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Originally published In Press as doi:10.1074/jbc.M103384200 on August 6, 2001

J. Biol. Chem., Vol. 276, Issue 42, 38899-38910, October 19, 2001
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Characterization of CD36/LIMPII Homologues in Dictyostelium discoideum*

Klaus-Peter JanssenDagger , René Rost, Ludwig Eichinger§, and Michael Schleicher

From the Institut für Zellbiologie, Ludwig-Maximilians-Universität, 80336 München, Germany

The CD36/LIMPII family is ubiquitously expressed in higher eukaryotes and consists of integral membrane proteins that have in part been characterized as cell adhesion receptors, scavenger receptors, or fatty acid transporters. However, no physiological role has been defined so far for the members of this family that localize specifically to vesicular compartments rather than to the cell surface, namely lysosomal integral membrane protein type II (LIMPII) from mammals and LmpA from the amoeba Dictyostelium discoideum. LmpA, the first described CD36/LIMPII homologue from lower eukaryotes, has initially been identified as a suppressor of the profilin-minus phenotype. We report the discovery and initial characterization of two new CD36/LIMPII-related proteins, both of which share several features with LmpA: (i) their size is considerably larger than that of the CD36/LIMPII proteins from higher eukaryotes; (ii) they show the characteristic "hairpin" topology of this protein family; (iii) they are heavily N-glycosylated; and (iv) they localize to vesicular structures of putative endolysosomal origin. However, they show intriguing differences in their developmental regulation and exhibit different sorting signals of the di-leucine or tyrosine-type in their carboxyl-terminal tail domains. These features make them promising candidates as a paradigm for the study of the function and evolution of the as yet poorly understood CD36/LIMPII proteins.


* This work was supported by grants from the Deutsche Forschungsgemeinschaft and the Fonds der Chemischen Industrie.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 nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF238324 and AF238325.

Dagger Present address and to whom correspondence should be addressed: Cellular Morphogenesis and Signalisation, UMR 144 CNRS-Institut Curie, 25 Rue d'Ulm, 75248 Paris, Cedex 05, France. Tel.: 33 1 42 34 63 61; Fax: 33 1 42 34 63 77; E-mail: klaus-peter.janssen@curie.fr.

§ Present address: Institut für Biochemie I, Med. Einrichtungen der Universität zu Köln, Joseph-Stelzmann-Strasse 52, 50931 Köln, Germany.


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