☆ 4.7 Review

Seipin-still a mysterious protein?

FRONTIERS IN CELL AND DEVELOPMENTAL BIOLOGY (2023)

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Key Factors Governing Initial Stages of Lipid Droplet Formation

Siyoung Kim et al.

Summary: This study investigates the initial stages of lipid droplet formation using a simplified model. The findings reveal that the rigidity of phospholipids plays a crucial role in droplet formation and membrane remodeling, while asymmetric tension determines the direction of bud growth. Additionally, two mechanisms of droplet growth, Ostwald ripening and merging, are observed.

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Article Chemistry, Multidisciplinary

Lipid Droplets Embedded in a Model Cell Membrane Create a Phospholipid Diffusion Barrier

Sevde Puza et al.

Summary: Lipid droplets (LDs) are organelles derived from the endoplasmic reticulum (ER) membrane and play a crucial role in lipid storage. The distribution of proteins between phospholipid bilayer and LD monolayer membranes is determined by the collective properties of protein-intrinsic and lipid-mediated features. In this study, researchers produced a freestanding phospholipid bilayer using microfluidics and observed the insertion of micrometer-sized LDs into the bilayer. They found that the LDs presented a lens shape and there was a diffusion barrier between the LD monolayer and the bilayer. This barrier may influence the partitioning of proteins between the ER membrane and LDs in living cells.

SMALL (2022)

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Article Cell Biology

Seipin localizes at endoplasmic-reticulum-mitochondria contact sites to control mitochondrial calcium import and metabolism in adipocytes

Yoann Combot et al.

Summary: Deficiency of seipin, an ER protein, leads to mitochondrial abnormalities and dysfunctions in adipose tissue. Seipin controls mitochondrial energy metabolism by regulating mitochondrial calcium influx at ER-mitochondria contact sites (MAMs). Reduced ATP production in seipin-deficient adipose tissue contributes to the development of lipodystrophy.

CELL REPORTS (2022)

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Article Cell Biology

Seipin collaborates with the ER membrane to control the sites of lipid droplet formation

Roger Schneiter et al.

Summary: Most cells store metabolic energy in lipid droplets (LDs), which consist of a hydrophobic core covered by a phospholipid monolayer. Recent evidence suggests that LD formation occurs in specific subdomains of the endoplasmic reticulum (ER) where proteins gather to initiate LD assembly. The lipodystrophy protein Seipin plays a crucial role in LD biogenesis by forming a large oligomeric toroidal structure that promotes LD nucleation. This article discusses the role of LD biogenesis factors that interact with Seipin to assemble functional LDs.

CURRENT OPINION IN CELL BIOLOGY (2022)

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Article Cell Biology

Lipid droplets form a network interconnected by the endoplasmic reticulum through which their proteins equilibrate

Stephanie Cottier et al.

Summary: Lipid droplets (LDs) are intracellular structures for neutral lipid storage, and their protein transfer is influenced by yeast cell fusion and the ER membrane. This transfer is continuous, bidirectional, and the LDs are interconnected through the ER membrane.

JOURNAL OF CELL SCIENCE (2022)

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Article Cell Biology

MOSPD2 is an endoplasmic reticulum-lipid droplet tether functioning in LD homeostasis

Mehdi Zouiouich et al.

Summary: Membrane contact sites between organelles are organized by protein bridges. MOSPD2, a member of the ER-anchored VAP family, forms contacts with lipid droplets through its CRAL-TRIO domain. The presence of MOSPD2 is crucial for the assembly of lipid droplets.

JOURNAL OF CELL BIOLOGY (2022)

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Article Biochemistry & Molecular Biology

Seipin forms a flexible cage at lipid droplet formation sites

Henning Arlt et al.

Summary: This study reports the structure of yeast seipin and suggests that it forms a flexible, cage-like structure in the endoplasmic reticulum membrane, facilitating lipid droplet formation and growth.

NATURE STRUCTURAL & MOLECULAR BIOLOGY (2022)

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Article Biology

Seipin transmembrane segments critically function in triglyceride nucleation and lipid droplet budding from the membrane

Siyoung Kim et al.

