Structure of a Lipid Droplet Protein
Open accessAbstract
The perilipin/ADRP/TIP47 (PAT) proteins localize to the surface of intracellular neutral lipid droplets. Perilipin is essential for lipid storage and hormone regulated lipolysis in adipocytes, and perilipin null mice exhibit a dramatic reduction in adipocyte lipid stores. A significant fraction of the approximately 200 amino acid N-terminal region of the PAT proteins consists of 11-mer helical repeats that are also found in apolipoproteins and other lipid-associated proteins. The C-terminal 60% of TIP47, a representative PAT protein, comprises a monomeric and independently folded unit. The crystal structure of the C-terminal portion of TIP47 was determined and refined at 2.8 A resolution. The structure consists of an alpha/beta domain of novel topology and a four-helix bundle resembling the LDL receptor binding domain of apolipoprotein E. The structure suggests an analogy between PAT proteins and apolipoproteins in which helical repeats interact with lipid while the ordered C-terminal region is involved in protein:protein interactions.
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The N-terminal domain of APOE forms a four-helix bundle that is homologous to the four-helix bundle domain of the perilipin family of lipid droplet proteins.
“The N-terminal domain of APOE forms a four-helix bundle that is homologous to the four-helix bundle domain of the perilipin family of LD proteins (Hickenbottom et al., 2004).”
From APOE traffics to astrocyte lipid droplets and modulates triglyceride saturation and droplet size (2024) · cites this paper as Hickenbottom et al., 2004
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Three-Dimensional Structure of the LDL Receptor-Binding Domain of Human Apolipoprotein E
Wilson, C., Wardell, M. R., Weisgraber, K. H., Mahley, R. W., & Agard, D. A. (1991) · Science · doi:10.1126/science.2063194 · Cited by 678 · see citing works
Lipid Binding-induced Conformational Change in Human Apolipoprotein E
Saito, H., Dhanasekaran, P., Baldwin, F., Weisgraber, K. H., Lund-Katz, S., & Phillips, M. C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106337200 · Cited by 113 · see citing works
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Proteome-wide analysis of chaperone-mediated autophagy targeting motifs
Kirchner, P., Bourdenx, M., Madrigal-Matute, J., Tiano, S., Diaz, A., Bartholdy, B. A., Will, B., & Cuervo, A. M. (2019) · PLOS Biology · doi:10.1371/journal.pbio.3000301 · Cited by 257 · see citing works
The cell biology of APOE in the brain
Windham, I. A., & Cohen, S. (2024) · Trends in Cell Biology · doi:10.1016/j.tcb.2023.09.004 · Cited by 103 · see citing works
APOE traffics to astrocyte lipid droplets and modulates triglyceride saturation and droplet size
Windham, I. A., Powers, A. E., Ragusa, J. V., Wallace, E. D., Zanellati, M. C., Williams, V. H., Wagner, C. H., White, K. K., & Cohen, S. (2024) · Journal of Cell Biology · doi:10.1083/jcb.202305003 · Cited by 96 · see citing works
- Authors
- Hickenbottom, S. J., Kimmel, A. R., Londos, C., & Hurley, J. H.
- Affiliations
- National Institutes of Health (US)
- Corresponding author
- Hurley, James H
- Venue
- Structure
- Publisher
- Elsevier BV
- Published
- 2004-07
- Volume
- 12
- Issue
- 7
- Pages
- 1199-1207
- ISSN
- 0969-2126 (ISSN-L)
- OpenAlex
- W1986318660
- Cited by
- 193
- References
- 2
- Citations by year
- 2026: 6 · 2025: 5 · 2024: 6 · 2023: 9 · 2022: 2 · 2021: 7 · 2020: 9 · 2019: 9 · 2018: 7 · 2017: 11 · 2016: 5 · 2015: 6 · 2014: 11 · 2013: 21 · 2012: 8
- FWCI
- 4.94
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Structure (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- perilipin, ADRP, TIP47, PAT proteins, lipid droplets, crystal structure, helical repeat, alpha/beta domain, four-helix bundle, apolipoprotein E, protein-lipid interactions, protein-protein interaction, adipocytes, fat deposition, lipolysis
- MeSH terms
- Perilipin-1, Perilipin-2, Perilipin-3, Amino Acid Sequence, Animals, Carrier Proteins, DNA-Binding Proteins, Humans, Membrane Proteins, Models, Molecular, Molecular Sequence Data, Phosphoproteins, Pregnancy Proteins, Recombinant Fusion Proteins, Structure-Activity Relationship, Protein Structure, Secondary, Crystallography, X-Ray, Vesicular Transport Proteins, Intracellular Signaling Peptides and Proteins, Lipid Metabolism, Mice
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