macrophages showed about 45% greater 15N enrichment than wild-type macrophages, with comparable levels between Aster-B KO and Aster-A/B DKO.
- Aster-B KO and Aster-A/B DKO macrophages had increased expression of SREBP2-regulated genes (Srebf2, Hmgcs, Hmgcr, Sqle, Ldlr) under low-cholesterol conditions, and Aster-A/B DKO macrophages showed concordant changes after cholesterol loading.
Methods
- Cosedimentation assays incubated purified Aster-B GRAM domain or ALO-D4 with liposomes containing varying cholesterol, phosphatidylcholine, phosphatidylserine, and/or phosphatidylethanolamine.
- NanoSIMS with 15N-labeled ALO-D4 was used to quantify accessible plasma membrane cholesterol in 3T3-L1 cells treated with control or Aster-A antisense oligonucleotide and in peritoneal macrophages from WT, Aster-B KO, and Aster-A/B DKO mice loaded with acetylated LDL or cyclodextrin-cholesterol.
- Confocal microscopy quantified fluorescent ALO-D4 binding, and real-time PCR measured SREBP2 target gene expression in macrophages cultured in 1% LPDS or cholesterol-loaded conditions.
Limitations
- Stated: the authors did not test accessible cholesterol after Aster-C deletion because Aster-C expression is extremely low in most immortalized cell types; suitable antibodies were unavailable to compare relative Aster-A and Aster-B protein levels; further studies are needed to understand cholesterol-dependent GRAM domain binding and the GRAM domain sequences mediating anionic phospholipid binding.
- Evident: accessible cholesterol was inferred from ALO-D4 binding rather than directly measured, and SREBP2 target gene expression was used as a proxy for cholesterol movement to the ER.
- Evident: the liposome cosedimentation assays use artificial membranes and may not fully replicate plasma membrane lipid organization.
Model-written summary. Check it against the paper before relying on it.
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- Findingnone given
The changes in gene expression were more pronounced in the double-knockout macrophages.
“Although the combined loss of Aster-A and Aster-B did not further increase amounts of PM accessible cholesterol, the changes in gene expression were more pronounced in the double-knockout macrophages.”
Quote in the paperNot a substantial claim - Findingown data
The Aster-B GRAM domain binds to phospholipid liposomes containing phosphatidylcholine, phosphatidylserine, and cholesterol.
“The Aster-B GRAM domain binds to phospholipid liposomes containing phosphatidylcholine, phosphatidylserine, and cholesterol.”
Quote in the paperSubstantial claim - Findingown data
In low-cholesterol medium containing 1% LPDS, both Aster-B KO and Aster-A/B DKO macrophages exhibited increased expression of Srebf2 and its target genes Hmgcs, Hmgcr, Sqle, and Ldlr.
“When macrophages were incubated in low-cholesterol medium containing 1% lipoprotein-deficient serum (LPDS), both Aster-B KO and Aster-A/B DKO macrophages exhibited increased expression of Srebf2 and its target genes (Hmgcs, Hmgcr, Sqle, and Ldlr) (Fig. 8B and C).”
Quote in the paperSubstantial claim - Findingown data
ALO-D4 binds phosphatidylcholine liposomes containing 40% or more cholesterol.
“we found that ALO-D4 could bind phosphatidylcholine (PC) liposomes containing 40% or more cholesterol (Fig. 1A).”
Quote in the paperNot a substantial claim - Findingown data
The Aster-B GRAM domain binds mixed phosphatidylcholine/phosphatidylserine liposomes containing 30% or more cholesterol.
“Additional studies showed that the Aster-B GRAM domain was able to bind mixed phosphatidylcholine/phosphatidylserine liposomes containing 30% or more cholesterol (Fig. 2).”
Quote in the paperSubstantial claim
- Findingown data
Incorporating phosphatidylserine into liposomes resulted in robust Aster-B GRAM domain binding in a concentration-dependent fashion.
“However, incorporating phosphatidylserine into the liposomes resulted in robust GRAM domain binding and did so in a concentration-dependent fashion (Fig. 1B).”
Quote in the paperSubstantial claim - Findingown data
Aster-B deletion, especially in the setting of sterol depletion, resulted in increased Gramd1a expression.
“Aster-B deletion, especially in the setting of sterol depletion, resulted in increased Gramd1a expression.”
Quote in the paperNot a substantial claim - Findingown data
Quantification of fluorescence intensities paralleled the NanoSIMS findings.