Summary: By utilizing molecular dynamics simulations and cell-based experiments, this study provides insights into the functions of seipin in lipid droplet (LD) biogenesis and maturation, including its roles in protein-lipid interactions, lipid diffusion, and LD formation and growth.

ELIFE (2022)

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Article Cell Biology

ORP5 and ORP8 orchestrate lipid droplet biogenesis and maintenance at ER-mitochondria contact sites

Valentin Guyard et al.

Summary: This study reveals the role of lipid transfer proteins ORP5 and ORP8 in controlling lipid droplet (LD) biogenesis at mitochondria-associated ER membrane (MAM) subdomains. It uncovers their involvement in LD nucleation and growth and emphasizes the importance of the integrity of ER-mitochondria contact sites for this process.

JOURNAL OF CELL BIOLOGY (2022)

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Lens Nucleation and Droplet Budding in a Membrane Model for Lipid Droplet Biogenesis

Frederik Viktor Hegaard et al.

Summary: Lipid droplet biogenesis, involving the formation and budding of droplets in cells, is a dynamic process that is not well understood. This study develops a controlled experimental system to model lipid droplet biogenesis and provides insights into the mechanism of droplet formation.

LANGMUIR (2022)

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Article Cell Biology

Triglyceride lipolysis triggers liquid crystalline phases in lipid droplets and alters the LD proteome

Sean Rogers et al.

Summary: The study reveals that yeast glucose restriction can induce liquid crystalline phase transitions and lipid demixing in lipid droplets, leading to selective remodeling of their proteome.

JOURNAL OF CELL BIOLOGY (2022)

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Article Biochemistry & Molecular Biology

Mice deficient in ER protein seipin have reduced adrenal cholesteryl ester lipid droplet formation and utilization

Wen-Jun Shen et al.

Summary: Cholesteryl ester-rich lipid droplets (LDs) play a crucial role in the synthesis of steroid hormones. Seipin protein is essential for the accumulation and formation of CE-rich LDs and its deficiency leads to severe abnormalities in LD maturation and morphology.

JOURNAL OF LIPID RESEARCH (2022)

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Article Cell Biology

PI(3)P and DFCP1 regulate the biogenesis of lipid droplets

Ivan Lukmantara et al.

Summary: In this study, we identified PI(3)P as a novel regulator of lipid droplet (LD) biogenesis, which impacts LD formation and lipidation through DFCP1. Disruption of cellular PI(3)P homeostasis affects the normal function and localization of DFCP1.

MOLECULAR BIOLOGY OF THE CELL (2022)

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Article Cell Biology

Identification of two pathways mediating protein targeting from ER to lipid droplets

Jiunn Song et al.

Summary: The study identifies two protein targeting pathways from the endoplasmic reticulum to lipid droplets and defines the key factors and mechanisms involved. These pathways play essential roles in the organization and function of eukaryotic cells.

NATURE CELL BIOLOGY (2022)

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Article Cell Biology

Seipin concentrates distinct neutral lipids via interactions with their acyl chain carboxyl esters

Mike F. Renne et al.

Summary: Renne et al. demonstrate that Seipin plays a role in the formation of lipid droplets containing different types of neutral lipids. The interaction between hydroxyl-residues and neutral lipid carboxyl esters is proposed as a general mechanism for Seipin-mediated lipid droplet formation. This finding provides insights into the cellular processes of lipid homeostasis and the function of Seipin.

JOURNAL OF CELL BIOLOGY (2022)

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Article Biophysics

Origin of gradients in lipid density and surface tension between connected lipid droplet and bilayer

Aymeric Chorlay et al.

Summary: The study utilized theory and experiments to investigate the physical parameters affecting phospholipid density and tension equilibrium between a bilayer and an oil droplet. It revealed the molecular interactions controlling the PL densities of the droplet monolayer and the bilayer, showing that the droplet monolayer has a lower density and higher surface tension compared to the bilayer. The research emphasizes the necessity of a PL density gradient for maintaining the mechanical and thermodynamic equilibrium of the droplet-bilayer continuity.

