AFAP

AFAP-110

A PH containing actin-binding protein (Flynn et al, 1993), containing an alpha-helical N-terminal region capable of self association through a leucine zipper interaction (Qian et al, 1998). AFAP-110 is a Src substrate and phosphorylation regulates self association (Qian et al, 1998). Most multi-domain, actin-binding proteins have their actin-binding region at, or close to the N-terminus (e.g. a-actinin, dystrophin, Abp1p, calponin), but AFAP-110 has its actin-binding domain at the C-terminus (Qian et al, 2000). The actin-binding domain of AFAP-110 is similar to CH domain of many other actin binding proteins.

References:-

Baisden, J. M., Gatesman, A. S., Cherezova, L., Jiang, B.-H. & Flynn, D. C. (2001) The intrinsic ability of AFAP-110 to alter actin filament integrity is linked with its ability to also activate cellular tyrosine kinases. Oncogene. 20, 6607-6616.

Flynn, D. C., Leu, T.-H., Reynolds, A. B. & Parsons, J. T. (1993) Identification and sequence analysis of cDNAs encoding a 110-Kilodalton actin filament-associated pp60^src substrate. Mol.Cell.Biol. 13, 7892-7900.

Guappone, A. C., Weimer, T. & Flynn, D. C. (1998) Formation of a stable src-AFAP-110 complex through either an amino-terminal or a carboxy-terminal SH2-binding motif. Molecular Carcinogenesis. 22, 110-119.

Qian, Y., Baisden, J. M., Zot, H. G., Van Winkle, W. B. & Flynn, D. C. (2000) The carboxy terminus of AFAP-110 modulates direct interactions with actin filaments and regulates its ability to alter actin filament integrity and induce lamellipodia formation. Exp.Cell Res. 255, 102-113.

Qian, Y., Baisden, J. M., Westin, E. H., Guappone, A. C., Kaoy, T. C. & Flynn, D. C. (1998) Src can regulate carboxy terminal interactions with AFAP-110, which influence self-association, cell localization and actin filament intergrity. Oncogene. 16, 2185-2195.