“Quantification of fluorescence intensities paralleled the NanoSIMS findings (Fig. 7B).”
Quote in the paperNot a substantial claim - Findingown data
Confocal microscopy showed increased binding of Alexa Fluor 594-conjugated 15N-labeled ALO-D4 to the PMs of Aster-B KO and Aster-A/B DKO macrophages.
“We observed increased binding of Alexa Fluor 594-conjugated 15 N-labeled ALO-D4 to the PMs of Aster-B KO and Aster-A/B DKO macrophages (Fig. 7A).”
Quote in the paperSubstantial claim - Findingown data
Binding of the Aster-B GRAM domain to cholesterol requires that liposomes contain phosphatidylserine.
“In contrast to ALO-D4, which binds cholesterol in phosphatidylcholine liposomes, the binding of the GRAM domain of Aster-B to cholesterol requires that liposomes contain phosphatidylserine.”
Quote in the paperSubstantial claim - Findingown data
The amounts of [13C]cholesterol in the PMs of 3T3-L1 fibroblasts treated with control ASO or Aster-A ASO were not different.
“The amounts of [ 13 C]cholesterol in the PMs of fibroblasts treated with the control ASO or the Aster-A ASO were not different (Fig. 3B).”
Quote in the paperSubstantial claim - Findingown data
Binding of the Aster-B GRAM domain to liposomes increases with increasing amounts of phosphatidylserine.
“There was increased binding of the Aster-B GRAM domain to liposomes with increasing amounts of phosphatidylserine in liposomes.”
Quote in the paperNot a substantial claim - Findingown data
The Aster-B GRAM domain does not bind to phospholipid liposomes containing phosphatidylcholine, phosphatidylethanolamine, and cholesterol.
“The Aster-B GRAM domain does not bind to phospholipid liposomes containing phosphatidylcholine, phosphatidylethanolamine (PE), and cholesterol.”
Quote in the paperSubstantial claim - Findingown data
15N enrichment is approximately 45% greater in Aster-B KO and Aster-A/B DKO macrophages than in wild-type macrophages.
“Quantification of 15 N/ 14 N ratios from WT (n ϭ 58), Aster-B KO (n ϭ 268), and Aster-A/B DKO (n ϭ 156) macrophages, revealing ϳ45% greater 15 N enrichment in Aster-B KO and Aster-A/B DKO macrophages than in WT macrophages.”
Quote in the paperSubstantial claim - Findingown data
The 15N/14N ratio was ~45% higher in Aster-B KO and Aster-A/B DKO macrophages than in WT macrophages.
“The 15 N/ 14 N ratio was ϳ45% higher in Aster-B KO and Aster-A/B DKO macrophages than in WT macrophages.”
Quote in the paperSubstantial claim - Findingown data
Aster deficiency results in increased 15N-labeled ALO-D4 binding to the plasma membranes of mouse peritoneal macrophages compared with wild-type macrophages.
“NanoSIMS images showing that Aster deficiency results in increased 15 N-labeled ALO-D4 binding to the plasma membranes of mouse peritoneal macrophages.”
- Also stated in: § Preparation of the Aster-B GRAM domain and testing its binding to liposomes. · plain
“15 N/ 14 N NanoSIMS images reveal more 15 N-labeled ALO-D4 binding to Aster-B and Aster-A/B DKO macrophages than to WT macrophages.”
Quote in the paperSubstantial claim - Also stated in: § Preparation of the Aster-B GRAM domain and testing its binding to liposomes. · plain
- Findingown data
NanoSIMS revealed higher levels of 15N-labeled ALO-D4 binding to peritoneal macrophages from Aster-B KO and Aster-A/B DKO mice than from WT mice.
“NanoSIMS revealed higher levels of 15 N-labeled ALO-D4 binding to the peritoneal macrophages from Aster-B KO mice and Aster-A/B DKO mice, indicating an expanded pool of accessible cholesterol in the PM (Fig. 5 and 6).”
Quote in the paperSubstantial claim - Findingown data
Incorporation of phosphatidylethanolamine into liposomes did not affect Aster-B GRAM domain binding.
“On the other hand, incorporation of phosphatidylethanolamine into the liposomes did not affect GRAM domain binding, providing further support for the specificity of Aster recruitment to membranes (Fig. 1C).”
