A proposed model of fat packaging by exchangeable lipid droplet proteins

Nathan E. Wolins; Dawn L. Brasaemle; Perry E. Bickel

doi:10.1016/j.febslet.2006.08.040

A proposed model of fat packaging by exchangeable lipid droplet proteins

Nathan E. Wolins, Dawn L. Brasaemle, Perry E. Bickel

Research output: Contribution to journal › Short survey › peer-review

330 Scopus citations

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.

Original language	English (US)
Pages (from-to)	5484-5491
Number of pages	8
Journal	FEBS Letters
Volume	580
Issue number	23
DOIs	https://doi.org/10.1016/j.febslet.2006.08.040
State	Published - Oct 9 2006

Keywords

ADRP
Adipophilin
Lipid droplet
MLDP
OXPAT
PAT proteins
PAT-1
Perilipin
S3-12
TIP47
Triacylglycerol

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/j.febslet.2006.08.040

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title = "A proposed model of fat packaging by exchangeable lipid droplet proteins",

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.",

keywords = "ADRP, Adipophilin, Lipid droplet, MLDP, OXPAT, PAT proteins, PAT-1, Perilipin, S3-12, TIP47, Triacylglycerol",

author = "Wolins, {Nathan E.} and Brasaemle, {Dawn L.} and Bickel, {Perry E.}",

note = "Funding Information: The authors thank James R. Skinner, Michelle Mo, and Benjamin Quaynor for expert technical assistance. We thank James R. Skinner and Dr. Robert P. Donaldson for critical review of the manuscript. The authors acknowledge support by Grants from NIH (RO1 DK068046 and DK059577, to P.E.B.; RO1 DK54797, to D.L.B.; and T32 DK07296, to N.E.W.), from the American Diabetes Association (to P.E.B. and to N.E.W.), and from the American Heart Association (to D.L.B.).",

year = "2006",

month = oct,

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doi = "10.1016/j.febslet.2006.08.040",

language = "English (US)",

volume = "580",

pages = "5484--5491",

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TY - JOUR

T1 - A proposed model of fat packaging by exchangeable lipid droplet proteins

AU - Wolins, Nathan E.

AU - Brasaemle, Dawn L.

AU - Bickel, Perry E.

N1 - Funding Information: The authors thank James R. Skinner, Michelle Mo, and Benjamin Quaynor for expert technical assistance. We thank James R. Skinner and Dr. Robert P. Donaldson for critical review of the manuscript. The authors acknowledge support by Grants from NIH (RO1 DK068046 and DK059577, to P.E.B.; RO1 DK54797, to D.L.B.; and T32 DK07296, to N.E.W.), from the American Diabetes Association (to P.E.B. and to N.E.W.), and from the American Heart Association (to D.L.B.).

PY - 2006/10/9

Y1 - 2006/10/9

N2 - 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.

AB - 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.

KW - ADRP

KW - Adipophilin

KW - Lipid droplet

KW - MLDP

KW - OXPAT

KW - PAT proteins

KW - PAT-1

KW - Perilipin

KW - S3-12

KW - TIP47

KW - Triacylglycerol

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DO - 10.1016/j.febslet.2006.08.040

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C2 - 16962104

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SN - 0014-5793

VL - 580

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JO - FEBS Letters

JF - FEBS Letters

IS - 23

ER -

A proposed model of fat packaging by exchangeable lipid droplet proteins

Abstract

Keywords

ASJC Scopus subject areas

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