Cutting edge: Proteasome involvement in the degradation of unassembled Ig light chains

Thomas O'Hare, Gregory D. Wiens, Elizabeth A. Whitcomb, Caroline A. Enns, Marvin B. Rittenberg

Research output: Contribution to journalArticle

21 Scopus citations

Abstract

Several studies on disposal of nonsecreted Ig L chains have identified the endoplasmic reticulum as the site of degradation. Here, we examine degradation of a nonsecreted Ig L chain, T15L, and an experimentally endoplasmic reticulum-retained secretion-competent L chain, D16L, in the absence of H chains. We demonstrate that 1) degradation is specifically impaired by the proteasome-specific inhibitors carboxybenzyl-leucyl-leucyl- leucine vinyl sulfone (Z-L3VS) and lactacystin, 2) L chain degradation occurs early in the biosynthetic pathway, and 3) degradation does not require vesicular transport. Our findings indicate that previous assertions of L chain disposal within the endoplasmic reticulum must be modified. To our knowledge, we provide the first direct evidence supporting a new paradigm for removal of nonsecreted Ig L chains via dislocation to cytosolic proteasomes.

Original languageEnglish (US)
Pages (from-to)11-14
Number of pages4
JournalJournal of Immunology
Volume163
Issue number1
StatePublished - Jul 1 1999

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

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    O'Hare, T., Wiens, G. D., Whitcomb, E. A., Enns, C. A., & Rittenberg, M. B. (1999). Cutting edge: Proteasome involvement in the degradation of unassembled Ig light chains. Journal of Immunology, 163(1), 11-14.