Quote in the paperSubstantial claim - Findingown data
Loss of Aster-B in macrophages results in increased binding of Alexa Fluor 594-conjugated 15N-labeled ALO-D4 to the plasma membrane.
“Loss of Aster-B in macrophages results in increased binding of Alexa Fluor 594-conjugated 15 N-labeled ALO-D4 to the plasma membrane.”
Quote in the paperSubstantial claim - Findingown data
The Aster-B GRAM domain did not bind pure phosphatidylcholine liposomes containing up to 50% cholesterol.
“In contrast, the Aster-B GRAM domain did not bind pure PC liposomes containing up to 50% cholesterol.”
Quote in the paperSubstantial claim - Findingown data
Binding of the Aster-B GRAM domain to PC/PS-containing liposomes increases with increasing amounts of cholesterol.
“Results of a cosedimentation assay showing increasing amounts of Aster-B GRAM domain in PC/PS-containing liposomes with increasing amounts of cholesterol.”
Quote in the paperSubstantial claim - Findingown data
The combined loss of Aster-A and Aster-B did not further increase amounts of PM accessible cholesterol.
“Although the combined loss of Aster-A and Aster-B did not further increase amounts of PM accessible cholesterol, the changes in gene expression were more pronounced in the double-knockout macrophages.”
Quote in the paperSubstantial claim - Findingown data
The 13C/12C ratio was ~55% higher in 3T3-L1 cells treated with Aster-A ASO than in cells treated with control ASO.
“The 13 C/ 12 C ratio was ϳ55% higher in cells treated with Aster-A ASO than in cells treated with the control ASO (Fig. 3B).”
Quote in the paperSubstantial claim - Interpretationreasoning
Aster proteins are important for regulating the PM accessible cholesterol pool in many, if not all, cells.
“The fact that we observed similar findings in different cell types and with different strategies for cholesterol loading (cyclodextrin-cholesterol complexes or Ac-LDL) strongly implied that Aster proteins are important for regulating the PM accessible cholesterol pool in many, if not all, cells.”
Quote in the paperSubstantial claim- Rests on an assumption: The Aster-A ASO specifically reduces Aster-A expression without off-target effects that could affect the accessible cholesterol pool.
- Rests on an assumption: The Aster-A and Aster-B knockout mice lack the respective proteins and the observed phenotypes are due to loss of these proteins rather than developmental compensation.
- Interpretationown data
The accessible cholesterol pool in the plasma membrane is expanded in the setting of Aster deficiency.
“The accessible cholesterol pool in the PM is expanded in the setting of Aster deficiency.”
Quote in the paperSubstantial claim - Interpretationown data
Aster proteins regulate the PM accessible cholesterol pool by moving surplus cholesterol to the ER.
“Our data demonstrate that Aster proteins regulate the PM accessible cholesterol pool by moving surplus cholesterol to the ER.”
Quote in the paperSubstantial claim- Rests on an assumption: The Aster-A ASO specifically reduces Aster-A expression without off-target effects that could affect the accessible cholesterol pool.
- Rests on an assumption: The Aster-A and Aster-B knockout mice lack the respective proteins and the observed phenotypes are due to loss of these proteins rather than developmental compensation.
- Rests on an assumption: Changes in SREBP2 target gene expression reflect changes in ER cholesterol and SREBP2 processing.
- Interpretationown data
Loss of Aster-B was sufficient to increase the PM pool of accessible cholesterol.
“In line with this idea, our NanoSIMS imaging results showed that loss of Aster-B was sufficient to increase the PM pool of accessible cholesterol.”
Quote in the paperSubstantial claim- Rests on an assumption: The Aster-A and Aster-B knockout mice lack the respective proteins and the observed phenotypes are due to loss of these proteins rather than developmental compensation.
- Interpretationown data
The amount of accessible cholesterol in phospholipid liposomes is a key determinant of Aster-B GRAM domain binding.
“Our cosedimentation assays revealed that the amount of accessible cholesterol in phospholipid liposomes is a key determinant of GRAM domain binding.”
Quote in the paperSubstantial claim - Interpretationown data
Processing of SREBP2 increased in the absence of Aster proteins.
“Our findings support the conclusion that processing of SREBP2 increased in the absence of Aster proteins.”
Quote in the paperSubstantial claim- Rests on an assumption: Changes in SREBP2 target gene expression reflect changes in ER cholesterol and SREBP2 processing.
