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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 

The giant protein HERC1 is recruited to aluminum fluoride-induced actin-rich surface protrusions in HeLa cells.

HERC1 is a very large protein involved in membrane traffic through both its ability to bind clathrin and its guanine nucleotide exchange factor ( GEF) activity over ARF and Rab family GTPases. Herein, we show that HERC1 is recruited onto actin-rich surface protrusions in ARF6-transfected HeLa cells upon aluminum fluoride (AlF(4)(-)) treatment. Moreover, the fact that HERC1 overexpression does not stimulate protrusion formation in the absence of AlF(4)(-), in conditions where ARNO does, indicates that HERC1 is not acting as an ARF6- GEF in this system, but that instead its recruitment takes place downstream of ARF6 activation. Finally, we suggest a phosphoinositide-binding mechanism whereby HERC1 may translocate to these protrusions.[1]

References

  1. The giant protein HERC1 is recruited to aluminum fluoride-induced actin-rich surface protrusions in HeLa cells. Garcia-Gonzalo, F.R., Muñoz, P., González, E., Casaroli-Marano, R.P., Vilaró, S., Bartrons, R., Ventura, F., Rosa, J.L. FEBS Lett. (2004) [Pubmed]
 
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