Disease relevance of LAS17

• In Saccharomyces cerevisiae, the WASP (Wiskott-Aldrich syndrome protein) homologue Las17p (also called Bee1p) is an important component of cortical actin patches [1].

High impact information on LAS17

• Catalytically inactive Lsb6 interacted with Las17 and promoted endosome motility [2].
• We showed previously that the yeast orthologue of the Wiskott-Aldrich Syndrome protein, Bee1/Las17p, and the type I myosins are key regulators of cortical actin polymerization [3].
• Its interactions with Las17p, Vrp1p, and the type I myosins are essential for this process [1].
• Here, we report the characterization of Lsb7/Bzz1p (for Las seventeen binding protein 7), an Src homology 3 (SH3) domain protein that interacts directly with Las17p via a polyproline-SH3 interaction [1].
• The exocytic SNARE Snc1p, which is recycled by an endocytic route, was also intracellularly accumulated, and inhibition of endocytic internalization suppressed the cytoplasmic accumulation of both Las17p and Snc1p [4].

Biological context of LAS17

• The actin patch assembly mutants las17 delta, sla1delta and vrp1 delta showed elevated levels of cell wall beta-1,6-glucan, and mutant cells were capable of only a limited number of cell divisions compared to wild-type [5].
• Interestingly, five ORFs were preys of both Rvs161p and Rvs167p (RVS167, LAS17, YNL094w, YMR192w and YPL249c) [6].
• Moreover, a high cell survival rate was attained with overexpression of LAS17, when cells in the stationary phase of the growth cycle were subjected to heat killing (48 degrees C) or ethanol killing (20% v/v) [7].
• Sake yeast strain UT-1 grows at a faster rate as a result of the overexpression of LAS17 than control cultures under various stresses such as high temperature, high ethanol concentration, and oxidative stress, and the tolerance to these stresses was increased compared with the control [7].
• The effects of the overexpression of LAS17/BEE1, which encodes a yeast protein exhibiting sequence homology to the Wiscott-Aldrich syndrome protein, on the cell growth of Saccharomyces cerevisiae were examined [7].

Associations of LAS17 with chemical compounds

• In addition, the rate of induction of rho- was markedly reduced by overexpression of LAS17 when serine, tyrosine, and aspartic acid were used as N sources and the yeast was cultured at 35 degrees C, while rho- strains in control cultures were induced at a high frequency [7].
• Lsb6 therefore is a novel regulator of Las17 that mediates endosome motility independent of phosphatidylinositol 4-phosphate synthesis [2].

Regulatory relationships of LAS17

• The addition of Las17p WA further enhances yeast actin polymerization by yArp2/3 and allows the complex to now assist muscle actin polymerization [8].

Other interactions of LAS17

• It colocalizes with cortical actin patches and with Las17p [1].
• In the present study, we have further defined its interaction site with both Sla1p and with Las17p, two regulators of actin dynamics [9].
• Las17 was a much stronger activator of Arp2/3 complex than its carboxyl-terminal (WA) fragment [10].

Analytical, diagnostic and therapeutic context of LAS17

• To identify other factors implicated with this complex in actin regulation, we isolated proteins that bind to Las17p by two-hybrid screening and affinity chromatography [1].

References