RasGap-related protein. A single CH domain exists in Vav (Adams
et al, 1992) and this has been suggested as
being the actin-binding region of Vav (Castresana
& Saraste, 1995). The CH (calponin homology)
domain is found usually in tandem in actin binding proteins. However, it
is generally been found that a single CH domain is insufficient for actin
binding (Gimona & Mittal, 1998).
J.M., Houston, H., Allen, J., Lints, T. and Harvey, R. (1992) Oncogene 7,
J. & Saraste, M. (1995). "Does Vav bind F-actin through a CH domain? FEBS
letters 374, 149-151.
M. & Mital, R. (1998). "The single CH domain of calponin is neither
sufficient nor necessary for F-actin binding." J.Cell Sci. 111,
Kranewitter, W. J. & Gimona, M. (1999) N-terminally
truncated Vav induces the formation of depolymerization-resistant actin
filaments in NIH 3T3 cells., FEBS letters. 455, 123-129.
Fackler, O. T., Luo, W., Geyer, M., Alberts, A. S.
& Peterlin, B. M. (1999) Activation of Vav by Nef induces cytoskeletal
rearrangements and downstream effector functions., Mol.Cell. 3, 729-739.