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Vol. 10, Issue 10, 3521-3538, October 1999
and
*Mécanismes Moléculaires de la Division Cellulaire et
du Développement, Unité Propre de Recherche 9005 du
Centre National de la Recherche Scientifique, Institut de Biologie
Moléculaire et Cellulaire, F-67084 Strasbourg, France; and
§Biozentrum, University of Basel, CH-4056 Basel,
Switzerland
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. LAS17 is an allele-specific multicopy
suppressor of ARP2 and ARP3 mutations;
overexpression restores both actin patch organization and endocytosis
defects in ARP2 temperature-sensitive (ts) cells. Six of
seven ARP2 ts mutants and at least one
ARP3 ts mutant are synthetically lethal with
las17
ts confirming functional interaction with the
Arp2/3 complex. Further characterization of las17
cells showed that receptor-mediated internalization of 
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.
Present Addresses: Atomic Energy Commission,
Department of Molecular Biology, P.O. Box 6091, Damascus, Syria;
Laboratory of Microorganism Genetic Diversity, National
Institute of Agrobiological Resources, 2-1-2, Kan-nondai, Tsuba, Japan;
and European Molecular Biology Laboratory, 1 Meyerhofstrasse, 69117 Heidelberg, Germany.
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