The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
Plan overview
We verified identity and domains, assembled recent primary and review literature (prioritizing 2023–2024), extracted mechanistic and localization evidence, integrated pathway/physiology findings (liver and intestine), assessed redundancy with paralogs, and compiled expert analyses. A compact evidence table is embedded for quick reference.
| Aspect | Key findings (1–2 sentences) | Primary sources (journal, year, URL) |
|---|---|---|
| Identity / nomenclature (GRAMD1A = Aster-A) | GRAMD1A is the gene encoding Aster-A, one of three Aster/GRAMD1 paralogs (Aster‑A/B/C) implicated in nonvesicular sterol transport. | Cell (Sandhu et al.), 2018, https://doi.org/10.1016/j.cell.2018.08.033 (sandhu2018asterproteinsfacilitate pages 1-3); eLife (Naito et al.), 2019, https://doi.org/10.7554/elife.51401 (naito2019movementofaccessible pages 2-3) |
| Domain architecture | Aster‑A contains an N-terminal GRAM lipid‑binding module, a central VASt / StART‑like (ASTER) sterol‑binding domain, and a C‑terminal single‑pass ER transmembrane helix. | Cell, 2018, https://doi.org/10.1016/j.cell.2018.08.033 (sandhu2018asterproteinsfacilitate pages 1-3); Cold Spring Harb Perspect (Kennelly & Tontonoz), 2023, https://doi.org/10.1101/cshperspect.a041263 (kennelly2023cholesteroltransportto pages 4-6) |
| ER anchoring and ER–PM contact site recruitment | Aster‑A is ER‑anchored via the C‑terminal TM helix and relocalizes to ER–PM contact sites upon increases in accessible PM cholesterol. | Cell, 2018, https://doi.org/10.1016/j.cell.2018.08.033 (sandhu2018asterproteinsfacilitate pages 1-3); eLife, 2019, https://doi.org/10.7554/elife.51401 (naito2019movementofaccessible pages 2-3) |
| GRAM domain sensing of accessible cholesterol + PS | The GRAM domain acts as a coincidence detector for accessible (unsequestered) PM cholesterol and anionic lipids (notably phosphatidylserine), triggering recruitment to contacts. | EMBO J / eLife mechanistic work (Ercan / Naito), 2019–2021, https://doi.org/10.7554/elife.51401 (naito2019movementofaccessible pages 22-24, sandhu2018theasterproteins pages 41-45) |
| Sterol binding / transfer by VASt / StART‑like domain | The central ASTER (VASt/StART‑like) domain contains a hydrophobic cavity that binds cholesterol and mediates intermembrane sterol transfer in vitro. | Cell, 2018, https://doi.org/10.1016/j.cell.2018.08.033 (sandhu2018asterproteinsfacilitate pages 1-3); Cold Spring Harb Perspect, 2023, https://doi.org/10.1101/cshperspect.a041263 (kennelly2023cholesteroltransportto pages 4-6) |
| Nonvesicular PM→ER transport and SREBP2 regulation | GRAMD1 proteins move accessible PM cholesterol to the ER; this transfer suppresses SREBP‑2 activation, and loss of GRAMD1s expands the accessible PM cholesterol pool and derepresses SREBP‑2. | eLife, 2019, https://doi.org/10.7554/elife.51401 (naito2019movementofaccessible pages 3-5); Cold Spring Harb Perspect, 2023, https://doi.org/10.1101/cshperspect.a041263 (kennelly2023cholesteroltransportto pages 4-6) |
| Golgi→ER transport control (2023) | Recent work shows GRAMD1s/Asters also export excess cholesterol from the Golgi to the ER, preventing Golgi cholesterol accumulation and chronic SREBP‑2 activation. | Nat Commun (Naito et al.), 2023, https://doi.org/10.1038/s41467-023-41213-w (naito2023regulationofcellular pages 1-2) |
| Complex formation with GRAMD1B/C | GRAMD1A can form homo‑ and heteromeric complexes with GRAMD1B/C via transmembrane regions and luminal helices, which modulate recruitment and function. | eLife, 2019, https://doi.org/10.7554/elife.51401 (naito2019movementofaccessible pages 2-3); Sandhu dissertation/analysis, 2018 (sandhu2018theasterproteins pages 90-95) |
| Tissue expression highlights | Paralogs show distinct tissue enrichments (e.g., Aster‑B high in adrenal); Aster‑A is broadly expressed with notable brain expression reported in reviews. | Cold Spring Harb Perspect, 2023, https://doi.org/10.1101/cshperspect.a041263 (kennelly2023cholesteroltransportto pages 4-6); Sandhu 2018 (sandhu2018theasterproteins pages 90-95) |
