Lysine acetylation of cytoskeletal proteins: Emergence of an actin code.
Journal
The Journal of cell biology
ISSN: 1540-8140
Titre abrégé: J Cell Biol
Pays: United States
ID NLM: 0375356
Informations de publication
Date de publication:
07 12 2020
07 12 2020
Historique:
received:
26
06
2020
revised:
26
08
2020
accepted:
02
09
2020
entrez:
12
10
2020
pubmed:
13
10
2020
medline:
31
3
2021
Statut:
ppublish
Résumé
Reversible lysine acetylation of nuclear proteins such as histones is a long-established important regulatory mechanism for chromatin remodeling and transcription. In the cytoplasm, acetylation of a number of cytoskeletal proteins, including tubulin, cortactin, and the formin mDia2, regulates both cytoskeletal assembly and stability. More recently, acetylation of actin itself was revealed to regulate cytoplasmic actin polymerization through the formin INF2, with downstream effects on ER-to-mitochondrial calcium transfer, mitochondrial fission, and vesicle transport. This finding raises the possibility that actin acetylation, along with other post-translational modifications to actin, might constitute an "actin code," similar to the "histone code" or "tubulin code," controlling functional shifts to these central cellular proteins. Given the multiple roles of actin in nuclear functions, its modifications might also have important roles in gene expression.
Identifiants
pubmed: 33044556
pii: 211455
doi: 10.1083/jcb.202006151
pmc: PMC7555357
pii:
doi:
Substances chimiques
Cytoskeletal Proteins
0
Lysine
K3Z4F929H6
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Review
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : NIGMS NIH HHS
ID : P20 GM113132
Pays : United States
Organisme : NIDDK NIH HHS
ID : R01 DK088826
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM122545
Pays : United States
Organisme : NIDDK NIH HHS
ID : T32 DK007199
Pays : United States
Informations de copyright
© 2020 A et al.
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