protein first identified (Robinson
et al, 1994)
in the Drosophila mutant of the same name that have disorganised canal
protein has four domains. From N to C, they are NTR N-terminal region
responsible for the timing of the protein localization to the canal, the BTB
region through which the protein self associates to form dimers, the IVR
interveneing region required for localization, the KREP, kelch repeat domain
consisting of six repeats . Many other proteins contain kelch-like repeat,
some of these have been shown to bind actin. Scruin
(Schmid et al,
1991) is the best
characterised of the ABPs that bind actin through KREPs. Drosophila
Kelch binds actin through KREP number 5 (Kelso
et al, 2002),
and this actin binding is inhibited by phosphorylation of tyr 627 by src64
Hara, T., Ishida, H., Raziuddin, R., Dorkhom,
S., Kamijo, K. & Miki, T. (2004) Novel Kelch-like Protein, KLEIP, Is Involved in
Actin Assembly at Cell-Cell Contact Sites of Madin-Darby Canine Kidney Cells.
Mol. Biol. Cell. 15, 1172-1184.
Kelso, R. J.,
Hudson, A. M. & Cooley, L. (2002) Drosophila kelch regulates actin
organization via Src64-dependent tyrosine phosphorylation., J.Cell Biol. 156,
Robinson, D. N., Cant, K. & Cooley, L.
(1994). "Morphogenesis of Drosophila ovarian ring canals." Development
Robinson, D. N. & Cooley, L. (1997). "Drosophila
Kelch is an oligomeric ring canal actin organizer." J.Cell Biol. 138(4),
Schmid, M.F., Matsudaira, P., Jeng, T.-W., Jakana, J.,
Towns-Andrews, E., Bordas, J. & Chiu, W. (1991). "Crystallographic
analysis of acrosomal bundle from Limulus sperm." J.Mol.Biol.
Vega, L. R. & , F. Solomon (1997).
"Microtubule function in morphological differentiation: Growth zones and
growth cones." Cell 89, 825-828.
L., Gregoire, F. & Sul, H.S. (2000). "Transient induction of ENC-1, a
kelch-related actin-binding protein, is required for adipocyte
differentiation." J.Biol.Chem. 275(22), 16845-16850.