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Vol. 10, Issue 6, 1997-2015, June 1999
*Cell Biology Unit, Institut de Genetique Humaine, Centre National
de la Recherche Scientifique UPR 1142, F-34396 Montpellier Cedex
5, France; and The intermediate filament protein vimentin is a major
phosphoprotein in mammalian fibroblasts, and reversible phosphorylation plays a key role in its dynamic rearrangement. Selective inhibition of
type 2A but not type 1 protein phosphatases led to hyperphosphorylation and concomitant disassembly of vimentin, characterized by a collapse into bundles around the nucleus. We have analyzed the potential role of
one of the major protein phosphatase 2A (PP2A) regulatory subunits,
B55, in vimentin dephosphorylation. In mammalian fibroblasts, B55
protein was distributed ubiquitously throughout the cytoplasm with a
fraction associated to vimentin. Specific depletion of B55 in living
cells by antisense B55 RNA was accompanied by disassembly and increased
phosphorylation of vimentin, as when type 2A phosphatases were
inhibited using okadaic acid. The presence of B55 was a prerequisite for PP2A to efficiently dephosphorylate vimentin in vitro or to induce
filament reassembly in situ. Both biochemical fractionation and
immunofluorescence analysis of detergent-extracted cells revealed that
fractions of PP2Ac, PR65, and B55 were tightly associated with
vimentin. Furthermore, vimentin-associated PP2A catalytic subunit was
displaced in B55-depleted cells. Taken together these data show that,
in mammalian fibroblasts, the intermediate filament protein vimentin is
dephosphorylated by PP2A, an event targeted by B55.
Friedrich Miescher-Institut, CH-4002
Basel, Switzerland
Corresponding author. E-mail address:
ned{at}igh.cnrs.fr.
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