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Originally published In Press as doi:10.1074/jbc.M009430200 on February 22, 2001

J. Biol. Chem., Vol. 276, Issue 19, 15905-15912, May 11, 2001
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Scp160p, an RNA-binding, Polysome-associated Protein, Localizes to the Endoplasmic Reticulum of Saccharomyces cerevisiae in a Microtubule-dependent Manner*

Steffen Frey, Martin Pool, and Matthias SeedorfDagger

From the Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), Im Neuenheimer Feld 282, D-69120 Heidelberg, Germany

Scp160p is an RNA-binding protein containing 14 tandemly repeated heterogenous nuclear ribonucleoprotein K-homology domains, which are implicated in RNA binding. Scp160p interacts with free and membrane-bound polysomes that are dependent upon the presence of mRNA. Despite its presence on cytosolic polysomes, Scp160p is predominantly localized to the endoplasmic reticulum (ER). Accumulation of Scp160p-ribosome complexes at the ER requires the function of microtubules but is independent of the actin cytoskeleton. We propose that the multi-K-homology-domain protein Scp160p functions as an RNA binding platform, interacting with polysomes that are transported to the ER.

* This work was supported by Sonderforschungsbereich 352 (to M. S.).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.

Dagger To whom correspondence should be addressed. Tel.: 49 6221 548299; Fax: 49 6221 545892; E-mail: m.seedorf@zmbh.uni-heidelberg.de.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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