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Originally published In Press as doi:10.1074/jbc.M002373200 on June 26, 2000

J. Biol. Chem., Vol. 275, Issue 39, 30653-30659, September 29, 2000
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The Long Signal Peptide Isoform and Its Alternative Processing Direct the Intracellular Trafficking of Interleukin-15*

Gloria KurysDagger , Yutaka TagayaDagger , Richard BamfordDagger , John A. Hanover§, and Thomas A. WaldmannDagger

From the Dagger  Metabolism Branch, NCI, National Institutes of Health and the § Laboratory of Cell Biochemistry and Biology, NIDDK, National Institutes of Health, Bethesda, Maryland 20892-1374

Two isoforms of interleukin (IL)-15 exist: one with a short and another with a long signal peptide (LSP). Experiments using combinations of the LSP and mature proteins IL-2, IL-15, and green fluorescent protein revealed complex pathways of intracellular trafficking. In one pathway, the LSP was unprocessed, and IL-15 was not glycosylated, remained in the cytoplasm, and was degraded. The second trafficking pathway involved endoplasmic reticulum entry, N-linked glycosylation, and alternative partial LSP processing. The third pathway involved endoplasmic reticulum entry, followed by glycosylation, complete processing, and ultimately secretion. The complex intracellular trafficking patterns of LSP-IL-15 with its impediments to secretion as well as impediments to translation may be required due to the potency of IL-15 as an inflammatory cytokine. In terms of a more positive role, we propose that intracellular infection may relieve the burdens on translation and intracellular trafficking to yield effective IL-15 expression.

* 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.

To whom correspondence should be addressed: National Cancer Institute, NIH, Bldg. 10, Rm. 4N115, 10 Center Drive, MSC 1374, Bethesda, MD 20892-1374. Tel.: 301-496-6653; Fax: 301-496-9956; E-mail: tawald@ helix.nih.gov.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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