- Premisecitation
Aster proteins are integral membrane proteins of the ER.
“The Aster proteins (Aster-A, Aster-B, and Aster-C), which are integral membrane proteins of the ER, play an important role in detecting cholesterol in the PM and moving it to the ER (7).”
Quote in the paperSubstantial claim0 of 1 sources checked- cites [7]
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
- Study design and conductown data
Exons 2 to 4 were efficiently deleted in the Aster-A knockout mice.
“Sequencing of the band confirmed the deletion; the red box in the graph indicates the deletion site, confirming that exons 2 to 4 were efficiently deleted.”
Quote in the paperSubstantial claim - Premisecitation
In living cells, Asters are recruited to the PM only in the setting of cholesterol loading.
“However, in living cells, Asters are recruited to the PM (where phosphatidylserine is invariably present) only in the setting of cholesterol loading (7).”
Quote in the paperSubstantial claim0 of 1 sources checked- cites [7]
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
- Interpretationown data
The accessible cholesterol pool in the PM is expanded in peritoneal macrophages from Aster-B KO and Aster-A/B DKO mice.
“NanoSIMS revealed higher levels of 15 N-labeled ALO-D4 binding to the peritoneal macrophages from Aster-B KO mice and Aster-A/B DKO mice, indicating an expanded pool of accessible cholesterol in the PM (Fig. 5 and 6).”
Quote in the paperSubstantial claim- Rests on an assumption: The Aster-A and Aster-B knockout mice lack the respective proteins and the observed phenotypes are due to loss of these proteins rather than developmental compensation.
- Interpretationown data
Inactivation of Aster genes activates the SREBP2 pathway.
“Inactivation of Aster genes activates the SREBP2 pathway.”
Quote in the paperSubstantial claim - Interpretationcitation
The three different Aster proteins perform similar functions in regulating PM cholesterol levels.
“Our results also add to evidence indicating that the three different Aster proteins perform similar functions in regulating PM cholesterol levels, despite the fact that they have distinct patterns of expression and are regulated independently (7).”
Quote in the paperSubstantial claim0 of 1 sources checked- cites [7]
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
- Interpretationown data
The Aster-B GRAM domain recognizes cholesterol in membranes containing phosphatidylserine.
“The Aster-B GRAM domain recognizes cholesterol in membranes containing phosphatidylserine.”
Quote in the paperSubstantial claim
- The quote only partly states this claim. 1
- It may state two separate claims as one. 3
- Probably not a substantial claim. 6
The quote only partly states this claim.
Findingown dataIn Aster-A/B DKO macrophages cholesterol loaded for 2 h with cyclodextrin-cholesterol complexes, concordant results (increased expression of SREBP2 target genes) were observed.
“Concordant results were observed in Aster-A/B DKO macrophages that had been cholesterol loaded for 2 h with cyclodextrincholesterol complexes (Fig. 8D and E).”
Quote in the paperSubstantial claimIt may state two separate claims as one.
Findingown dataGene expression perturbations in cholesterol-loaded Aster-B KO macrophages followed the same trend, although induction of SREBP2 target genes was more modest.
“Gene expression perturbations in cholesterolloaded Aster-B KO macrophages followed the same trend, although the induction of SREBP2 target genes was more modest.”
Quote in the paperNot a substantial claimIt may state two separate claims as one.
PremisecitationAster proteins play an important role in detecting cholesterol in the PM and moving it to the ER.
“The Aster proteins (Aster-A, Aster-B, and Aster-C), which are integral membrane proteins of the ER, play an important role in detecting cholesterol in the PM and moving it to the ER (7).”
Quote in the paperSubstantial claim0 of 1 sources checked- cites [7]
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
Probably not a substantial claim. The paper’s conclusions may not depend on it.
Study design and conductown dataAster-A global-knockout mice carry a frameshift mutation caused by deletion of the region between exon 2 and intron 4.
“CRISPR guides targeted the region between exon 2 and intron 4, resulting in a frameshift mutation caused by deletion of the targeted region between exon 2 and intron 4.”
Quote in the paperNot a substantial claimIt may state two separate claims as one.
Interpretationown dataWhen Aster protein expression is reduced, the PM accessible pool is expanded and the ER pool contracts, as evident from increased activity of SREBP-regulated genes.
“When Aster protein expression is reduced, the PM accessible pool is expanded and the ER pool contracts, as evident from increased activity of SREBP-regulated genes.”
