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Vav

A 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).

References:-

Adams, J.M., Houston, H., Allen, J., Lints, T. and Harvey, R. (1992) Oncogene 7, 611-618.

Castresana, J. & Saraste, M. (1995). "Does Vav bind F-actin through a CH domain? FEBS letters 374, 149-151.

Gimona, M. & Mital, R. (1998). "The single CH domain of calponin is neither  sufficient nor necessary for F-actin binding." J.Cell Sci. 111, 1813-1821.

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.

 
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