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A more recent version of this article appeared on February 24, 2006
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M508632200v1
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Papers In Press, published online ahead of print December 20, 2005
J. Biol. Chem, 10.1074/jbc.M508632200
Submitted on August 5, 2005
Revised on November 28, 2005
Accepted on December 20, 2005

Degradation of endocytosed epidermal growth factor and virally-ubiquitinated MHC class I is independent of mammalian ESCRTII

Katherine Bowers, Sian C Piper, Melissa A Edeling, Sally R Gray, David J Owen, Paul J Lehner, and J Paul Luzio

Cambridge Institute for Medical Research and Dept. Clinical Biochemistry, University of Cambridge, Cambridge, Cambs CB2 2XY

Corresponding Author: kb123{at}cam.ac.uk

Models for protein sorting at multivesicular bodies in the endocytic pathway of mammalian cells have relied largely on data obtained from yeast. These data suggest the essential role of four ESCRT complexes in multivesicular body protein sorting. However, the putative mammalian ESCRTII complex (hVps25p, hVps22p and hVps36p) has no proven functional role in endosomal transport. We have characterized the human ESCRTII complex, and investigated its function in endosomal trafficking. The human ESCRTII proteins interact with one another, with hVps20p (a component of ESCRTIII) and with their yeast homologues. Our interaction data from yeast two hybrid studies along with experiments with purified proteins suggest an essential role for the N-terminal domain of hVps22p in the formation of a heterotetrameric ESCRTII complex. Although human ESCRTII is found in the cytoplasm and in the nucleus, it can be recruited to endosomes on overexpression of dominant-negative hVps4Bp. Interestingly, we find that siRNA depletion of mammalian ESCRTII does not affect degradation of epidermal growth factor, a known cargo of the multivesicular body protein sorting pathway. We also show that depletion of the deubiquitinating enzymes AMSH and UBPY have opposite effects on EGF degradation, with UBPY-depletion causing dramatic swelling of endosomes. Down-regulation of another cargo, the major histocompatibility complex class I in cells expressing the Kaposi's sarcoma-associated herpesvirus protein K3, is unaffected in ESCRTII-depleted cells. Our data suggest that mammalian ESCRTII may be redundant, cargo-specific or not required for protein sorting at the multivesicular body.


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