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The giant protein HERC1 is recruited to aluminum fluoride‐induced actin‐rich surface protrusions in HeLa cells
Author(s) -
Garcia-Gonzalo Francesc R,
Muñoz Purificación,
González Elena,
Casaroli-Marano Ricardo P,
Vilaró Senén,
Bartrons Ramon,
Ventura Francesc,
Rosa Jose Luis
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(04)00030-4
Subject(s) - guanine nucleotide exchange factor , rab , microbiology and biotechnology , actin , gtpase , transfection , chemistry , hela , clathrin , biophysics , biology , endocytosis , biochemistry , receptor , cell , gene
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.