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Journal of Cell Science, Vol 107, Issue 5 1289-1295, Copyright © 1994 by Company of Biologists

JOURNAL ARTICLES

Trafficking of interleukin 2 and transferrin in endosomal fractions of T lymphocytes

V Duprez, M Smoljanovic, M Lieb and A Dautry-Varsat
Unite de Biologie des Interactions Cellulaires, CNRS URA 361, Institut Pasteur, Paris, France.

The T lymphocyte growth factor interleukin 2 binds to surface high-affinity receptors and is rapidly internalized and degraded in acidic organelles. The alpha and beta chains of high-affinity interleukin 2 receptors are internalized together with interleukin 2. To identify the intracellular pathway followed by interleukin 2, we have compared the subcellular distribution of interleukin 2, transferrin and a fluid-phase marker, horseradish peroxidase, in the human T cell line IARC 301.5. Transferrin was used as a marker of early and recycling endosomes, and horseradish peroxidase to probe for the whole endocytic pathway. Fractionation of intracellular organelles on a discontinuous sucrose gradient showed that internalized interleukin 2 is initially mostly found in compartments with similar densities to transferrin, e.g. early and recycling endosomes. The kinetics of entry and exit of interleukin 2 from such organelles was much slower than that of transferrin. Later on, interleukin 2 is predominantly found in dense lysosome-containing fractions. Very little, if any, interleukin 2 was found in fractions corresponding to late endosomes containing horseradish peroxidase. These results suggest that, after endocytosis, interleukin 2 enters early or recycling endosomes before it reaches dense lysosomes.
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A Subtil, A Hemar, and A Dautry-Varsat
Rapid endocytosis of interleukin 2 receptors when clathrin-coated pit endocytosis is inhibited
J. Cell Sci., January 12, 1994; 107(12): 3461 - 3468.
[Abstract] [PDF]


© The Company of Biologists Ltd 1994