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Coactosin (CLP)

A 17 kDa actin-binding protein originally isolated from Dictyostelium (de Hostos et al, 1993) but since found in humans where it has been discovered to be a binding partner for 5-Lipoxygenase (5LO) (Provost et al, 2001) an enzyme pivotally involved in the production of leukotrienes from arachidonic acid. 5LO is itself an actin-binding protein (Lepley & Fitzpatrick, 1994; Provost et al, 2001a).  The human version of coactosin is named CLP (Coactosin-Like Protein), an F-actin but not a G-actin binding protein (Provost et al 2001b) that apparently inhibits the capping activity of CapZ , despite the fact that CLP itself does not alter the kinetics of actin polymerization (Rohrig et al, 1995).  CLP is expressed in lung, placenta, kidney and leucocytes (Provost et al 2001b) co-localizing with fibers in transfected COS cells. 

Coactosin and CLP both show homology to the ADF/cofilin family (de Hostos et al, 1993) and yet it contains a LKKAET -like motif found in other actin-binding proteins that in the case of CLP is responsible for binding 5LO (Provost et al, 2001a).  Lysine 75 has been found to be important for the binding of actin (Provost et al 2001b).

References

de Hostas, E. L., B. Bradtke, et al. (1993). “Coactosin, a 17 kDa F-actin binding protein from Dictyostelium discoideum.” Cell Mot.Cytoskeleton 26, 181-191.

Lepley, R.A. & Fitzpatrick, F.A. (1994). J.Biol.Chem. 269, 24163-24168

Provost, P., Doucet, J., Hammarberg, T., Gerisch, G., Samuelsson, B. & Radmark, O. (2001a) 5-Lipoxygenase interacts with coactosin-like protein., J. Biol.Chem. 276, 16520-16527.

Provost, P., Doucet, J., Stock, A., Gerisch, G., Samuelsson, B. & Radmark, O. (2001b) Coactosin-like protein, a human F-actin-bining protein: critical role of lysine-75., Biochem. J. 359, 255-263.

Rohrig, U., Gerisch, G., Morozova, L., Schliecher, M. & Wegner, A. (1995) Coactosin interferes with the capping of actin filaments., FEBS letters. 374, 284-286.

 

 
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