BIOPHYSICAL JOURNAL (2021)

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Article Biochemistry & Molecular Biology

CG32803 is the fly homolog of LDAF1 and influences lipid storage in vivo

Eugenia Chartschenko et al.

Summary: Seipin protein plays a key role in lipid droplets (LDs) biogenesis, with recent findings showing a cooperation between human Seipin and Lipid droplet assembly factor 1 (LDAF1). LDAF1 proteins may have an evolutionarily conserved function in LDs biogenesis, with certain functional aspects shared between LDO and mammalian LDAF1 proteins. The relationship between LDO and LDAF1 proteins is still under debate.

INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY (2021)

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Article Cell Biology

Nuclear lipid droplets form in the inner nuclear membrane in a seipin-independent manner

Kamil Soltysik et al.

Summary: The inner nuclear membrane of U2OS cells contains triglyceride synthesis enzymes that generate nuclear lipid droplets in situ. Inhibition of mTOR increases nuclear lipid droplets by inducing nuclear translocation of lipin-1 phosphatidic acid phosphatase. Seipin, essential for normal cytoplasmic lipid droplet formation, is absent in the inner nuclear membrane and restrains nuclear lipid droplet formation by affecting lipin-1 expression and intracellular phosphatidic acid distribution.

JOURNAL OF CELL BIOLOGY (2021)

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Article Biochemistry & Molecular Biology

Seipin traps triacylglycerols to facilitate their nanoscale clustering in the endoplasmic reticulum membrane

Xavier Prasanna et al.

Summary: Seipin can trap TAGs in the ER bilayer via its luminal hydrophobic helices, serving as a catalyst for seeding the TAG cluster and generating a favorable promethin binding interface.

PLOS BIOLOGY (2021)

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Review Cell Biology

Lipid Droplet Nucleation

Abdou Rachid Thiam et al.

Summary: This review focuses on the nucleation step of lipid droplet assembly, discussing how membrane biophysical and physicochemical properties control this process and the role of proteins in orchestrating lipid droplet biogenesis.

TRENDS IN CELL BIOLOGY (2021)

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Article Biology

Pre-existing bilayer stresses modulate triglyceride accumulation in the ER versus lipid droplets

Valeria Zoni et al.

Summary: The interactions between lipid acyl-chains play a key role in regulating the storage of neutral lipids in lipid droplets, affecting their distribution in cells. Different types of acyl-chains have distinct effects on lipid droplet formation and lipid storage.

ELIFE (2021)

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Article Multidisciplinary Sciences

Mechanism of lipid droplet formation by the yeast Sei1/Ldb16 Seipin complex

Yoel A. Klug et al.

Summary: The study revealed the mechanism of lipid droplet formation by the coordination of yeast Seipin Sei1 and its partner Ldb16. Sei1 assembles a homooligomeric ring in the ER to concentrate triacylglycerol, promoting Ldb16 stability and lipid droplet assembly.

NATURE COMMUNICATIONS (2021)

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Article Cardiac & Cardiovascular Systems

Seipin Deficiency Accelerates Heart Failure Due to Calcium Handling Abnormalities and Endoplasmic Reticulum Stress in Mice

Xiaoyue Wu et al.

Summary: Seipin deficiency can lead to hypertrophic cardiomyopathy and heart failure in mice after TAC, likely due to impaired myocardial calcium handling, ER stress, inflammation, and apoptosis.

FRONTIERS IN CARDIOVASCULAR MEDICINE (2021)

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Article Cell Biology

FIT2 organizes lipid droplet biogenesis with ER tubule-forming proteins and septins

Fang Chen et al.

Summary: FIT2 interacts with ER tubule-forming proteins and septin 7 to facilitate nascent LD biogenesis. Depletion of these proteins leads to a decrease in the number and size of LDs within cells.

