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J. Biol. Chem., Vol. 275, Issue 43, 33329-33335, October 27, 2000
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From the Annexins are a family of proteins that bind
phospholipids in a calcium-dependent manner. Analysis of
the sequences of the different members of the annexin family revealed
the presence of a pentapeptide biochemically related to KFERQ in some
annexins but not in others. Such sequences have been proposed to be a
targeting sequence for chaperone-mediated autophagy, a lysosomal
pathway of protein degradation that is activated in confluent cells in response to removal of serum growth factors. We demonstrate that annexins II and VI, which contain KFERQ-like sequences, are degraded more rapidly in response to serum withdrawal, while annexins V and XI,
without such sequences, are degraded at the same rate in the presence
and absence of serum. Using isolated lysosomes, only the annexins
containing KFERQ-like sequences are degraded by chaperone
mediated-autophagy. Annexins V and XI could associate with lysosomes
but did not enter the lysosomes and were not proteolytic substrates.
Furthermore, four annexins containing KFERQ-like sequences, annexins I,
II, IV, and VI, are enriched in lysosomes with high chaperone-mediated
autophagy activity as expected for substrate proteins. These results
provide striking evidence for the importance of KFERQ motifs in
substrates of chaperone-mediated autophagy.
Selective Degradation of Annexins by Chaperone-mediated
Autophagy*
§,
,**
Department of Physiology, Tufts University
School of Medicine, Boston, Massachusetts 02111 and the
¶ Department of Pre-Clinical Sciences, University of the West
Indies, St. Augustine, Eric Williams Medical Sciences Complex, Uriah
Butler Highway, Champs Fleurs,
Trinidad and Tobago, West Indies
*
This work was supported by National Institutes of Health
Grants AG00829 (to A. M. C.) and AG06116 (to J. F. D.), an American Federation for Aging Research research grant
(to A. M. C.), and a grant from the University of the West
Indies Campus Research Fund (to J. A. B.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Current address: Dept. of Molecular and Cellular Pharmacology,
University of Miami, School of Medicine, Miami, FL 33101.
**
To whom correspondence may be addressed: Dept. of Physiology,
Tufts University School of Medicine, 136 Harrison Ave., Boston, MA
02111. Tel.: 617-636-6707; Fax: 617-636-0445; E-mail:
james.dice@tufts.edu.
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