| Hepatic role in systemic lipid homeostasis (2023) | Hepatocyte Aster function is critical for nonvesicular sterol flux to the ER and systemic lipid homeostasis; liver Aster loss perturbs ER cholesterol sensing and systemic sterol handling (Nature Metabolism, 2023). | Nat Metab (Xiao et al.), 2023, https://doi.org/10.1038/s42255-022-00722-6 (discussed in reviews) (naito2023regulationofcellular pages 1-2, ferrari2023asterdependentnonvesiculartransport pages 1-3) |
| Intestinal dietary cholesterol uptake & pharmacologic inhibition (2023) | Aster‑B/C aid enterocyte PM→ER cholesterol movement downstream of NPC1L1; Aster deficiency reduces dietary cholesterol absorption and small‑molecule Aster inhibitors can blunt uptake (Science, 2023). | Science (Ferrari et al.), 2023, https://doi.org/10.1126/science.adf0966 (ferrari2023asterdependentnonvesiculartransport pages 1-3) |
| Aster‑C whole‑body balance minor (2024) | Genetic loss of Aster‑C alone produces modest effects on whole‑body cholesterol under varied diets, suggesting partial redundancy among paralogs. | Front Physiol (Banerjee et al.), 2024, https://doi.org/10.3389/fphys.2024.1371096 (ferrari2023asterdependentnonvesiculartransport pages 1-3, sandhu2018theasterproteins pages 45-49) |
Table: Compact, citable summary of GRAMD1A (Aster‑A) identity, domains, mechanism, localization, and recent (2023–2024) in vivo roles with primary-source links and context IDs for verification.
Gene/protein verification and nomenclature
- Target identity: GRAMD1A (HGNC:29305) encodes Aster-A, a human endoplasmic reticulum (ER)–resident lipid transfer protein of the Aster/GRAMD1 family (Aster-A/B/C; genes GRAMD1A/B/C). This aligns with UniProt Q96CP6 and the literature that established the Aster nomenclature (Aster-A for GRAMD1A) (sandhu2018asterproteinsfacilitate pages 1-3, naito2019movementofaccessible pages 2-3).
- Organism: Homo sapiens. All cited mechanistic studies include human cell systems or human proteins, consistent with the target (sandhu2018asterproteinsfacilitate pages 1-3, naito2019movementofaccessible pages 2-3).
- Domain architecture: Aster-A comprises an N-terminal GRAM domain, a central VASt/StART-like (often called ASTER) sterol-binding module, and a C-terminal single-pass ER transmembrane (TM) helix. The VASt/StART-like domain forms a hydrophobic cavity for sterol binding; the GRAM domain mediates cholesterol- and anionic lipid–dependent membrane engagement; the TM helix anchors the protein in the ER (sandhu2018asterproteinsfacilitate pages 1-3, kennelly2023cholesteroltransportto pages 4-6, sandhu2018theasterproteins pages 41-45).
Key concepts and definitions (current understanding)
- Function and substrate specificity: GRAMD1A (Aster-A) mediates nonvesicular transfer of “accessible” plasma membrane (PM) cholesterol to the ER at ER–PM contact sites. The transported substrate is cholesterol (and select sterols in vitro) bound within the ASTER/VASt/StART-like cavity. This transfer contributes to feedback suppression of SREBP-2 and to cholesterol esterification in the ER (naito2019movementofaccessible pages 3-5, sandhu2018asterproteinsfacilitate pages 1-3, kennelly2023cholesteroltransportto pages 4-6).
- Accessible cholesterol pool: A non-raft, unsequestered PM cholesterol fraction that can be acutely expanded (e.g., by sphingomyelin hydrolysis) and detected by cytolysin-derived probes. GRAMD1 proteins respond to transient expansions of this pool to initiate PM→ER cholesterol transfer (naito2019movementofaccessible pages 3-5, kennelly2023cholesteroltransportto pages 4-6).
- ER–PM membrane contact sites (MCS): Physical appositions where Aster-A is recruited to move cholesterol without vesicular trafficking; Aster-A marks a subset of ER–PM contacts specialized for sterol transport (sandhu2018asterproteinsfacilitate pages 1-3, naito2019movementofaccessible pages 2-3).
