Mapping the micro-proteome of the nuclear lamina and lamina-associated domains.
Animals
Cell Line
Cell Nucleus
/ genetics
Chromatin
/ metabolism
DNA
/ metabolism
DNA-Binding Proteins
/ metabolism
Genome
Heterochromatin
/ metabolism
Humans
Membrane Proteins
/ metabolism
Mice
NIH 3T3 Cells
Nuclear Lamina
/ genetics
Nuclear Proteins
/ genetics
Protein Binding
/ physiology
Protein Domains
/ physiology
Proteome
/ genetics
Proteomics
/ methods
Journal
Life science alliance
ISSN: 2575-1077
Titre abrégé: Life Sci Alliance
Pays: United States
ID NLM: 101728869
Informations de publication
Date de publication:
05 2021
05 2021
Historique:
received:
12
05
2020
revised:
08
02
2021
accepted:
09
02
2021
entrez:
24
3
2021
pubmed:
25
3
2021
medline:
13
10
2021
Statut:
epublish
Résumé
The nuclear lamina is a proteinaceous network of filaments that provide both structural and gene regulatory functions by tethering proteins and large domains of DNA, the so-called lamina-associated domains (LADs), to the periphery of the nucleus. LADs are a large fraction of the mammalian genome that are repressed, in part, by their association to the nuclear periphery. The genesis and maintenance of LADs is poorly understood as are the proteins that participate in these functions. In an effort to identify proteins that reside at the nuclear periphery and potentially interact with LADs, we have taken a two-pronged approach. First, we have undertaken an interactome analysis of the inner nuclear membrane bound LAP2β to further characterize the nuclear lamina proteome. To accomplish this, we have leveraged the BioID system, which previously has been successfully used to characterize the nuclear lamina proteome. Second, we have established a system to identify proteins that bind to LADs by developing a chromatin-directed BioID system. We combined the BioID system with the m6A-tracer system which binds to LADs in live cells to identify both LAD proximal and nuclear lamina proteins. In combining these datasets, we have further characterized the protein network at the nuclear lamina, identified putative LAD proximal proteins and found several proteins that appear to interface with both micro-proteomes. Importantly, several proteins essential for LAD function, including heterochromatin regulating proteins related to H3K9 methylation, were identified in this study.
Identifiants
pubmed: 33758005
pii: 4/5/e202000774
doi: 10.26508/lsa.202000774
pmc: PMC8008952
pii:
doi:
Substances chimiques
Chromatin
0
DNA-Binding Proteins
0
Heterochromatin
0
Membrane Proteins
0
Nuclear Proteins
0
Proteome
0
lamina-associated polypeptide 2
0
DNA
9007-49-2
Banques de données
GENBANK
['GO:0034399', 'GO:0005652', 'GO:0016363']
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM132427
Pays : United States
Organisme : NIA NIH HHS
ID : R21 AG050132
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM007445
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM007814
Pays : United States
Informations de copyright
© 2021 Wong et al.
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