PLIN1
GeneName
PLIN1
Summary
PLIN1, also known as Perilipin or simply PLIN, is a 56 kDa protein that is primarily localised to lipid droplets within cells. It plays a pivotal role in the regulation of lipid metabolism and storage by coating lipid droplets and preventing unnecessary lipolysis. PLIN1 is expressed in various tissues, particularly in adipose tissue, where it is involved in the cellular response to cold and the overall lipid catabolic process. Its lipid-binding capability is essential for maintaining lipid droplet integrity and facilitating lipid metabolism.
Importance
PLIN1 is relevant to: - Understanding obesity and metabolic disorders due to its role in lipid storage and mobilisation - Investigating the mechanisms of cold-induced thermogenesis in adipose tissue - Exploring lipid-related diseases, including non-alcoholic fatty liver disease, as it influences lipid metabolism - Studying the dynamics of lipid droplets in various cellular contexts, which can provide insights into cellular energy homeostasis
Top Products
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Abcam Product Citation Summary
The data indicates that PLIN1 is being studied in the context of adipocyte hypertrophy, particularly in mouse adipose tissue. This suggests a focus on the role of PLIN1 in fat cell development and function.
Abcam Product Citation Table
Function
Modulator of adipocyte lipid metabolism. Coats lipid storage droplets to protect them from breakdown by hormone-sensitive lipase (HSL). Its absence may result in leanness. Plays a role in unilocular lipid droplet formation by activating CIDEC. Their interaction promotes lipid droplet enlargement and directional net neutral lipid transfer. May modulate lipolysis and triglyceride levels.
Involvement in disease
Lipodystrophy, familial partial, 4
FPLD4
A form of lipodystrophy characterized by loss of subcutaneous adipose tissue primarily affecting the lower limbs, insulin-resistant diabetes mellitus, hypertriglyceridemia, and hypertension.
None
The disease is caused by variants affecting the gene represented in this entry.
Post-translational modifications
Major cAMP-dependent protein kinase-substrate in adipocytes, also dephosphorylated by PP1. When phosphorylated, may be maximally sensitive to HSL and when unphosphorylated, may play a role in the inhibition of lipolysis, by acting as a barrier in lipid droplet (By similarity).
Sequence Similarities
Belongs to the perilipin family.
Tissue Specificity
Detected in adipocytes from white adipose tissue (at protein level) (PubMed:27832861). Detected in visceral adipose tissue and mammary gland (PubMed:9521880).
Cellular localization
- Endoplasmic reticulum
- Lipid droplet
- Lipid droplet surface-associated.
Alternative names
PERI, PLIN, PLIN1, Perilipin-1, Lipid droplet-associated protein