Fig. 8: Las17 P387 is not required for Las17 binding to Sla1 SH3 domains. | Communications Biology

Fig. 8: Las17 P387 is not required for Las17 binding to Sla1 SH3 domains.

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

Fig. 8

A Purified individual GST-tagged Sla1 SH3 domains were used to probe a Celluspot array consisting of a series of 12 amino acid peptides starting with residue 181, and subsequent peptides starting at two amino acid intervals, up to amino acid 540. Binding of GST-Sla1 SH3 to the array was identified by further probing of HRP-tagged anti-GST and subsequent visualisation using chemiluminescence. Peptide spots corresponding to actin binding sites on Las17 (pink), additional spots including P387A (red) and P388A (green) and their corresponding wild type peptide (blue) are also shown. Binding to the peptide containing P387A is strongly reduced or abrogated for each Sla1 SH3 domain. B Microscale Thermophoresis of Las17 300–422 wild type (blue), P387A (red) and P388A (green) showing that neither of these mutations affects Las17 binding to actin. Error bars are standard error of mean.

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