Quote in the paperSubstantial claim- Rests on an assumption: The Aster-A ASO specifically reduces Aster-A expression without off-target effects that could affect the accessible cholesterol pool.
- Rests on an assumption: The Aster-A and Aster-B knockout mice lack the respective proteins and the observed phenotypes are due to loss of these proteins rather than developmental compensation.
- Rests on an assumption: Changes in SREBP2 target gene expression reflect changes in ER cholesterol and SREBP2 processing.
Probably not a substantial claim. The paper’s conclusions may not depend on it.
PremisecitationAster-B knockout mice have been previously described.
“Aster-B knockout mice have been previously described (7).”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites [7]
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
Probably not a substantial claim. The paper’s conclusions may not depend on it.
PremisecitationThe GRAM domain of Aster-B is able to bind immobilized phosphatidylserine or liposomes containing high levels of phosphatidylserine (≥80 mol%) in the absence of cholesterol.
“Earlier studies showed that the GRAM domain of Aster-B is able to bind immobilized phosphatidylserine or liposomes containing high levels of phosphatidylserine (Ն80 mol%) in the absence of cholesterol (7,8).”
Quote in the paperNot a substantial claim0 of 2 sources checked- cites [7]
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
- cites [8]
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
Probably not a substantial claim. The paper’s conclusions may not depend on it.
PremisecitationThe inner leaflet of the PM normally contains ~10 mol% phosphatidylserine.
“The inner leaflet of the PM normally contains ϳ10 mol% phosphatidylserine (14).”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites [14]
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
Probably not a substantial claim. The paper’s conclusions may not depend on it.
PremisecitationNaito et al. showed that all three Aster/Gramd1 proteins move cholesterol to the ER when the PM pool of accessible cholesterol is expanded by treating cells with sphingomyelinase.
“They showed that all three Aster/Gramd1 proteins move cholesterol to the ER when the PM pool of accessible cholesterol is expanded by treating cells with sphingomyelinase.”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites [8]
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
Probably not a substantial claim. The paper’s conclusions may not depend on it.
PremisecitationNaito et al. reported that the presence of anionic lipids, including phosphatidylserine, enhanced the binding of the Aster GRAM domain to cholesterol-containing liposomes in cosedimentation assays.
“They further reported that the presence of anionic lipids, including phosphatidylserine, enhanced the binding of the Aster GRAM domain to cholesterol-containing liposomes in cosedimentation assays (8).”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites [8]
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
The paper relies on this without support.
The Aster-A ASO specifically reduces Aster-A expression without off-target effects that could affect the accessible cholesterol pool.
“We were able to effectively knock down the expression of Aster-A, the main Aster family member in 3T3-L1 cells (7), with an antisense oligonucleotide (ASO).”
The paper relies on this without support.
The Aster-A and Aster-B knockout mice lack the respective proteins and the observed phenotypes are due to loss of these proteins rather than developmental compensation.
“We generated Aster-A knockout (KO) mice (Fig. 4A and B) and showed that Aster-A transcripts were absent from the peritoneal macrophages of these mice (Fig. 4C).”
The paper relies on this without support.
Changes in SREBP2 target gene expression reflect changes in ER cholesterol and SREBP2 processing.
“Our findings support the conclusion that processing of SREBP2 increased in the absence of Aster proteins.”
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Previous studies showed that in macrophages and hepatocytes Asters specifically recognize the accessible pool of plasma membrane cholesterol.
“Previous studies showed that in macrophages (33) and hepatocytes (28) Asters specifically recognize the accessible pool of PM cholesterol (34, 35).”
From Aster-dependent nonvesicular transport facilitates dietary cholesterol uptake (2023) · cites this paper as [33]
The Results and Discussion report that Aster deficiency expands the accessible plasma-membrane cholesterol pool in mouse macrophages, and the Results show that an Aster GRAM domain recognizes cholesterol in the presence of phosphatidylserine. The paper examines macrophages and fibroblasts, not hepatocytes, and does not establish that Asters specifically recognize the accessible pool in hepatocytes. The indexed passages provide no page numbers. (LLM, conf=0.86)
Experimental — accuracy not yet measuredThe recruitment of Asters to the PM depends on the cholesterol and phosphatidylserine content in the inner leaflet.
“The recruitment of Asters to the PM depends on the cholesterol and phosphatidylserine content in the inner leaflet (25, 26, 33).”
