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J. Biol. Chem., Vol. 277, Issue 48, 46504-46511, November 29, 2002
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From the Biochemie-Zentrum Heidelberg,
Ruprecht-Karls-Universität Heidelberg, Im Neuenheimer Feld
328, D-69120 Heidelberg, Germany
The p24 proteins belong to a highly conserved
family of membrane proteins that cycle in the early secretory pathway.
They bind to the coat proteins of COPI and COPII vesicles, and are proposed to be involved in vesicle biogenesis, cargo uptake, and quality control, but their precise function is still under debate. Most
p24 proteins form hetero-oligomers, essential for their correct localization and stability. Functional insights regarding the mechanisms of their steady state localization and the role of interaction with coat proteins has been hampered by a lack of data on
their concentration and state of oligomerization within the
endoplasmic reticulum, the intermediate compartment, and Golgi complex. We have determined for all mammalian p24 family
members the size of the oligomers formed and their stoichiometric
relation in each of these individual organelles. In contrast to earlier reports, we show that individual members exist as dimers and monomers and that the ratio between these two forms depends on both the organelle investigated and the p24 protein. We find unequal quantities, with p23 and p27 building up concentration gradients, ruling out a
simple 1:1 stoichiometry. In addition, we show differential cycling of
individual p24 members. These data point to a complex and dynamic
system of altering dimerizations of the family members.
Oligomeric State and Stoichiometry of p24 Proteins in the
Early Secretory Pathway*,
*
Work in the laboratory of the authors is supported by grants
of the German Research Foundation (to B. B. and F. T. W.), the Human
Frontiers Science Program Organization (to F. T. W.), and the Peter
and Traudl Engelhorn Foundation (to B. B.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
The on-line version of this article (available at
http://www.jbc.org) contains Figures I-V and their legends.
To whom correspondence should be addressed. Tel.: 0049-6221544160;
Fax: 0049-6221544366; E-mail:
Felix.Wieland@urz.uni-heidelberg.de.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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