| Autor: |
Madania, Ammar, Dumoulin, Pascal, Grava, Sandrine, Kitamoto, Hiroko, Scha¨rer-Brodbeck, Claudia, Soulard, Alexandre, Moreau, Violaine, Winsor, Barbara |
| Zdroj: |
Molecular Biology of the Cell; October 1999, Vol. 10 Issue: 10 p3521-3538, 18p |
| Abstrakt: |
Yeast Las17 protein is homologous to the Wiskott–Aldrich Syndrome protein, which is implicated in severe immunodeficiency. Las17p/Bee1p has been shown to be important for actin patch assembly and actin polymerization. Here we show that Las17p interacts with the Arp2/3 complex. LAS17is an allele-specific multicopy suppressor of ARP2and ARP3mutations; overexpression restores both actin patch organization and endocytosis defects in ARP2temperature-sensitive (ts) cells. Six of seven ARP2ts mutants and at least oneARP3ts mutant are synthetically lethal withlas17?ts confirming functional interaction with the Arp2/3 complex. Further characterization of las17?cells showed that receptor-mediated internalization of a factor by the Ste2 receptor is severely defective. The polarity of normal bipolar bud site selection is lost. Las17-gfp remains localized in cortical patches in vivo independently of polymerized actin and is required for the polarized localization of Arp2/3 as well as actin. Coimmunoprecipitation of Arp2p with Las17p indicates that Las17p interacts directly with the complex. Two hybrid results also suggest that Las17p interacts with actin, verprolin, Rvs167p and several other proteins including Src homology 3 (SH3) domain proteins, suggesting that Las17p may integrate signals from different regulatory cascades destined for the Arp2/3p complex and the actin cytoskeleton. |
| Databáze: |
Supplemental Index |
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