From Aster-dependent nonvesicular transport facilitates dietary cholesterol uptake (2023) · cites this paper as [33]
The Results report cholesterol-dependent recruitment of Asters to the plasma membrane in living cells and phosphatidylserine-dependent binding of the Aster-B GRAM domain to liposomes. The Discussion proposes that cholesterol alters phosphatidylserine presentation in the inner leaflet, but does not establish that recruitment in living cells depends on the inner leaflet’s phosphatidylserine content. (LLM, conf=0.83)
Experimental — accuracy not yet measuredPrevious studies demonstrated that Aster proteins are required for transport of cholesterol from the PM to the ER when cholesterol is delivered directly to the PM by cholesterol/MCD complexes or liberated within the membrane by sphingomyelinase treatment.
“Previous studies from the laboratories of Tontonoz and coworkers (8, 9) and Saheki and coworkers (10, 11) demonstrated that Aster proteins are required for the transport of cholesterol from the PM to the ER when cholesterol is delivered directly to the PM by incubation with cholesterol/MCD complexes or when it is liberated within the membrane by sphingomyelinase treatment.”
From Interplay between Asters/GRAMD1s and phosphatidylserine in intermembrane transport of LDL cholesterol (2022) · cites this paper as [9]
GRAMD1b has a direct role in extracting and transporting accessible cholesterol from the PM to the ER.
“consistent with the direct role of GRAMD1b in extracting and transporting accessible cholesterol from the PM to the ER (Naito et al, 2019; Ferrari et al, 2020)”
From Molecular basis of accessible plasma membrane cholesterol recognition by the GRAM domain of GRAMD1b (2021) · cites this paper as Ferrari et al, 2020
In the absence of GRAMD1s, accessible cholesterol is inefficiently transported from the plasma membrane to the endoplasmic reticulum, resulting in chronic expansion of accessible plasma membrane cholesterol.
“In the absence of GRAMD1s, accessible cholesterol is inefficiently transported from the PM to the ER, resulting in a chronic expansion of accessible PM cholesterol (Naito et al, 2019; Ferrari et al, 2020).”
From Molecular basis of accessible plasma membrane cholesterol recognition by the GRAM domain of GRAMD1b (2021) · cites this paper as Ferrari et al, 2020
GRAMD1B is a member of the Aster family and a known cholesterol transporter.
“GRAMD1B is a member of the Aster family and a known cholesterol transporter40,66.”
From GRAMD1B is a regulator of lipid homeostasis, autophagic flux and phosphorylated tau (2025) · cites this paper as [66]
AI-3d has been found to inhibit cholesterol uptake and maintain lipid homeostasis.
“AI-3d has been found to inhibit cholesterol uptake and maintain lipid homeostasis40,66.”
From GRAMD1B is a regulator of lipid homeostasis, autophagic flux and phosphorylated tau (2025) · cites this paper as [66]
Using scRNA-seq, genes (e.g., GRAMD1B, VEGFB, MIAT, COMT, NRP1, DSEL, NR2F2, HMGCS1, and LDLR) and biological pathways related to lipid metabolism are increased in excitatory neurons of MAPT R406W mutant HNOs compared to isogenic control HNOs.
“Using scRNA-seq, we found that genes (e.g., GRAMD1B, VEGFB, MIAT, COMT, NRP1, DSEL, NR2F2, HMGCS1, and LDLR)9,58,66,69–71 and biological pathways related to lipid metabolism are increased in excitatory neurons of MAPT R406W mutant HNOs compared to isogenic control HNOs (Fig. 4a, b and Supplementary Fig. 2a–c).”
From GRAMD1B is a regulator of lipid homeostasis, autophagic flux and phosphorylated tau (2025) · cites this paper as [66]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
Each contradiction between two passages listed here was confirmed by an independent check.
Mouse-generation methods cite the fibroblast figure
MinorThe mouse-generation methods say the CRISPR strategy is outlined in Fig. 3A, but the figure captions identify Fig. 4A as the mouse-generation strategy; Fig. 3A shows fibroblast NanoSIMS images.
“Aster-A global-knockout mice were generated at the Transgenic Mouse Facility at the University of California, Irvine, CA, on a C57BL/6N background using the CRISPR/Cas9 strategy outlined in Fig. 3A.”
