The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
PAT proteins, an ancient family of lipid droplet proteins that regulate cellular lipid stores
Open accessAbstract
Summary The PAT family of lipid droplet proteins includes 5 members in mammals: perilipin, adipose differentiation-related protein (ADRP), tail-interacting protein of 47 kiloDaltons (TIP47), S3-12, and OXPAT. Members of this family are also present in evolutionarily distant organisms, including insects, slime molds and fungi. All PAT proteins share sequence similarity and the ability to bind intracellular lipid droplets, either constitutively or in response to metabolic stimuli, such as increased lipid flux into or out of lipid droplets. Positioned at the lipid droplet surface, PAT proteins manage access of other proteins (lipases) to the lipid esters within the lipid droplet core and can interact with cellular machinery important for lipid droplet biogenesis. Genetic variations in the gene for the best characterized of the mammalian PAT proteins, perilipin, have been associated with metabolic phenotypes, including type 2 diabetes mellitus and obesity. In this review, we discuss how the PAT proteins regulate cellular lipid metabolism both in mammals and in model organisms.
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Cites
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Perilipin Expression in Human Adipose Tissues: Effects of Severe Obesity, Gender, and Depot
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Adipophilin is a sensitive marker for lipid loading in human blood monocytes
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Caseation of human tuberculosis granulomas correlates with elevated host lipid metabolism
Kim, M., Wainwright, H. C., Locketz, M., Bekker, L., Walther, G. B., Dittrich, C., Visser, A., Wang, W., Hsu, F., Wiehart, U., et al. (2010) · EMBO Molecular Medicine · doi:10.1002/emmm.201000079 · Cited by 489
Alcohol effects on hepatic lipid metabolism
Jeon, S., & Carr, R. (2020) · Journal of Lipid Research · doi:10.1194/jlr.r119000547 · Cited by 326
Lipid droplets: A dynamic organelle moves into focus
Beller, M., Thiel, K., Thul, P. J., & Jäckle, H. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.03.022 · Cited by 263
Mitochondrial and cellular mechanisms for managing lipid excess
Aon, M. A., Bhatt, N., & Cortassa, S. C. (2014) · Frontiers in Physiology · doi:10.3389/fphys.2014.00282 · Cited by 253
“The adipose tissue LD has a core predominantly formed by TAG whereas in most cells cholesterol and TAG share the nuclear core of the LD (Singh and Cuervo, 2012).”
BackgroundRole of intramyocelluar lipids in human health
Coen, P. M., & Goodpaster, B. H. (2012) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2012.05.009 · Cited by 252
Metadata
- Authors
- Bickel, P. E., Tansey, J. T., & Welte, M. A.
- Venue
- Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids
- Publisher
- Elsevier BV
- Published
- 2009-06
- Volume
- 1791
- Issue
- 6
- Pages
- 419-440
- ISSN
- 1388-1981 (ISSN-L)
- OpenAlex
- W2060905615
- Cited by
- 670
- References
- 8
- FWCI
- 20.87
- Type
- journal article
- Language
- en
- Open access
- green
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