期刊
CURRENT BIOLOGY
卷 18, 期 3, 页码 203-210出版社
CELL PRESS
DOI: 10.1016/j.cub.2008.01.026
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资金
- Medical Research Council [G0600249] Funding Source: researchfish
- MRC [G0600249] Funding Source: UKRI
- Medical Research Council [G0600249] Funding Source: Medline
Actin polymerization drives multiple cell processes involving movement and shape change. SCAR/WAVE proteins connect signaling to actin polymerization through the activation of the Arp2/3 complex. SCAR/WAVE is normally found in a complex with four other proteins: PIR121, Nap1, Abi2, and HSPC300 (Figure S1A available online) [1-3]. However, there is no consensus as to whether the complex functions as an unchanging unit or if it alters its composition in response to stimulation, as originally proposed by Eden et al. [1]. It also is unclear whether complex members exclusively regulate SCAR/WAVEs or if they have additional targets [4-6]. Here, we analyze the roles of the unique Dictyostelium Abi. We find that abiA null mutants show less severe defects in motility than do scar null cells, indicating-unexpectedly-that SCAR retains partial activity in the absence of Abi. Furthermore, abiA null mutants have a serious defect in cytokinesis, which is not seen in other SCAR complex mutants and is seen only when SCAR itself is present. Detailed examination reveals that normal cytokinesis requires SCAR activity, apparently regulated through multiple pathways.
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