“Figure: 4 FIG 4 FIG 4 Generation of Aster-A knockout mice.(A) Strategy for generating Gramd1a (Aster-A) knockout mice by CRISPR-Cas9 genome editing.”
Fibroblast cholesterol loading is described as both unchanged and 55% higher
MinorThe results say PM [13C]cholesterol did not differ between the ASO groups, but then report a roughly 55% higher 13C/12C ratio in the Aster-A ASO group. These statements conflict about whether the groups had comparable cholesterol loading.
“The amounts of [ 13 C]cholesterol in the PMs of fibroblasts treated with the control ASO or the Aster-A ASO were not different (Fig. 3B).”
“The 13 C/ 12 C ratio was ϳ55% higher in cells treated with Aster-A ASO than in cells treated with the control ASO (Fig. 3B).”
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Molecular basis of accessible plasma membrane cholesterol recognition by the GRAM domain of GRAMD1b
Ercan, B., Naito, T., Koh, D. H. Z., Dharmawan, D., & Saheki, Y. (2021) · The EMBO Journal · doi:10.15252/embj.2020106524 · Cited by 132
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Patched 1 reduces the accessibility of cholesterol in the outer leaflet of membranes
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Cholesterol metabolism: from lipidomics to immunology
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Aster-dependent nonvesicular transport facilitates dietary cholesterol uptake
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Hepatic nonvesicular cholesterol transport is critical for systemic lipid homeostasis
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Stay in touch with the endoplasmic reticulum
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GRAMD1-mediated accessible cholesterol sensing and transport
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Cellular cholesterol and how to find it
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Selective Aster inhibitors distinguish vesicular and nonvesicular sterol transport mechanisms
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Visualization of accessible cholesterol using a GRAM domain-based biosensor
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Cholesterol Transport to the Endoplasmic ReticulumPreprint
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Self-citationSpecificity of lipid transfer proteins: An in vitro story
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25-hydroxycholesterol: an integrator of antiviral ability and signaling
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Ogasawara, F., & Ueda, K. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102702 · Cited by 20
T cell cholesterol transport links intestinal immune responses to dietary lipid absorption
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Self-citationN-SREBP2 Provides a Mechanism for Dynamic Control of Cellular Cholesterol Homeostasis
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Photosensitizer proximity labeling captures the lipid and protein interactomes
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Aster-B–dependent estradiol synthesis protects female mice from diet-induced obesity
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Self-citationGRAMD1B is a regulator of lipid homeostasis, autophagic flux and phosphorylated tau
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Creating and sensing asymmetric lipid distributions throughout the cell
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The nonvesicular sterol transporter Aster-C plays a minor role in whole body cholesterol balance
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Cholesterol binding to VCAM-1 promotes vascular inflammationPreprint
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Metadata
- Authors
- Ferrari, A., He, C., Kennelly, J. P., Sandhu, J., Xiao, X., Chi, X., Jiang, H., Young, S. G., & Tontonoz, P.
- Affiliations
- University of California, Los Angeles (US)
- Department of Pathology and Laboratory Medicine and Department of Biological Chemistry, University of California, Los Angeles
- The University of Western Australia (AU)
- Corresponding author
- Tontonoz, Peter
- ORCID
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2020-09-14
- Volume
- 40
- Issue
- 19
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- PMC
- PMC7491948
- OpenAlex
- W3045552307
- Semantic Scholar
- 01481e64e105e316a680aefc33453af7ca681d2d
- Cited by
- 66
- References
- 19
- Citations by year
- 2026: 7 · 2025: 11 · 2024: 10 · 2023: 13 · 2022: 13 · 2021: 11 · 2020: 1
- FWCI
- 3.87
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Molecular and Cellular Biology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- UWA Profiles and Research Repository (UWA) (submittedVersion, other-oa)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- NHLBI (P01 HL146358)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Cholesterol and Lipid Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Lipids, and Metabolism
- Keywords
- plasma membrane cholesterol, cholesterol esterification, endoplasmic reticulum cholesterol, phosphatidylserine, macrophages, cholesterol homeostasis
- MeSH terms
- Animals, Bacterial Proteins, Cell Membrane, Cholesterol, Endoplasmic Reticulum, Fibroblasts, Liposomes, Membrane Glycoproteins, Mice, Inbred C57BL, Macrophages, Peritoneal, Mice, Knockout, Spectrometry, Mass, Secondary Ion, 3T3-L1 Cells, Mice, Sterol Regulatory Element Binding Protein 2
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