F-actin binding region of SPIN90 C-terminus is essential for actin polymerization and lamellipodia formation

Dae Joong Kim; Sung Hyun Kim; Seon Myung Kim; Jeom Il Bae; Joohong Ahnn; Woo Keun Song

doi:10.1080/15419060701225010

F-actin binding region of SPIN90 C-terminus is essential for actin polymerization and lamellipodia formation

Dae Joong Kim
, Sung Hyun Kim
, Seon Myung Kim
, Jeom Il Bae
, Joohong Ahnn
, Woo Keun Song

Research output: Contribution to journal › Article › peer-review

9 Citations (Scopus)

Abstract

We recently reported that SPIN90 is able to bind with several proteins involved in regulating actin cytoskeleton networks, including dynamin, WASP, βPIX, and Nck. Based on these findings, we investigated how SPIN90 regulates the actin cytoskeleton and promotes actin assembly. This study demonstrated that aluminium fluoride-induced localization of SPIN90 to lamellipodia requires amino acids 582-722 at the SPIN90 C-terminus, which is also essential for F-actin binding and Arp2/3 complex mediated polymerization of actin into branched actin filaments. Furthermore, after deletion of the F-actin binding region (582-722 SPIN90) failed to localize at the membrane edge and was unable to promote lamellipodia formation, suggesting that the F-actin binding region in the SPIN90 C-terminus is essential for the formation of branched actin networks and regulation of the actin cytoskeleton at the leading edge of cells.

Original language	English
Pages (from-to)	33-43
Number of pages	11
Journal	Cell Communication and Adhesion
Volume	14
Issue number	1
DOIs	https://doi.org/10.1080/15419060701225010
Publication status	Published - Jan 2007

Bibliographical note

Funding Information:
This study was supported in part by grants from the National Research Laboratory and Molecular & Cellular BioDiscovery Research Group (The Ministry of Science & Technology).

Keywords

Actin filament branching
Actin polymerization
Arp2/3 complex
F-actin
Lamellipodia
SPIN90

Access to Document

10.1080/15419060701225010

Cite this

@article{dde405307be34f37ac0ec9fa2810c9ae,

title = "F-actin binding region of SPIN90 C-terminus is essential for actin polymerization and lamellipodia formation",

abstract = "We recently reported that SPIN90 is able to bind with several proteins involved in regulating actin cytoskeleton networks, including dynamin, WASP, βPIX, and Nck. Based on these findings, we investigated how SPIN90 regulates the actin cytoskeleton and promotes actin assembly. This study demonstrated that aluminium fluoride-induced localization of SPIN90 to lamellipodia requires amino acids 582-722 at the SPIN90 C-terminus, which is also essential for F-actin binding and Arp2/3 complex mediated polymerization of actin into branched actin filaments. Furthermore, after deletion of the F-actin binding region (582-722 SPIN90) failed to localize at the membrane edge and was unable to promote lamellipodia formation, suggesting that the F-actin binding region in the SPIN90 C-terminus is essential for the formation of branched actin networks and regulation of the actin cytoskeleton at the leading edge of cells.",

keywords = "Actin filament branching, Actin polymerization, Arp2/3 complex, F-actin, Lamellipodia, SPIN90",

author = "Kim, \{Dae Joong\} and Kim, \{Sung Hyun\} and Kim, \{Seon Myung\} and Bae, \{Jeom Il\} and Joohong Ahnn and Song, \{Woo Keun\}",

note = "Funding Information: This study was supported in part by grants from the National Research Laboratory and Molecular \& Cellular BioDiscovery Research Group (The Ministry of Science \& Technology).",

year = "2007",

month = jan,

doi = "10.1080/15419060701225010",

language = "English",

volume = "14",

pages = "33--43",

journal = "Cell Communication and Adhesion",

issn = "1541-9061",

publisher = "Taylor and Francis Ltd.",

number = "1",

}

TY - JOUR

T1 - F-actin binding region of SPIN90 C-terminus is essential for actin polymerization and lamellipodia formation

AU - Kim, Dae Joong

AU - Kim, Sung Hyun

AU - Kim, Seon Myung

AU - Bae, Jeom Il

AU - Ahnn, Joohong

AU - Song, Woo Keun

N1 - Funding Information: This study was supported in part by grants from the National Research Laboratory and Molecular & Cellular BioDiscovery Research Group (The Ministry of Science & Technology).

PY - 2007/1

Y1 - 2007/1

N2 - We recently reported that SPIN90 is able to bind with several proteins involved in regulating actin cytoskeleton networks, including dynamin, WASP, βPIX, and Nck. Based on these findings, we investigated how SPIN90 regulates the actin cytoskeleton and promotes actin assembly. This study demonstrated that aluminium fluoride-induced localization of SPIN90 to lamellipodia requires amino acids 582-722 at the SPIN90 C-terminus, which is also essential for F-actin binding and Arp2/3 complex mediated polymerization of actin into branched actin filaments. Furthermore, after deletion of the F-actin binding region (582-722 SPIN90) failed to localize at the membrane edge and was unable to promote lamellipodia formation, suggesting that the F-actin binding region in the SPIN90 C-terminus is essential for the formation of branched actin networks and regulation of the actin cytoskeleton at the leading edge of cells.

AB - We recently reported that SPIN90 is able to bind with several proteins involved in regulating actin cytoskeleton networks, including dynamin, WASP, βPIX, and Nck. Based on these findings, we investigated how SPIN90 regulates the actin cytoskeleton and promotes actin assembly. This study demonstrated that aluminium fluoride-induced localization of SPIN90 to lamellipodia requires amino acids 582-722 at the SPIN90 C-terminus, which is also essential for F-actin binding and Arp2/3 complex mediated polymerization of actin into branched actin filaments. Furthermore, after deletion of the F-actin binding region (582-722 SPIN90) failed to localize at the membrane edge and was unable to promote lamellipodia formation, suggesting that the F-actin binding region in the SPIN90 C-terminus is essential for the formation of branched actin networks and regulation of the actin cytoskeleton at the leading edge of cells.

KW - Actin filament branching

KW - Actin polymerization

KW - Arp2/3 complex

KW - F-actin

KW - Lamellipodia

KW - SPIN90

UR - https://www.scopus.com/pages/publications/34247584045

U2 - 10.1080/15419060701225010

DO - 10.1080/15419060701225010

M3 - Article

C2 - 17453829

AN - SCOPUS:34247584045

SN - 1541-9061

VL - 14

SP - 33

EP - 43

JO - Cell Communication and Adhesion

JF - Cell Communication and Adhesion

IS - 1

ER -

F-actin binding region of SPIN90 C-terminus is essential for actin polymerization and lamellipodia formation

Abstract

Bibliographical note

Keywords

Access to Document

Other files and links

Fingerprint

Cite this