Email updates

Keep up to date with the latest news and content from BMC Cell Biology and BioMed Central.

Open Access Research article

Inclusion of Scar/WAVE3 in a similar complex to Scar/WAVE1 and 2

Craig F Stovold, Thomas H Millard and Laura M Machesky*

Author Affiliations

School of Biosciences, The University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK

For all author emails, please log on.

BMC Cell Biology 2005, 6:11  doi:10.1186/1471-2121-6-11

Published: 7 March 2005

Additional files

Additional File 1:

Characterization of HSPC300 and Abi1 binding domain of Scar/WAVE1. (A) Schematic representation of the domain architecture of Scar/WAVE family proteins and the deletion constructs used in these experiments. Numbers indicate start or end point of Scar/WAVE1 deletion mutants in amino acid residue position. Start/End points for Scar/WAVE2 deletion mutants are FL = 498, delta A = 456, SPW = 455, SP = 435, SB = 245, SHD = 170, BPWA = 171, PWA = 246. Start/End points for Scar/WAVE3 deletion mutants are FL = 499, delta A = 488, SPW = 457, SP = 439, SB = 238, SHD = 171, BPWA = 172, PWA = 239. FL; Full length. SHD; Scar Homology Domain. B; Basic Rich Region. PRR; Proline rich region. W; Wiskott Homology 2 domain. C; Central or connecting region. A; Acidic Rich Region. (B) Co-immunoprecipitation of HA-Abi1 with Myc-Scar/WAVE deletion constructs. (C) Co-immunoprecipitation of HA-Abi1 or HA-HSPC300 respectively with Myc-Scar/WAVE deletion constructs. Protein G beads were used to immunoprecipitate protein from transiently transfected Cos 7 fibroblasts before (-Ab) and after addition (+Ab) of an anti-Myc (9E10) monoclonal antibody. Bead bound fractions and supernatants (Sup) were analysed by SDS-PAGE followed by immunoblotting. Blots were probed with an anti-HA polyclonal antibody for the presence of HA-Abi1 or HA-HSPC300 in immunoprecipitated complexes.

Format: EPS Size: 455KB Download file

Open Data