- Paralogs and complexes: GRAMD1A forms homo- and hetero-oligomeric complexes with GRAMD1B and GRAMD1C through TM/luminal regions, modulating recruitment and function (naito2019movementofaccessible pages 2-3, naito2019movementofaccessible pages 3-5).
Mechanism and domain-level biochemistry
- GRAM domain (sensing and recruitment): The GRAM domain functions as a coincidence detector for (i) accessible PM cholesterol and (ii) anionic phospholipids, prominently phosphatidylserine (PS). Deleting the GRAM domain abolishes cholesterol-dependent PM recruitment, while the isolated GRAM domain is necessary and sufficient for cholesterol-triggered recruitment to the PM. Structural/biochemical analyses indicate distinct, synergistic sites within GRAMD1 GRAM domains for cholesterol and PS sensing (sandhu2018theasterproteins pages 41-45, naito2019movementofaccessible pages 22-24, kennelly2023cholesteroltransportto pages 4-6).
- VASt/StART-like (ASTER) domain (binding/transfer): Aster-A’s ASTER domain is a VASt/StART-like fold with a largely enclosed sterol-binding pocket that carries one sterol and supports intermembrane transfer. Structural features and mutational analyses indicate a ligand-binding mode distinct from classical StART proteins yet optimized for sterol transfer at contacts (sandhu2018asterproteinsfacilitate pages 1-3, sandhu2018theasterproteins pages 41-45, kennelly2023cholesteroltransportto pages 4-6).
- ER anchoring and ER–PM MCS localization: The C-terminal TM helix anchors Aster-A in the ER; upon PM cholesterol loading (e.g., exogenous cholesterol or sphingomyelinase treatment), Aster-A rapidly relocalizes to ER–PM contacts in a GRAM-dependent manner. Aster-defined contacts partially overlap with, but are distinct from, ORP/E-Syt contact domains (sandhu2018asterproteinsfacilitate pages 1-3, sandhu2018theasterproteins pages 41-45).
- Transport directionality and targets: Aster-A mediates PM→ER cholesterol transfer when the PM accessible pool expands, down its chemical potential gradient, thereby supplying the ER for esterification and feedback. Emerging data also show Aster paralogs facilitate Golgi→ER export of excess cholesterol to prevent Golgi accumulation, integrating Asters into ER–Golgi and ER–PM sterol circuits (naito2019movementofaccessible pages 3-5, naito2023regulationofcellular pages 1-2).
- Pathway consequences: Loss of GRAMD1 function (single or triple knockout/knockdown) expands the accessible PM cholesterol pool, impairs PM→ER sterol flux, delays or diminishes SREBP-2 suppression by exogenous cholesterol, and reduces cholesteryl ester formation—placing Aster-A upstream of ER sterol sensing and ACAT-mediated esterification (naito2019movementofaccessible pages 3-5, sandhu2018theasterproteins pages 45-49).
Recent developments and latest research (prioritizing 2023–2024)
- ER sterol homeostasis at ER–Golgi contacts (2023): GRAMD1s (including Aster-A) cooperate with ORP9/OSBP to maintain cholesterol distribution by exporting excess Golgi cholesterol to the ER, averting Golgi sterol accumulation and chronic SREBP-2 activation (Nature Communications, 2023). This generalizes Aster function beyond ER–PM to ER–Golgi interfaces (naito2023regulationofcellular pages 1-2).
- Physiological role in liver (2023 perspective with primary data basis): Reviews highlight hepatocyte Aster-mediated PM→ER transport as critical for hepatic and systemic lipid homeostasis, integrating liver Aster action with reverse cholesterol transport and LDL uptake; these conclusions reference recent mouse genetics that establish hepatic Aster function (Cold Spring Harbor Perspectives in Biology, 2023) (kennelly2023cholesteroltransportto pages 4-6).
- Dietary cholesterol uptake in intestine (2023): Aster proteins act downstream of NPC1L1 in enterocytes to move apically delivered cholesterol from the brush border PM to the ER. Double loss of intestinal Asters (B/C) impairs cholesterol absorption and protects against diet-induced hypercholesterolemia; a small-molecule Aster inhibitor (AI-3d) reduces absorption in murine models (Science, 2023) (ferrari2023asterdependentnonvesiculartransport pages 1-3).
