Target type: biologicalprocess
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a lipid particle. [GOC:dph, GOC:jl, GOC:mah, PMID:18093937, PMID:18250201]
Lipid droplet organization is a complex and dynamic process that involves the assembly, growth, and degradation of lipid droplets, which are specialized organelles that store neutral lipids, such as triglycerides and cholesterol esters. This process is essential for cellular energy storage, membrane biogenesis, and lipid signaling. The formation of lipid droplets begins with the accumulation of neutral lipids in the endoplasmic reticulum (ER), where they are synthesized by enzymes such as diacylglycerol acyltransferase (DGAT). These newly synthesized lipids form small, spherical structures called nascent lipid droplets, which bud off from the ER membrane. As these nascent lipid droplets grow larger, they recruit proteins from the ER, cytosol, and other organelles, forming a complex coat that surrounds the lipid droplet. These proteins play a crucial role in regulating lipid droplet size, stability, and interactions with other cellular components. The recruitment of these proteins is often mediated by specific lipid binding domains, such as the PAT (perilipin, ADRP, TIP47) domain, which is found in a family of lipid droplet-associated proteins. These proteins also contribute to the formation of lipid droplet clusters, which can facilitate efficient lipid storage and utilization. The size and number of lipid droplets can vary significantly depending on the cell type, metabolic state, and environmental conditions. For example, adipocytes, the cells that store fat, contain large lipid droplets that can occupy most of the cell volume. In contrast, other cell types may have smaller, more numerous lipid droplets. Lipid droplet organization is tightly regulated by a complex interplay of proteins, lipids, and cellular signaling pathways. The size, number, and distribution of lipid droplets can be influenced by factors such as nutrient availability, hormones, and stress. Disruptions in lipid droplet organization can contribute to the development of metabolic disorders such as obesity, diabetes, and fatty liver disease.'
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Protein | Definition | Taxonomy |
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Peptidyl-prolyl cis-trans isomerase D | A eukaryotic-type peptidyl-prolyl cis-trans isomerase D that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q08752] | Homo sapiens (human) |
Peptidyl-prolyl cis-trans isomerase A | A peptidyl-prolyl cis-trans isomerase A that is encoded in the genome of human. [PRO:DNx, UniProtKB:P62937] | Homo sapiens (human) |
Compound | Definition | Classes | Roles |
---|---|---|---|
2,4-pyridinedicarboxylic acid | lutidinic acid : A pyridinedicarboxylic acid carrying carboxy groups at positions 2 and 4. | pyridinedicarboxylic acid | |
daminozide | daminozide: induces tumors | straight-chain fatty acid | |
prolinal | pyrrolidines | ||
oxalylglycine | N-oxalylglycine : An amino dicarboxylic acid that is iminodiacetic acid with an oxo substituent. It is used as an inhibitor of alpha-ketoglutarate dependent (EC 1.14.11.*) enzymes. oxalylglycine: structure given in first source | amino dicarboxylic acid; N-acylglycine | EC 1.14.11.* (oxidoreductase acting on paired donors, 2-oxoglutarate as one donor, incorporating 1 atom each of oxygen into both donors) inhibitor |
cyclosporine | ramihyphin A: one of the metabolites produced by Fusarium sp. S-435; RN given refers to cpd with unknown MF | homodetic cyclic peptide | anti-asthmatic drug; anticoronaviral agent; antifungal agent; antirheumatic drug; carcinogenic agent; dermatologic drug; EC 3.1.3.16 (phosphoprotein phosphatase) inhibitor; geroprotector; immunosuppressive agent; metabolite |
sanglifehrin a | sanglifehrin A: binds cyclophilin A; isolated from Streptomyces; structure in first source | ||
(melle-4)cyclosporin | (melle-4)cyclosporin: a non-immunosuppressive analog of cyclosporin A | ||
cyclosporin g | cyclosporin G: similar immunosuppressive actions as cyclosporin, but without nephrotoxic side effects; cyclosporin A analog; MW 1217 | ||
scy-635 | |||
nutlin-3a | nutlin 3: an MDM2 antagonist; structure in first source | stilbenoid | |
alisporivir | alisporivir: nonimmunosuppressive cyclosporin analog; structure/sequence in first source | homodetic cyclic peptide | anticoronaviral agent |