(Downloading may take up to 30 seconds.
If the slide opens in your browser, select File -> Save As to save it.)
Click on image to view larger version.

Fig. 2. Domain structures of actin regulatory proteins important for T-cell activation. Binding partners are shown below the domain with which they associate. Sites of phosphorylation that have been implicated in regulating protein function are indicated. Regions with sequence and functional similarity are similarly colored. Note, for example, that WASp and WAVE proteins share a conserved VCA domain responsible for binding actin monomers and the Arp2/3 complex. This domain consists of three subdomains: the WASp-homology 2 (WH2)/verprolin region, a cofilin homology region and an acidic region. HS1 contains only the acidic subdomain within its N-terminal acidic region (NTA), whereas WIP contains two copies of the WH2/verprolin subdomain. Note also the prevalence of proline-rich regions (Pro) among actin regulatory proteins at the IS; these regions are responsible for numerous interactions with SH3-domain-containing proteins involved in T-cell signaling. WH1, WASp homology domain 1; GBD, GTPase binding domain; WHD, WAVE homology domain; BR, basic region; HTH, helix-turn-helix (cortactin) repeat region; CC, coiled-coil region; SH3, Src homology 3 domain; ADF, actin depolymerizing factor/cofilin; FERM, Band 4.1, ezrin, radixin moesin homology domain.