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 The protein was isolated first from Dictyostelium (Condeelis & Geosits, 1990) it became clear ABP120 that belongs to the filamin group of actin binding proteins when the cDNA was cloned and sequenced (Noegel et al, 1989).  These share a similar actin binding domain with, a-actinin, dystrophin, filamin and b-spectrin amongst others, and an elongated tail consisting of seven b-sheet Ig-like repeats.  The protein dimerizes through a self associating, explaining how the protein crosslinks actin.  The actin binding region of ABP has been identified to within a 27 amino-acid region (Bresnick et al,1990;1991). Dictyostelium also expresses another filamin like protein - ABP240, but deletion of ABP120 alters the structure of actin filaments in vivo (Cox et al, 1995), leading to altered motility (Cox et al, 1992), the phenotype can be rescued by re-expression 


Bresnick, A., V. Warren, et al. (1990). “Identification of a short sequence essential for actin binding by Dictyostelium ABP-120.” J. Biol. Chem. 265, 9236-9240.

Bresnick, A. R., P. A. Janmey, et al. (1991). “Evidence that a 27-residue sequence is the actin-binding site of ABP-120.” J. Biol. Chem. 266, 12989-12993.

Brink, M., G. Gerisch, et al. (1990). “A Dictyostelium mutant lacking an F-actin cross-linking protein the 120-kD gelation factor.” J.Cell Biol. 111, 1477-1489.

Condeelis, J. A., S. Geosits, et al. (1982). "Isolation of a new actin-binding protein from Dictyostelium discoideum." Cell Motil. 2, 273-285.

Cox, D., J. Condeelis, et al. (1992). “Targeted Disruption of the ABP-120 Gene Leads to Cells with Altered Motility.”  J. Cell Biol. 116(4), 943-955.

Cox, D., J. A. Ridsdale, et al. (1995). “Genetic deletion of ABP-120 alters the three-dimensional organization of actin filaments in Dictyostelium pseudopods.” J. Cell Biol. 128: 819-835.

Fukui, Y., E. de Hostos, et al. (1999). "Architectural dynamics of F-actin in eupodia suggests their role in invasive locomotion in Dictyostelium." Exp.Cell Res. 249, 33-45.

Pang, K. M., E. Lee, et al. (1998). "Use of fusion protein between GFP and an actin binding domain to visualize transient filamentous-actin structures." Curr. Biol. 8, 405-408.

Ponte, E., Rivero, F., Fechheimer, M., Noegel, A.A., & Bozzaro, S. (2000). "Severe developmental defects in Dictyostelium discoidium null mutants for actin-binding proteins." Mech.Development 91, 153-161.

Noegel, A. A., Rapp, S., Lottspeich, F., Schleicher, M. & Stewart, M. (1989) The Dictyostelium gelation factor shares a putative actin binding site with a-actinins and dystrophin and also has a rod domain containing six 100-residue motifs that appear to have a cross-beta conformation, J. Cell Biol. 109, 607-618.


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