Arpin Regulates Migration Persistence by Interacting with Both Tankyrases and the Arp2/3 Complex.
Arp2/3
Arpin
Tankyrase
cell migration
migration persistence
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
16 Apr 2021
16 Apr 2021
Historique:
received:
17
03
2021
revised:
11
04
2021
accepted:
13
04
2021
entrez:
30
4
2021
pubmed:
1
5
2021
medline:
13
5
2021
Statut:
epublish
Résumé
During cell migration, protrusion of the leading edge is driven by the polymerization of Arp2/3-dependent branched actin networks. Migration persistence is negatively regulated by the Arp2/3 inhibitory protein Arpin. To better understand Arpin regulation in the cell, we looked for its interacting partners and identified both Tankyrase 1 and 2 (TNKS) using a yeast two-hybrid screening and coimmunoprecipitation with full-length Arpin as bait. Arpin interacts with ankyrin repeats of TNKS through a C-terminal-binding site on its acidic tail, which overlaps with the Arp2/3-binding site. Arpin was found to dissolve the liquid-liquid phase separation of TNKS upon overexpression. To uncouple the interactions of Arpin with TNKS and Arp2/3, we introduced point mutations in the Arpin tail and attempted to rescue the increased migration persistence of the Arpin knockout cells using random plasmid integration or compensating knock-ins at the
Identifiants
pubmed: 33923443
pii: ijms22084115
doi: 10.3390/ijms22084115
pmc: PMC8073056
pii:
doi:
Substances chimiques
Carrier Proteins
0
arpin protein, human
0
TNKS2 protein, human
EC 2.4.2.30
Tankyrases
EC 2.4.2.30
TNKS protein, human
EC 2.4.4.30
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Agence Nationale de la Recherche
ID : ANR-15-CE13-0016-01
Organisme : Institut National Du Cancer
ID : INCA_6521
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