Activation of Arp2/3 complex-dependent actin polymerization by plant proteins distantly related to Scar/WAVE
Autor: | Rong Li, Mary J. Frank, Laurie G. Smith, Julia Dyachok, Coumaran Egile, Stevan Djakovic, Michelle Nolasco |
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Rok vydání: | 2004 |
Předmět: |
DNA
Plant Recombinant Fusion Proteins Molecular Sequence Data Arabidopsis Arp2/3 complex macromolecular substances Genes Plant Zea mays Actin-Related Protein 2-3 Complex Homology (biology) Animals Amino Acid Sequence Actin Plant Proteins Genetics Multidisciplinary Base Sequence Sequence Homology Amino Acid biology Arabidopsis Proteins Cell morphogenesis BRICK1 Microfilament Proteins Biological Sciences Cofilin biology.organism_classification Actins Wiskott-Aldrich Syndrome Protein Family Cell biology Actin-Related Protein 3 Multiprotein Complexes Actin-Related Protein 2 HSPC300 biology.protein WAVE complex |
Zdroj: | Frank, M; Egile, C; Dyachok, J; Djakovic, S; Nolasco, M; Li, R; et al.(2004). Activation of Arp2/3 complex-dependent actin polymerization by plant proteins distantly related to Scar/WAVE. Proceedings of the National Academy of Sciences of the United States of America, 101(46), 16379-16384. UC San Diego: Retrieved from: http://www.escholarship.org/uc/item/8h27r1bk |
ISSN: | 1091-6490 0027-8424 |
Popis: | The Arp2/3 complex, a highly conserved nucleator of F-actin polymerization, plays a key role in the regulation of actin dynamics eukaryotic cells. In animal cells and yeasts, Wiskott-Aldrich Syndrome protein (WASP)/suppressor of cAMP receptor (Scar)/WASP family verprolin homologous (WAVE) family proteins activate the Arp2/3 complex in response to localized cues. Like other eukaryotes, plants have an Arp2/3 complex, which has recently been shown to play an important role in F-actin organization and cell morphogenesis. However, no activators of the Arp2/3 complex have been identified in plants, which lack obvious homologs of WASP/Scar/WAVE family proteins. Here, we identify a family of Scar/WAVE-related plant Arp2/3 activators. Like Scar/WAVE proteins, four proteins identified in Arabidopsis thaliana (AtSCAR1 to AtSCAR4) and one in maize (ZmSCAR1) have a C-terminal WASP homology 2 (WH2)/acidic (WA)-verprolin homology/cofilin homology/acidic (VCA)-like domain, which we show can activate the bovine Arp2/3 complex. At their N termini, AtSCAR1 to ATSCAR4, along with a fifth protein lacking a VCA/WA-like domain at its C terminus (At4g18600), are related to the N-terminal Scar homology domains of Scar/WAVE family proteins. Analysis of gene expression patterns suggests functional redundancy among members of the AtSCAR family. Full-length AtSCAR1 and ATSCAR3 proteins and their Scar homology domains bind in vitro to AtBRICK 1 (AtBRK1), the Arabidopsis homolog of HSPC300, a WAVE-binding protein recently identified as a component of a complex implicated in the regulation of Scar/WAVE activity. Thus, AtSCAR proteins are likely to function in association with AtBRK1, and perhaps other Arabidopsis homologs of WAVE complex components, to regulate activation of the Arp2,3 complex in vivo . |
Databáze: | OpenAIRE |
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