Fig. 1: SH3 domains of Sla1 bind Las17 and inhibit Arp2/3-dependent nucleation of actin polymerisation by Las17. | Communications Biology

Fig. 1: SH3 domains of Sla1 bind Las17 and inhibit Arp2/3-dependent nucleation of actin polymerisation by Las17.

From: Competitive binding of actin and SH3 domains at proline-rich regions of Las17/WASP regulates actin polymerisation

Fig. 1

A Schematic diagram outlining one possible arrangement of Sla1 SH3 domains bound to the N-terminal PPR of Las17 (amino acids 300-422). SH3 domains of Sla1 are numbered #1, #2 and #3. The PPR-N of Las17 is the region shown to bind SH3 domains. PP in pink boxes indicate poly-proline tracts in this region. Other regions of Las17 are included but not to scale. B Representative pyrene actin assays show inhibition of Las17-Arp2/3 mediated actin polymerisation by Sla1-SH3 domains when added as separate domains (orange #1, green #2 or cyan #3) or on a single peptide (red). Actin; 3 µM, Las17; 300 nM, and Sla1 SH3 domains; 300 nM each. C Biolayer Interferometry measurements of the affinity of Sla1 SH3 domains for Las17 (aa 300-422). Sla1 SH3#1 (aa 3-68), SH3#3 (aa 354-413), SH3#1-2 (aa 5-131), SH3#1-3 (aa 5-413).

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