JOURNAL OF CELL BIOLOGY (2021)

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Article Cell Biology

Retinyl esters form lipid droplets independently of triacylglycerol and seipin

Martijn R. Molenaar et al.

Summary: The study demonstrates an alternative pathway of lipid droplet biogenesis independent of seipin, where retinyl esters can spontaneously accumulate and form lipid droplets in lipid bilayers. Even in cells that do not normally produce retinyl esters, the production of retinyl esters can induce the formation of lipid droplets.

JOURNAL OF CELL BIOLOGY (2021)

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Review Cell Biology

Seipin: harvesting fat and keeping adipocytes healthy

Monala Jayaprakash Rao et al.

Summary: Seipin plays a crucial role in the assembly and maintenance of cytoplasmic lipid droplets, and its absence can lead to lipodystrophy. New evidence suggests that Seipin attracts triglyceride monomers for droplet formation, but may not be directly involved in the assembly of nuclear lipid droplets. Additionally, Seipin may also suppress the formation of nuclear lipid droplets.

TRENDS IN CELL BIOLOGY (2021)

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Article Cell Biology

Specific subdomain localization of ER resident proteins and membrane contact sites resolved by electron microscopy

Behnam Lak et al.

Summary: The endoplasmic reticulum is a complex organelle with diverse structural subdomains, and the localization of ER proteins is influenced by cellular environment and correct protein expression level. An analysis of ER-mitochondria contacts revealed different types of membrane contact sites that responded differently to changes in cellular lipid loading status.

EUROPEAN JOURNAL OF CELL BIOLOGY (2021)

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Oligomers of the lipodystrophy protein seipin may co-ordinate GPAT3 and AGPAT2 enzymes to facilitate adipocyte differentiation

M. F. Michelle Sim et al.

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Membrane Curvature Catalyzes Lipid Droplet Assembly

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Seipin and Nem1 establish discrete ER subdomains to initiate yeast lipid droplet biogenesis

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Lipid droplet biogenesis: A mystery unmixing?

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SEIPIN Isoforms Interact with the Membrane-Tethering Protein VAP27-1 for Lipid Droplet Formation[OPEN]

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Direct lysosome-based autophagy of lipid droplets in hepatocytes

Ryan J. Schulze et al.

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Cerebellar ataxia disease-associated Snx14 promotes lipid droplet growth at ER-droplet contacts

Sanchari Datta et al.

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SEIPIN overexpression in the liver may alleviate hepatic steatosis by influencing the intracellular calcium level

Qiang Li et al.

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Promethin Is a Conserved Seipin Partner Protein

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The ER-Localized Protein DFCP1 Modulates ER-Lipid Droplet Contact Formation

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Membrane Asymmetry Imposes Directionality on Lipid Droplet Emergence from the ER

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Seipin Facilitates Triglyceride Flow to Lipid Droplet and Counteracts Droplet Ripening via Endoplasmic Reticulum Contact

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The biogenesis of lipid droplets: Lipids take center stage

Mingming Gao et al.

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Dietary fatty acids promote lipid droplet diversity through seipin enrichment in an ER subdomain

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Liquid-crystalline phase transitions in lipid droplets are related to cellular states and specific organelle association

Julia Mahamid et al.

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LDAF1 and Seipin Form a Lipid Droplet Assembly Complex

Jeeyun Chung et al.

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Identification of seipin-linked factors that act as determinants of a lipid droplet subpopulation

Michal Eisenberg-Bord et al.

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Regulation of lipid droplets by metabolically controlled Ldo isoforms

Vitor Teixeira et al.

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Architecture of Lipid Droplets in Endoplasmic Reticulum Is Determined by Phospholipid Intrinsic Curvature

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Rab18 promotes lipid droplet (LD) growth by tethering the ER to LDs through SNARE and NRZ interactions

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Seipin regulates lipid homeostasis by ensuring calcium-dependent mitochondrial metabolism

Long Ding et al.

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VPS13A and VPS13C are lipid transport proteins differentially localized at ER contact sites

Nikit Kumar et al.