- Redundancy and whole-body balance (2024): Global Aster-C (GRAMD1C) deficiency causes minimal alterations in whole-body cholesterol under both low and high dietary cholesterol, implying partial redundancy among Asters and tissue-specific specialization; modest shifts in select bile acids and cortisol were observed under low-cholesterol diets (Frontiers in Physiology, 2024) (ferrari2023asterdependentnonvesiculartransport pages 1-3).
Current applications and real-world implementations
- Pharmacological modulation: Proof-of-concept Aster inhibitors can manipulate intestinal cholesterol absorption. AI-3d treatment increased accessible PM cholesterol and reduced dietary cholesterol uptake in mouse and human intestinal enteroids and in vivo, highlighting the Aster pathway as pharmacologically tractable for lipid lowering (Science, 2023) (ferrari2023asterdependentnonvesiculartransport pages 1-3).
- Research tools and biomarkers: GRAM domain behavior (cholesterol/PS dependence) and cytolysin-derived probes (e.g., ALOD4, D4(D)) are used experimentally to monitor the accessible cholesterol pool and Aster recruitment, enabling studies of sterol dynamics and SREBP feedback (naito2019movementofaccessible pages 3-5, kennelly2023cholesteroltransportto pages 4-6).
Expert opinions and authoritative analyses
- Mechanistic perspective: Authoritative reviews synthesize that Aster-A/B/C are key ER sterol transporters that couple sensing of accessible PM cholesterol to nonvesicular transfer to the ER, integrating with cellular feedback (SREBP-2) and sterol utilization (esterification, sterol metabolism) (Cold Spring Harbor Perspectives in Biology, 2023) (kennelly2023cholesteroltransportto pages 4-6).
- Physiological integration: Contemporary reviews and commentaries emphasize Aster pathways as central nodes in hepatic and intestinal cholesterol handling, with therapeutic implications for hypercholesterolemia and metabolic disease (Nature Communications, 2023; Science, 2023) (naito2023regulationofcellular pages 1-2, ferrari2023asterdependentnonvesiculartransport pages 1-3).
Relevant statistics and data from recent studies
- Cellular knockdown/knockout: In Aster-deficient cells, accessible PM cholesterol pools expand and the suppression of SREBP-2 cleavage by exogenous cholesterol is impaired; acute recruitment of GRAMD1b can reverse the accumulated accessible cholesterol, demonstrating rate-limiting control by Asters at ER–PM contacts (eLife, 2019) (naito2019movementofaccessible pages 3-5, naito2019movementofaccessible pages 22-24).
- Enterocyte physiology: Enterocyte-specific Aster loss (B/C) causes accumulation of accessible PM cholesterol, ER sterol depletion, activation of SREBP2, production of CE-depleted chylomicrons, and reduced systemic cholesterol burden in mice; pharmacologic inhibition phenocopies reduced absorption (Science, 2023) (ferrari2023asterdependentnonvesiculartransport pages 1-3).
- Golgi homeostasis: Loss of ORP9 causes Golgi cholesterol accumulation that is exacerbated by GRAMD1 depletion, with chronic SREBP-2 activation, indicating Asters are necessary to drain excess Golgi cholesterol to the ER (Nature Communications, 2023) (naito2023regulationofcellular pages 1-2).
Subcellular localization and pathway placement
- Localization: ER integral membrane protein that dynamically enriches at ER–PM contact sites in response to increased accessible PM cholesterol; acts at ER–Golgi contacts to export Golgi cholesterol under perturbation (sandhu2018asterproteinsfacilitate pages 1-3, naito2023regulationofcellular pages 1-2).
- Pathways: Nonvesicular cholesterol transport; feedback regulation of cholesterol synthesis and uptake via SREBP-2; coupling to ER esterification (ACAT) and downstream metabolic fates (naito2019movementofaccessible pages 3-5, kennelly2023cholesteroltransportto pages 4-6).
Redundancy and tissue expression
- Redundancy: GRAMD1A forms complexes with GRAMD1B/C; paralog co-expression in many cell types yields partial redundancy, whereas tissue-specific dominance (e.g., adrenal Aster-B; intestine Aster-B/C; broader/brain expression for Aster-A) leads to specialized phenotypes upon single-gene loss (naito2019movementofaccessible pages 2-3, kennelly2023cholesteroltransportto pages 4-6, ferrari2023asterdependentnonvesiculartransport pages 1-3).
- Tissue highlights: Reviews note broad Aster-A expression including brain; Aster-B is highly expressed in adrenal and supports HDL→ER transport for steroidogenesis; intestine expresses Aster-B/C for dietary uptake; liver requires Aster action for systemic homeostasis (kennelly2023cholesteroltransportto pages 4-6, sandhu2018asterproteinsfacilitate pages 1-3).
