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PMID: 16962104 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Review

A proposed model of fat packaging by exchangeable lipid droplet proteins.

FEBS letters ·Vol. 580 ·No. 23 ·2006-10-09 ·Pages 5484-91

Wolins NE, Brasaemle DL, Bickel PE

Abstract

Humans have evolved mechanisms of efficient fat storage to survive famine, but these mechanisms contribute to obesity in our current environment of plentiful food and reduced activity. Little is known about how animals package fat within cells. Five related structural proteins serve roles in packaging fat into lipid droplets. The proteins TIP47, S3-12, and OXPAT/MLDP/PAT-1 move from the cytosol to coat nascent lipid droplets during rapid fat storage. In contrast, perilipin and adipophilin constitutively associate with lipid droplets and play roles in sustained fat storage and regulation of lipolysis. Different tissues express different complements of these lipid droplet proteins. Thus, the tissue-specific complement of these proteins determines how tissues manage lipid stores.

MeSH Terms
Adipose Tissue/metabolism Animals Humans Lipid Metabolism Models, Biological Protein Binding Proteins/metabolism Triglycerides/metabolism
Chemicals
Proteins Triglycerides
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Wolins Nathan E
Department of Medicine, Division of Endocrinology, Metabolism and Lipid Research, Washington University School of Medicine, Saint Louis, MO 63110, USA.
Brasaemle Dawn L
Bickel Perry E
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
2006-10-09
Epub
2006-00-01
Pages
5484-91
Language
English
Region
England
NLM ID
0155157
Subset
IM
Grants
NIDDK NIH HHS · DK059577 · United States
NIDDK NIH HHS · R01 DK068046 · United States
NIDDK NIH HHS · R01 DK54797 · United States
NIDDK NIH HHS · T32 DK07296 · United States
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