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MBC in Press, published online ahead of print August 17, 2005
Mol. Biol. Cell 10.1091/mbc.E05-04-0327

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Submitted on April 20, 2005
Revised on August 9, 2005
Accepted on August 10, 2005

CD74 Is a Member of the Regulated Intramembrane Proteolysis (RIP)-processed Protein Family

Shirly Becker-Herman,* Galit Arie,* Helena Medvedovsky,* Anat Kerem, and Idit Shachar

Department of Immunology, Weizmann Institute of Science, 76100 Rehovot, Israel

Monitoring Editor: Peter Walter

Quite a few regulatory proteins, including transcription factors, are normally maintained in a dormant state to be activated following internal or environmental cues. Recently, a novel strategy, requiring proteolytic cleavage, was described for the mobilization of dormant transcription factors. These transcription factors are initially synthesized in an inactive form, while "nesting" in integral membrane precursor proteins. Following a cleavage event, these new active factors are released from the membrane and can migrate into the nucleus to drive regulated gene transcription. This mechanism, "regulated intramembrane proteolysis (RIP)", controls diverse biological processes in prokaryotes and eukaryotes in response to a variety of signals. The MHC class II chaperone, CD74 (invariant chain, Ii), was previously shown to function as a signaling molecule in several pathways. Recently, we demonstrated that following intramembranal cleavage, the CD74 cytosolic fragment (CD74-ICD) is released and induces activation of transcription mediated by the NF-{kappa}B p65/RelA homodimer and the B cell enriched coactivator, TAFII105. Here, we add CD74 to the growing family of RIP processed proteins. Our studies show that CD74 ectodomain must be processed in the endocytic compartments to allow its intramembrane cleavage that liberates CD74 intracellular domain (CD74-ICD). We demonstrate that CD74-ICD translocates to the nucleus and induces the activation of the p65 member of NF-{kappa}B in this compartment.

* These authors contributed equally to this work.

Address correspondence to: Idit Shachar (idit.shachar{at}weizmann.ac.il)




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