Cooperation between tropomyosin and α-actinin inhibits fimbrin association with actin filament networks in fission yeast.
Actin Cytoskeleton
/ metabolism
Actin Depolymerizing Factors
/ genetics
Actinin
/ genetics
Actins
/ genetics
Cell Cycle Proteins
/ genetics
Green Fluorescent Proteins
/ genetics
Membrane Glycoproteins
/ genetics
Microfilament Proteins
/ genetics
Microscopy, Fluorescence
/ methods
Protein Binding
Schizosaccharomyces
/ genetics
Schizosaccharomyces pombe Proteins
/ genetics
Time-Lapse Imaging
/ methods
Tropomyosin
/ genetics
Ain1
Cdc8
S. pombe
actin patch
cell biology
contractile ring
cytokinesis
endocytosis
Journal
eLife
ISSN: 2050-084X
Titre abrégé: Elife
Pays: England
ID NLM: 101579614
Informations de publication
Date de publication:
10 06 2019
10 06 2019
Historique:
received:
30
03
2019
accepted:
29
05
2019
entrez:
11
6
2019
pubmed:
11
6
2019
medline:
3
3
2020
Statut:
epublish
Résumé
We previously discovered that competition between fission yeast actin binding proteins (ABPs) for binding F-actin facilitates their sorting to different cellular networks. Specifically, competition between endocytic actin patch ABPs fimbrin Fim1 and cofilin Adf1 enhances their activities, and prevents tropomyosin Cdc8's association with actin patches. However, these interactions do not explain how Fim1 is prevented from associating strongly with other F-actin networks such as the contractile ring. Here, we identified α-actinin Ain1, a contractile ring ABP, as another Fim1 competitor. Fim1 competes with Ain1 for association with F-actin, which is dependent upon their F-actin residence time. While Fim1 outcompetes both Ain1 and Cdc8 individually, Cdc8 enhances the F-actin bundling activity of Ain1, allowing Ain1 to generate F-actin bundles that Cdc8 can bind in the presence of Fim1. Therefore, the combination of contractile ring ABPs Ain1 and Cdc8 is capable of inhibiting Fim1's association with F-actin networks.
Identifiants
pubmed: 31180322
doi: 10.7554/eLife.47279
pii: 47279
pmc: PMC6557641
doi:
pii:
Substances chimiques
Actin Depolymerizing Factors
0
Actins
0
Adf1 protein, S pombe
0
Cdc8 protein, S pombe
0
Cell Cycle Proteins
0
Membrane Glycoproteins
0
Microfilament Proteins
0
Schizosaccharomyces pombe Proteins
0
Tropomyosin
0
plastin
0
Actinin
11003-00-2
Green Fluorescent Proteins
147336-22-9
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : American Cancer Society
ID : RSG-11-126-01-CSM
Pays : International
Organisme : NIH HHS
ID : T32 GM0071832
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM079265
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM071832
Pays : United States
Organisme : NIGMS NIH HHS
ID : R25 GM109439
Pays : United States
Organisme : National Science Foundation
ID : Graduate Research Fellowship DGE-1746045
Pays : International
Organisme : NIH HHS
ID : R01 GM079265
Pays : United States
Organisme : NIH HHS
ID : IMSD R25GM109439
Pays : United States
Organisme : National Science Foundation
ID : Graduate Research Fellowship DGE-1144082
Pays : International
Informations de copyright
© 2019, Christensen et al.
Déclaration de conflit d'intérêts
JC, KH, AM, RB, CS, AH, MO, DK No competing interests declared
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