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The PKA-mediated phosphorylation of serine 492 of perilipin A promotes lipolysis by triggering lipid droplet dispersion

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TitleInfo (displayLabel = Citation Title); (type = uniform)
Title
The PKA-mediated phosphorylation of serine 492 of perilipin A promotes lipolysis by triggering lipid droplet dispersion
Name (ID = NAME001); (type = personal)
NamePart (type = family)
Liang
NamePart (type = given)
Xiaofang
DisplayForm
Xiaofang Liang
Role
RoleTerm (authority = RULIB)
author
Name (ID = NAME002); (type = personal)
NamePart (type = family)
Brasaemle
NamePart (type = given)
Dawn
Affiliation
Advisory Committee
DisplayForm
Dawn L Brasaemle
Role
RoleTerm (authority = RULIB)
chair
Name (ID = NAME003); (type = personal)
NamePart (type = family)
Carman
NamePart (type = given)
George
Affiliation
Advisory Committee
DisplayForm
George M Carman
Role
RoleTerm (authority = RULIB)
internal member
Name (ID = NAME004); (type = personal)
NamePart (type = family)
Cohick
NamePart (type = given)
Wendie
Affiliation
Advisory Committee
DisplayForm
Wendie S Cohick
Role
RoleTerm (authority = RULIB)
internal member
Name (ID = NAME005); (type = corporate)
NamePart
Rutgers University
Role
RoleTerm (authority = RULIB)
degree grantor
Name (ID = NAME006); (type = corporate)
NamePart
Graduate School - New Brunswick
Role
RoleTerm (authority = RULIB)
school
TypeOfResource
Text
Genre (authority = marcgt)
theses
OriginInfo
DateCreated (qualifier = exact)
2008
DateOther (qualifier = exact); (type = degree)
2008-10
Language
LanguageTerm
English
PhysicalDescription
Form (authority = marcform)
electronic
InternetMediaType
application/pdf
InternetMediaType
text/xml
Extent
ix, 58 pages
Abstract
The lipid droplet protein perilipin A plays a key role in regulating triglyceride storage and hydrolysis. The phosphorylation of perilipin A by PKA facilitates lipolysis mediated by hormone-sensitive lipase (HSL) and adipose triglyceride lipase (ATGL) in adipocytes. Previous studies show that the phosphorylation of serine 492 of perilipin A drives lipid droplet fragmentation and dispersion following PKA-activation. These studies address the hypothesis that lipid droplet dispersion triggered by the phosphorylation of serine 492 promotes PKA-stimulated lipolysis. Adenoviral constructs encoding ectopic perilipin A (PeriA) and three mutated forms were generated, including 1) Not5, with all PKA site serines mutated to alanine or glutamic acid except PKA site #5; 2) S492A, with a single mutation of the fifth PKA site serine to alanine; and 3) All5, with all PKA sites serines substituted with alanine or glutamic acid. All forms of perilipin A and β-galactosidase were expressed in NIH 3T3 CarΔ fibroblasts, which express ATGL but lack endogenous perilipin A and HSL. Cells expressing unmodified perilipin A and mutated forms had similar levels of basal lipolysis. Six hours treatment with forskolin/IBMX in PeriA cells increases lipolysis by 2.2-fold, to levels similar to those of control cells expressing β-galactosidase. When compared to lipolysis in PeriA cells, phosphorylation of serine 492 alone (Not5) contributes to 77.5% of maximal lipolysis, whereas phosphorylation of all five other PKA sites (S492A) yields only 66.6% of maximal lipolysis. Stimulated lipolysis in cells expressing perilipin lacking all PKA sites (All5) increased only 16% over basal levels. Immunofluorescence microscopy shows that phosphorylation of serine 492 is necessary and sufficient to drive the full dispersion of lipid droplets following PKA-stimulation. In conclusion, PKA-mediated phosphorylation of serine 492 of perilipin A facilitates lipolysis at least partially through the stimulation of lipid droplet dispersion.
Note (type = degree)
M.S.
Note (type = bibliography)
Includes bibliographical references (p. 53-58).
Subject (ID = SUBJ1); (authority = RUETD)
Topic
Nutritional Sciences
Subject (ID = SUBJ2); (authority = ETD-LCSH)
Topic
Proteins
Subject (ID = SUBJ3); (authority = ETD-LCSH)
Topic
Lipids
Subject (ID = SUBJ4); (authority = ETD-LCSH)
Topic
Fat cells
Subject (ID = SUBJ5); (authority = ETD-LCSH)
Topic
Obesity--Nutritional aspects
RelatedItem (type = host)
TitleInfo
Title
Graduate School - New Brunswick Electronic Theses and Dissertations
Identifier (type = local)
rucore19991600001
Identifier (type = hdl)
http://hdl.rutgers.edu/1782.2/rucore10001600001.ETD.17520
Identifier
ETD_1204
Location
PhysicalLocation (authority = marcorg); (displayLabel = Rutgers, The State University of New Jersey)
NjNbRU
Identifier (type = doi)
doi:10.7282/T3V1253C
Genre (authority = ExL-Esploro)
ETD graduate
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The author owns the copyright to this work.
Copyright
Status
Copyright protected
Availability
Status
Open
AssociatedEntity (AUTHORITY = rulib); (ID = 1)
Name
Xiaofang Liang
Role
Copyright holder
Affiliation
Rutgers University. Graduate School - New Brunswick
RightsEvent (AUTHORITY = rulib); (ID = 1)
Type
Permission or license
Detail
Non-exclusive ETD license
AssociatedObject (AUTHORITY = rulib); (ID = 1)
Type
License
Name
Author Agreement License
Detail
I hereby grant to the Rutgers University Libraries and to my school the non-exclusive right to archive, reproduce and distribute my thesis or dissertation, in whole or in part, and/or my abstract, in whole or in part, in and from an electronic format, subject to the release date subsequently stipulated in this submittal form and approved by my school. I represent and stipulate that the thesis or dissertation and its abstract are my original work, that they do not infringe or violate any rights of others, and that I make these grants as the sole owner of the rights to my thesis or dissertation and its abstract. I represent that I have obtained written permissions, when necessary, from the owner(s) of each third party copyrighted matter to be included in my thesis or dissertation and will supply copies of such upon request by my school. I acknowledge that RU ETD and my school will not distribute my thesis or dissertation or its abstract if, in their reasonable judgment, they believe all such rights have not been secured. I acknowledge that I retain ownership rights to the copyright of my work. I also retain the right to use all or part of this thesis or dissertation in future works, such as articles or books.
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