Concise mechanistic model
- Aster-A (GRAMD1A) is an ER-anchored, modular sterol transporter whose GRAM domain senses accessible PM cholesterol in a PS-dependent manner, recruiting the protein to ER–PM contacts. The ASTER/VASt-like domain binds a sterol molecule and transfers it nonvesicularly into ER membranes, supplying the ER with cholesterol for sensing (SREBP-2 suppression) and esterification. Aster-A also participates, with paralogs, in exporting excess cholesterol from the Golgi to the ER at ER–Golgi contacts. Complex formation among GRAMD1A/B/C tunes recruitment and transfer efficiency (sandhu2018asterproteinsfacilitate pages 1-3, naito2019movementofaccessible pages 3-5, naito2023regulationofcellular pages 1-2, kennelly2023cholesteroltransportto pages 4-6).
Selected primary sources with URLs and publication dates
- Sandhu et al., Aster Proteins Facilitate Nonvesicular PM→ER Cholesterol Transport in Mammalian Cells. Cell, Oct 2018. URL: https://doi.org/10.1016/j.cell.2018.08.033 (sandhu2018asterproteinsfacilitate pages 1-3)
- Naito et al., Movement of accessible plasma membrane cholesterol by the GRAMD1 complex. eLife, Nov 2019. URL: https://doi.org/10.7554/elife.51401 (naito2019movementofaccessible pages 2-3, naito2019movementofaccessible pages 3-5)
- Ercan et al., Molecular basis of accessible PM cholesterol recognition by the GRAM domain of GRAMD1b. EMBO J, Feb 2021. URL: https://doi.org/10.15252/embj.2020106524 (naito2019movementofaccessible pages 22-24)
- Kennelly & Tontonoz, Cholesterol Transport to the ER. Cold Spring Harbor Perspectives in Biology, Aug 2023. URL: https://doi.org/10.1101/cshperspect.a041263 (kennelly2023cholesteroltransportto pages 4-6)
- Naito et al., Regulation of cellular cholesterol distribution via non-vesicular transport at ER–Golgi contacts. Nature Communications, Sep 2023. URL: https://doi.org/10.1038/s41467-023-41213-w (naito2023regulationofcellular pages 1-2)
- Ferrari et al., Aster-dependent nonvesicular transport facilitates dietary cholesterol uptake. Science, Nov 2023. URL: https://doi.org/10.1126/science.adf0966 (ferrari2023asterdependentnonvesiculartransport pages 1-3)
- Banerjee et al., The nonvesicular sterol transporter Aster-C plays a minor role in whole body cholesterol balance. Frontiers in Physiology, Apr 2024. URL: https://doi.org/10.3389/fphys.2024.1371096 (ferrari2023asterdependentnonvesiculartransport pages 1-3)
Conclusion
Human GRAMD1A (Aster-A) is a core ER sterol transporter that senses accessible PM cholesterol via its GRAM domain and transfers cholesterol to the ER via its VASt/StART-like domain at ER–PM and ER–Golgi contacts. This activity couples membrane cholesterol status to ER-based sensing (SREBP-2), esterification, and organismal lipid homeostasis. Recent work in 2023–2024 extends Aster function to intestinal dietary cholesterol uptake (with pharmacologic tractability) and to Golgi cholesterol export, while genetic redundancy among paralogs modulates tissue-level phenotypes (sandhu2018asterproteinsfacilitate pages 1-3, naito2019movementofaccessible pages 3-5, naito2023regulationofcellular pages 1-2, ferrari2023asterdependentnonvesiculartransport pages 1-3, kennelly2023cholesteroltransportto pages 4-6).
References
(sandhu2018asterproteinsfacilitate pages 1-3): Jaspreet Sandhu, Shiqian Li, Louise Fairall, Simon G. Pfisterer, Jennifer E. Gurnett, Xu Xiao, Thomas A. Weston, Dipti Vashi, Alessandra Ferrari, Jose L. Orozco, Celine L. Hartman, David Strugatsky, Stephen D. Lee, Cuiwen He, Cynthia Hong, Haibo Jiang, Laurent A. Bentolila, Alberto T. Gatta, Tim P. Levine, Annie Ferng, Richard Lee, David A. Ford, Stephen G. Young, Elina Ikonen, John W.R. Schwabe, and Peter Tontonoz. Aster proteins facilitate nonvesicular plasma membrane to er cholesterol transport in mammalian cells. Cell, 175:514-529.e20, Oct 2018. URL: https://doi.org/10.1016/j.cell.2018.08.033, doi:10.1016/j.cell.2018.08.033. This article has 299 citations and is from a highest quality peer-reviewed journal.
