TY - JOUR
T1 - Palmitoylated Proteins in Dendritic Spine Remodeling
AU - Albanesi, Joseph P.
AU - Barylko, Barbara
AU - DeMartino, George N.
AU - Jameson, David M.
N1 - Funding Information:
Funding. This work was supported in part by National Institutes of Health (NIH) grant R21MH119516 (JA and DJ).
Publisher Copyright:
© Copyright © 2020 Albanesi, Barylko, DeMartino and Jameson.
PY - 2020/6/16
Y1 - 2020/6/16
N2 - Activity-responsive changes in the actin cytoskeleton are required for the biogenesis, motility, and remodeling of dendritic spines. These changes are governed by proteins that regulate the polymerization, depolymerization, bundling, and branching of actin filaments. Thus, processes that have been extensively characterized in the context of non-neuronal cell shape change and migration are also critical for learning and memory. In this review article, we highlight actin regulatory proteins that associate, at least transiently, with the dendritic plasma membrane. All of these proteins have been shown, either in directed studies or in high—throughput screens, to undergo palmitoylation, a potentially reversible, and stimulus-dependent cysteine modification. Palmitoylation increases the affinity of peripheral proteins for the membrane bilayer and contributes to their subcellular localization and recruitment to cholesterol-rich membrane microdomains.
AB - Activity-responsive changes in the actin cytoskeleton are required for the biogenesis, motility, and remodeling of dendritic spines. These changes are governed by proteins that regulate the polymerization, depolymerization, bundling, and branching of actin filaments. Thus, processes that have been extensively characterized in the context of non-neuronal cell shape change and migration are also critical for learning and memory. In this review article, we highlight actin regulatory proteins that associate, at least transiently, with the dendritic plasma membrane. All of these proteins have been shown, either in directed studies or in high—throughput screens, to undergo palmitoylation, a potentially reversible, and stimulus-dependent cysteine modification. Palmitoylation increases the affinity of peripheral proteins for the membrane bilayer and contributes to their subcellular localization and recruitment to cholesterol-rich membrane microdomains.
KW - actin assembly
KW - cytoskeletal remodeling
KW - dendritic spines
KW - palmitoylation
KW - synaptic plasticity
UR - http://www.scopus.com/inward/record.url?scp=85087316232&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85087316232&partnerID=8YFLogxK
U2 - 10.3389/fnsyn.2020.00022
DO - 10.3389/fnsyn.2020.00022
M3 - Review article
C2 - 32655390
AN - SCOPUS:85087316232
SN - 1663-3563
VL - 12
JO - Frontiers in Synaptic Neuroscience
JF - Frontiers in Synaptic Neuroscience
M1 - 22
ER -