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J. Biol. Chem., Vol. 278, Issue 21, 18922-18929, May 23, 2003

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Immunoglobulin Light Chains Dictate Vesicular Transport-dependent and -independent Routes for IgM Degradation by the Ubiquitin-Proteasome Pathway^*

Yechiel Elkabetz  , Anat Kerem  , Lilach Tencer , Dorit Winitz , Ron R. Kopito ¶ and Shoshana Bar-Nun  ||

From the Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel, ^¶ Department of Biological Sciences, Stanford University, Stanford, California 94305

Degradation of IgM µ heavy chains in light chain-negative pre-B cells is independent of vesicular transport, as is evident by its insensitivity to brefeldin A or cell permeabilization. Conversely, by the same criteria, degradation of the secretory µs heavy chain in light chain-expressing B cells depends on vesicular transport. To investigate whether the presence of conventional light chains or the developmental stage of the B-lymphocytes dictates the degradative route taken by µ, we express in 70Z/3 pre-B cells either ectopically or by lipopolysaccharides-stimulated differentiation into B cells and show their assembly with µ heavy chains. The resulting sensitivity of µ degradation to brefeldin A and cell permeabilization demonstrates that conventional light chains, a hallmark of B cell differentiation, are necessary and sufficient to divert µ from a vesicular transport-independent to a vesicular transport-dependent degradative route. Although both routes converge at the ubiquitin-proteasome degradation pathway, only in light chain-expressing cells is vesicular transport a prerequisite for µ ubiquitination.

Received for publication, August 26, 2002 , and in revised form, February 25, 2003.

^|| To whom correspondence should be addressed. Tel.: 972-3-6408984; Fax: 972-3-6406834; E-mail: sbnun{at}post.tau.ac.il.

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