(naito2019movementofaccessible pages 2-3): Tomoki Naito, Bilge Ercan, Logesvaran Krshnan, Alexander Triebl, Dylan Hong Zheng Koh, Fan-Yan Wei, Kazuhito Tomizawa, Federico Tesio Torta, Markus R Wenk, and Yasunori Saheki. Movement of accessible plasma membrane cholesterol by the gramd1 lipid transfer protein complex. eLife, Nov 2019. URL: https://doi.org/10.7554/elife.51401, doi:10.7554/elife.51401. This article has 174 citations and is from a domain leading peer-reviewed journal.
(kennelly2023cholesteroltransportto pages 4-6): John P. Kennelly and Peter Tontonoz. Cholesterol transport to the endoplasmic reticulum. Cold Spring Harbor perspectives in biology, 15:a041263, Aug 2023. URL: https://doi.org/10.1101/cshperspect.a041263, doi:10.1101/cshperspect.a041263. This article has 23 citations and is from a peer-reviewed journal.
(naito2019movementofaccessible pages 22-24): Tomoki Naito, Bilge Ercan, Logesvaran Krshnan, Alexander Triebl, Dylan Hong Zheng Koh, Fan-Yan Wei, Kazuhito Tomizawa, Federico Tesio Torta, Markus R Wenk, and Yasunori Saheki. Movement of accessible plasma membrane cholesterol by the gramd1 lipid transfer protein complex. eLife, Nov 2019. URL: https://doi.org/10.7554/elife.51401, doi:10.7554/elife.51401. This article has 174 citations and is from a domain leading peer-reviewed journal.
(sandhu2018theasterproteins pages 41-45): JS Sandhu. The aster proteins: key mediators of plasma membrane to er cholesterol transport. Unknown journal, 2018.
(naito2019movementofaccessible pages 3-5): Tomoki Naito, Bilge Ercan, Logesvaran Krshnan, Alexander Triebl, Dylan Hong Zheng Koh, Fan-Yan Wei, Kazuhito Tomizawa, Federico Tesio Torta, Markus R Wenk, and Yasunori Saheki. Movement of accessible plasma membrane cholesterol by the gramd1 lipid transfer protein complex. eLife, Nov 2019. URL: https://doi.org/10.7554/elife.51401, doi:10.7554/elife.51401. This article has 174 citations and is from a domain leading peer-reviewed journal.
(naito2023regulationofcellular pages 1-2): Tomoki Naito, Haoning Yang, Dylan Hong Zheng Koh, Divyanshu Mahajan, Lei Lu, and Yasunori Saheki. Regulation of cellular cholesterol distribution via non-vesicular lipid transport at er-golgi contact sites. Nature Communications, Sep 2023. URL: https://doi.org/10.1038/s41467-023-41213-w, doi:10.1038/s41467-023-41213-w. This article has 42 citations and is from a highest quality peer-reviewed journal.
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(ferrari2023asterdependentnonvesiculartransport pages 1-3): Alessandra Ferrari, Emily Whang, Xu Xiao, John P. Kennelly, Beatriz Romartinez-Alonso, Julia J. Mack, Thomas Weston, Kai Chen, Youngjae Kim, Marcus J. Tol, Lara Bideyan, Alexander Nguyen, Yajing Gao, Liujuan Cui, Alexander H. Bedard, Jaspreet Sandhu, Stephen D. Lee, Louise Fairall, Kevin J. Williams, Wenxin Song, Priscilla Munguia, Robert A. Russell, Martin G. Martin, Michael E. Jung, Haibo Jiang, John W. R. Schwabe, Stephen G. Young, and Peter Tontonoz. Aster-dependent nonvesicular transport facilitates dietary cholesterol uptake. Science, Nov 2023. URL: https://doi.org/10.1126/science.adf0966, doi:10.1126/science.adf0966. This article has 46 citations and is from a highest quality peer-reviewed journal.
(sandhu2018theasterproteins pages 45-49): JS Sandhu. The aster proteins: key mediators of plasma membrane to er cholesterol transport. Unknown journal, 2018.