Interactions among subunits of human Arp2/3 complex: p20-Arc as the hub

Xiangshan Zhao; Zhenye Yang; Min Qian; Xueliang Zhu

doi:10.1006/bbrc.2000.4151

Interactions among subunits of human Arp2/3 complex: p20-Arc as the hub

Xiangshan Zhao, Zhenye Yang, Min Qian, Xueliang Zhu

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

16 Scopus citations

Abstract

The Arp2/3 complex is critical for nucleation and crosslinking of actin filaments. To gain insight into its subunit topology and assembly pathway, we systematically examined interactions among subunits of human Arp2/3 complex by yeast two-hybrid assays. It was shown that p20-Arc was able to interact with p21-Arc, p34-Arc, and p16-Arc, respectively. In contrast, p41-Arc only interacted with p20-Arc/p16-Arc heterodimer. In addition, we found that structural integrity was important for association between p20-Arc and p21-Arc, while the N-terminal half of p34-Arc was dispensable for its binding to p20-Arc. Our data suggest a key role of p20-Arc and a multistep pathway for the complex formation.

Original language	English (US)
Pages (from-to)	513-517
Number of pages	5
Journal	Biochemical and Biophysical Research Communications
Volume	280
Issue number	2
DOIs	https://doi.org/10.1006/bbrc.2000.4151
State	Published - 2001
Externally published	Yes

Keywords

Actin
Arp2/3 complex
Subunit
Yeast twohybrid assay

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1006/bbrc.2000.4151

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title = "Interactions among subunits of human Arp2/3 complex: p20-Arc as the hub",

abstract = "The Arp2/3 complex is critical for nucleation and crosslinking of actin filaments. To gain insight into its subunit topology and assembly pathway, we systematically examined interactions among subunits of human Arp2/3 complex by yeast two-hybrid assays. It was shown that p20-Arc was able to interact with p21-Arc, p34-Arc, and p16-Arc, respectively. In contrast, p41-Arc only interacted with p20-Arc/p16-Arc heterodimer. In addition, we found that structural integrity was important for association between p20-Arc and p21-Arc, while the N-terminal half of p34-Arc was dispensable for its binding to p20-Arc. Our data suggest a key role of p20-Arc and a multistep pathway for the complex formation.",

keywords = "Actin, Arp2/3 complex, Subunit, Yeast twohybrid assay",

author = "Xiangshan Zhao and Zhenye Yang and Min Qian and Xueliang Zhu",

note = "Funding Information: We thank Xiumin Yan and Qiongping Huang for technical assistance, and Dr. Gengxi Hu at Shanghai Institute of Biochemistry and Cell Biology for providing the p20-Arc cDNA. This work was supported by Grants KJ951-B1-608 and KJ95T-06 from the Chinese Academy of Sciences, and Grant 39870185 from the Natural Science Foundation of China.",

year = "2001",

doi = "10.1006/bbrc.2000.4151",

language = "English (US)",

volume = "280",

pages = "513--517",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Elsevier B.V.",

number = "2",

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TY - JOUR

T1 - Interactions among subunits of human Arp2/3 complex

T2 - p20-Arc as the hub

AU - Zhao, Xiangshan

AU - Yang, Zhenye

AU - Qian, Min

AU - Zhu, Xueliang

N1 - Funding Information: We thank Xiumin Yan and Qiongping Huang for technical assistance, and Dr. Gengxi Hu at Shanghai Institute of Biochemistry and Cell Biology for providing the p20-Arc cDNA. This work was supported by Grants KJ951-B1-608 and KJ95T-06 from the Chinese Academy of Sciences, and Grant 39870185 from the Natural Science Foundation of China.

PY - 2001

Y1 - 2001

N2 - The Arp2/3 complex is critical for nucleation and crosslinking of actin filaments. To gain insight into its subunit topology and assembly pathway, we systematically examined interactions among subunits of human Arp2/3 complex by yeast two-hybrid assays. It was shown that p20-Arc was able to interact with p21-Arc, p34-Arc, and p16-Arc, respectively. In contrast, p41-Arc only interacted with p20-Arc/p16-Arc heterodimer. In addition, we found that structural integrity was important for association between p20-Arc and p21-Arc, while the N-terminal half of p34-Arc was dispensable for its binding to p20-Arc. Our data suggest a key role of p20-Arc and a multistep pathway for the complex formation.

AB - The Arp2/3 complex is critical for nucleation and crosslinking of actin filaments. To gain insight into its subunit topology and assembly pathway, we systematically examined interactions among subunits of human Arp2/3 complex by yeast two-hybrid assays. It was shown that p20-Arc was able to interact with p21-Arc, p34-Arc, and p16-Arc, respectively. In contrast, p41-Arc only interacted with p20-Arc/p16-Arc heterodimer. In addition, we found that structural integrity was important for association between p20-Arc and p21-Arc, while the N-terminal half of p34-Arc was dispensable for its binding to p20-Arc. Our data suggest a key role of p20-Arc and a multistep pathway for the complex formation.

KW - Actin

KW - Arp2/3 complex

KW - Subunit

KW - Yeast twohybrid assay

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AN - SCOPUS:0034816314

SN - 0006-291X

VL - 280

SP - 513

EP - 517

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 2

ER -

Interactions among subunits of human Arp2/3 complex: p20-Arc as the hub

Abstract

Keywords

ASJC Scopus subject areas

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