Journal
JOURNAL OF CELLULAR PHYSIOLOGY
Volume 215, Issue 3, Pages 794-802Publisher
WILEY
DOI: 10.1002/jcp.21364
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Funding
- Telethon [GGP06155] Funding Source: Medline
- Associazione Italiana per la Ricerca sul Cancro Funding Source: Custom
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When expressed in the absence of light chains, secretory I1g-mu chains (R,) undergo endoplasmic reticulum associated degradation (ERAD). This process involves the recognition of terminally misfolded or unassembled molecules, their retro-translocation across the ER membrane and ubiquitination for degradation by cytosolic proteasomes. The molecular components of the ERAD pathway and their coordination remain largely unknown. Here we employed co-immunoprecipitation, silencing or over-expression assays to show that SELIL and HRD1 are involved in the degradation of unassembled Ig-mu(s), but have minor effects on another substrate, TCR-alpha. SELIL and HRD1 localize in the early secretory apparatus and are induced by ER stress and during B cell differentiation, concomitantly with the onset of massive IgM secretion. These findings reveal a role for SELIL and HRD1 in IgM quality control.
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