| RRC ID |
605
|
| 著者 |
Michelot A, Guérin C, Huang S, Ingouff M, Richard S, Rodiuc N, Staiger CJ, Blanchoin L.
|
| タイトル |
The formin homology 1 domain modulates the actin nucleation and bundling activity of Arabidopsis FORMIN1.
|
| ジャーナル |
Plant Cell
|
| Abstract |
The organization of actin filaments into large ordered structures is a tightly controlled feature of many cellular processes. However, the mechanisms by which actin filament polymerization is initiated from the available pool of profilin-bound actin monomers remain unknown in plants. Because the spontaneous polymerization of actin monomers bound to profilin is inhibited, the intervention of an actin promoting factor is required for efficient actin polymerization. Two such factors have been characterized from yeasts and metazoans: the Arp2/3 complex, a complex of seven highly conserved subunits including two actin-related proteins (ARP2 and ARP3), and the FORMIN family of proteins. The recent finding that Arabidopsis thaliana plants lacking a functional Arp2/3 complex exhibit rather modest morphological defects leads us to consider whether the large FORMIN family plays a central role in the regulation of actin polymerization. Here, we have characterized the mechanism of action of Arabidopsis FORMIN1 (AFH1). Overexpression of AFH1 in pollen tubes has been shown previously to induce abnormal actin cable formation. We demonstrate that AFH1 has a unique behavior when compared with nonplant formins. The activity of the formin homology domain 2 (FH2), containing the actin binding activity, is modulated by the formin homology domain 1 (FH1). Indeed, the presence of the FH1 domain switches the FH2 domain from a tight capper (Kd approximately 3.7 nM) able to nucleate actin filaments that grow only in the pointed-end direction to a leaky capper that allows barbed-end elongation and efficient nucleation of actin filaments from actin monomers bound to profilin. Another exciting feature of AFH1 is its ability to bind to the side and bundle actin filaments. We have identified an actin nucleator that is able to organize actin filaments directly into unbranched actin filament bundles. We suggest that AFH1 plays a central role in the initiation and organization of actin cables from the pool of actin monomers bound to profilin.
|
| 巻・号 |
17(8)
|
| ページ |
2296-313
|
| 公開日 |
2005-8-1
|
| DOI |
10.1105/tpc.105.030908
|
| PII |
tpc.105.030908
|
| PMID |
15994911
|
| PMC |
PMC1182490
|
| MeSH |
Actins / metabolism*
Amino Acid Sequence
Arabidopsis Proteins / chemistry
Arabidopsis Proteins / metabolism*
Base Sequence
Formins
Kinetics
Membrane Proteins / chemistry
Membrane Proteins / metabolism*
Molecular Sequence Data
Sequence Alignment
Sequence Homology, Amino Acid
|
| IF |
9.618
|
| 引用数 |
131
|
|
WOS 分野
|
PLANT SCIENCES
BIOCHEMISTRY & MOLECULAR BIOLOGY
CELL BIOLOGY
|
| リソース情報 |
| シロイヌナズナ / 植物培養細胞・遺伝子 |
pda07914 |
