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J Biol Chem, Vol. 274, Issue 44, 31593-31596, October 29, 1999
Ca2+-dependent Association of S100A6
(Calcyclin) with the Plasma Membrane and the Nuclear Envelope
Theresia B.
Stradal and
Mario
Gimona
From the Department of Cell Biology, Institute of Molecular
Biology, Austrian Academy of Sciences, Billrothstrasse 11, A-5020
Salzburg, Austria
Expression of S100A6 (Calcyclin), a member of the
S100 family and of Zn2+-binding proteins is elevated
in a number of malignant tumors. In vitro the protein
associates with several actin-binding proteins and annexins in a
Ca2+-dependent manner. We have now studied the
subcellular localization of S100A6 using a new, specific monoclonal
antibody. Immunofluorescence microscopy of unfixed, ultrathin, frozen
sections demonstrated a dual localization of S100A6 at the nuclear
envelope and the plasma membrane of porcine smooth muscle only in the
presence of Ca2+. The same localization was found by
immunofluorescence and immunogold electron microscopy as well as by
confocal laser scanning microscopy with cultured, fixed, human CaKi-2
and porcine ST interphase cells. Upon cell division, however, S100A6
was found exclusively in the cytoplasm. Cell fractionation studies
showed that S100A6 was present in the microsomal fraction in the
presence of Ca2+ and was released from this fraction by the
addition of EGTA/EDTA but not by Triton X-100. The data demonstrate
that S100A6 is localized both at the plasma membrane and the nuclear
envelope in vivo and suggest a
Ca2+-dependent interaction with annexins or
other components of the nuclear envelope.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.

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Copyright © 1999 by the American Society for Biochemistry and Molecular Biology.
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