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Vol. 9, Issue 11, 3133-3146, November 1998
§
*Combined Program in Pediatric Gastroenterology and Nutrition,
Massachusetts General Hospital East, Charlestown, Massachusetts 02129;
and
ARNO is a member of a family of guanine-nucleotide exchange
factors with specificity for the ADP-ribosylation factor (ARF) GTPases. ARNO possesses a central catalytic domain with homology to
yeast Sec7p and an adjacent C-terminal pleckstrin homology (PH) domain.
We have previously shown that ARNO localizes to the plasma membrane in
vivo and efficiently catalyzes ARF6 nucleotide exchange in vitro. In
addition to a role in endocytosis, ARF6 has also been shown to regulate
assembly of the actin cytoskeleton. To determine whether ARNO is an
upstream regulator of ARF6 in vivo, we examined the distribution of
actin in HeLa cells overexpressing ARNO. We found that, while
expression of ARNO leads to disassembly of actin stress fibers, it does
not result in obvious changes in cell morphology. However, treatment of
ARNO transfectants with the PKC agonist phorbol 12-myristate 13-acetate
results in the dramatic redistribution of ARNO, ARF6, and actin into
membrane protrusions resembling lamellipodia. This process requires ARF activation, as actin rearrangement does not occur in cells expressing a
catalytically inactive ARNO mutant. PKC phosphorylates ARNO at a site
immediately C-terminal to its PH domain. However, mutation of this site
had no effect on the ability of ARNO to regulate actin rearrangement,
suggesting that phosphorylation of ARNO by PKC does not positively
regulate its activity. Finally, we demonstrate that an ARNO mutant
lacking the C-terminal PH domain no longer mediates cytoskeletal
reorganization, indicating a role for this domain in appropriate
membrane localization. Taken together, these data suggest that ARNO
represents an important link between cell surface receptors, ARF6, and
the actin cytoskeleton.
Program in Immunology and
Program in
Biological and Biomedical Sciences, Harvard Medical School, Boston,
Massachusetts 02115
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