Home
Resource
Oligomerization of nicotinic acetylcholine receptors in membranes with DHA-enriched domains
PDF
PDF format is widely accepted and good for printing.
Plug-in required
PDF-1(2.13 MB)
Citation & Export
View Usage Statistics
Staff View

Citation & Export
Hide

Simple citation

Woods, Kristen N.. Oligomerization of nicotinic acetylcholine receptors in membranes with DHA-enriched domains. Retrieved from https://doi.org/doi:10.7282/T3G1646D

Export

Click here for information about Citation Management Tools at Rutgers.

Statistics
Hide

Description

TitleOligomerization of nicotinic acetylcholine receptors in membranes with DHA-enriched domains
NameWoods, Kristen N. (author); Brannigan, Jessica Grace (chair); Klein, Eric (internal member); Martin, Joseph (internal member); Rutgers University; Camden Graduate School
Date Created2018
Other Date2018-05 (degree)
SubjectComputational and Integrative Biology, Unsaturated fatty acids
Extent1 online resource (v, 33 p. : ill.)
DescriptionThe nicotinic acetylcholine receptor (nAChR) is an excitatory neurotransmitter receptor that mediates muscle functioning by forming nAChR-associated, lattice networks. At the neuromuscular junction (NMJ), synaptic and intracellular proteins, notably Agrin, MusK, and rapsyn, ultimately stabilize these highly dense networks. Interestingly, experimental evidence suggests that cholesterol-rich domains, known as lipid rafts, facilitate signaling among Agrin-Musk and rapsyn, and their presence is essential for healthy nAChR clustering. In spite of their importance, the structural and functional mechanisms of lipid domains are currently unknown. Alongside cholesterol, Docosahexaenoic acid omega-3 fatty acids (DHA-PUFAs) are prevalent at the NMJ, correlate with domain formation, and strongly promote neuronal health. In the present study, we computationally explored the role of DHA-PUFAs on nAChR clustering in the presence and absence of lipid domains. Within coarse-grained (CG) model membranes, nAChRs consistently partitioned into flexible, liquid-disordered domains; boundary lipids were rich in DHA-PUFAs regardless of the number of nAChR molecules, but preventing domain formation also reduced the likelihood of these acyl chains aggregating around nAChR. Taken together, our findings suggest that by inducing domain formation in membranes, DHA plays a critical role in the early stages of nAChR oligomerization.
NoteM.S.
NoteIncludes bibliographical references
Noteby Kristen N. Woods
Genretheses, ETD graduate
Persistent URLhttps://doi.org/doi:10.7282/T3G1646D
Languageeng
CollectionCamden Graduate School Electronic Theses and Dissertations
Organization NameRutgers, The State University of New Jersey
RightsThe author owns the copyright to this work.
Version 8.5.5
Rutgers University Libraries - Copyright ©2024