The WAVE complex associates with sites of saddle membrane curvature.
Actin Cytoskeleton
/ genetics
Actin-Related Protein 2-3 Complex
/ genetics
Animals
Cell Membrane
/ genetics
Cell Movement
Cell Shape
HEK293 Cells
HL-60 Cells
Human Umbilical Vein Endothelial Cells
/ metabolism
Humans
Macrophages
/ metabolism
Melanoma, Experimental
/ genetics
Mice
Microscopy, Confocal
Microscopy, Electron, Transmission
Microscopy, Fluorescence
Nerve Tissue Proteins
/ genetics
Protein Transport
Pseudopodia
/ genetics
Signal Transduction
Time Factors
Wiskott-Aldrich Syndrome Protein Family
/ genetics
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:
02 08 2021
02 08 2021
Historique:
received:
06
04
2020
revised:
13
04
2021
accepted:
18
05
2021
entrez:
7
6
2021
pubmed:
8
6
2021
medline:
21
10
2021
Statut:
ppublish
Résumé
How local interactions of actin regulators yield large-scale organization of cell shape and movement is not well understood. Here we investigate how the WAVE complex organizes sheet-like lamellipodia. Using super-resolution microscopy, we find that the WAVE complex forms actin-independent 230-nm-wide rings that localize to regions of saddle membrane curvature. This pattern of enrichment could explain several emergent cell behaviors, such as expanding and self-straightening lamellipodia and the ability of endothelial cells to recognize and seal transcellular holes. The WAVE complex recruits IRSp53 to sites of saddle curvature but does not depend on IRSp53 for its own localization. Although the WAVE complex stimulates actin nucleation via the Arp2/3 complex, sheet-like protrusions are still observed in ARP2-null, but not WAVE complex-null, cells. Therefore, the WAVE complex has additional roles in cell morphogenesis beyond Arp2/3 complex activation. Our work defines organizing principles of the WAVE complex lamellipodial template and suggests how feedback between cell shape and actin regulators instructs cell morphogenesis.
Identifiants
pubmed: 34096975
pii: 212260
doi: 10.1083/jcb.202003086
pmc: PMC8185649
pii:
doi:
Substances chimiques
Actin-Related Protein 2-3 Complex
0
BAIAP2 protein, human
0
Baiap2 protein, mouse
0
Nerve Tissue Proteins
0
Wiskott-Aldrich Syndrome Protein Family
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Video-Audio Media
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : NIGMS NIH HHS
ID : T32 GM007810
Pays : United States
Organisme : NIAID NIH HHS
ID : R01 AI052116
Pays : United States
Organisme : NIBIB NIH HHS
ID : T32 EB009383
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM118167
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM008284
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM067547
Pays : United States
Informations de copyright
© 2021 Pipathsouk et al.
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