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Lipid droplet and peroxisome biogenesis occur at the same ER subdomains

Amit S. Joshi et al.

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Seipin and the membrane-shaping protein Pex30 cooperate in organelle budding from the endoplasmic reticulum

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Human SEIPIN Binds Anionic Phospholipids

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Pet10p is a yeast perilipin that stabilizes lipid droplets and promotes their assembly

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ER Membrane Phospholipids and Surface Tension Control Cellular Lipid Droplet Formation

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Seipin regulates ER-lipid droplet contacts and cargo delivery

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SEIPIN Regulates Lipid Droplet Expansion and Adipocyte Development by Modulating the Activity of Glycerol-3-phosphate Acyltransferase

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Seipin is required for converting nascent to mature lipid droplets

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Seipin is involved in the regulation of phosphatidic acid metabolism at a subdomain of the nuclear envelope in yeast

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Dissecting seipin function: the localized accumulation of phosphatidic acid at ER/LD junctions in the absence of seipin is suppressed by Sei1pΔNterm only in combination with Ldb16p

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The seipin complex Fld1/Ldb16 stabilizes ER-lipid droplet contact sites

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A conserved family of proteins facilitates nascent lipid droplet budding from the ER

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Seipin oligomers can interact directly with AGPAT2 and lipin 1, physically scaffolding critical regulators of adipogenesis

Md Mesbah Uddin Talukder et al.

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Seipin Promotes Adipose Tissue Fat Storage through the ER Ca2+-ATPase SERCA

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Control of lipid droplet size in budding yeast requires the collaboration between Fld1 and Ldb16

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Lack of testicular seipin causes teratozoospermia syndrome in men

Min Jiang et al.

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Acyl-CoA synthetase 3 promotes lipid droplet biogenesis in ER microdomains

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A new seipin-associated neurodegenerative syndrome

Encarna Guillen-Navarro et al.

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The biophysics and cell biology of lipid droplets

Abdou Rachid Thiam et al.

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The human lipodystrophy protein seipin is an ER membrane adaptor for the adipogenic PA phosphatase lipin 1

M. F. Michelle Sim et al.

MOLECULAR METABOLISM (2013)

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Perilipin family members preferentially sequester to either triacylglycerol-specific or cholesteryl-ester-specific intracellular lipid storage droplets

Kai Hsieh et al.

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Translation Inhibitors Induce Formation of Cholesterol Ester-Rich Lipid Droplets

Michitaka Suzuki et al.

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Fsp27 promotes lipid droplet growth by lipid exchange and transfer at lipid droplet contact sites

Jingyi Gong et al.

JOURNAL OF CELL BIOLOGY (2011)

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The yeast lipin orthologue Pah1p is important for biogenesis of lipid droplets

Oludotun Adeyo et al.

JOURNAL OF CELL BIOLOGY (2011)

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Lipid droplets are functionally connected to the endoplasmic reticulum in Saccharomyces cerevisiae

Nicolas Jacquier et al.

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A Role for Phosphatidic Acid in the Formation of Supersized Lipid Droplets

Weihua Fei et al.

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Seipin Is a Discrete Homooligomer

Derk Binns et al.

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Triglyceride Blisters in Lipid Bilayers: Implications for Lipid Droplet Biogenesis and the Mobile Lipid Signal in Cancer Cell Membranes

Himanshu Khandelia et al.

PLOS ONE (2010)

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Seipin deficiency alters fatty acid Δ9 desaturation and lipid droplet formation in Berardinelli-Seip congenital lipodystrophy

Emilie Boutet et al.

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Seipinopathy: a novel endoplasmic reticulum stress-associated disease

Daisuke Ito et al.

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Structural and biochemical properties of lipid particles from the yeast Saccharomyces cerevisiae

Tibor Czabany et al.

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Fld1p, a functional homologue of human seipin, regulates the size of lipid droplets in yeast

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The lipodystrophy protein seipin is found at endoplasmic reticulum lipid droplet junctions and is important for droplet morphology

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Membrane topology of the human seipin protein

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