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J. Biol. Chem., Vol. 275, Issue 38, 29887-29893, September 22, 2000
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From the Section on Cellular Neurobiology, Laboratory of
Developmental Neurobiology, NICHD, National Institutes of Health,
Bethesda, Maryland 20892
Membrane carboxypeptidase E (CPE) is a sorting
receptor for targeting prohormones, such as
pro-opiomelanocortin, to the regulated secretory pathway in
endocrine cells. Its membrane association is necessary for it to bind a
prohormone sorting signal at the trans-Golgi network (TGN)
to facilitate targeting. In this study, we examined the lipid
interaction of CPE in bovine pituitary secretory granule membranes,
which are derived from the TGN. We show that CPE is associated with
detergent-resistant lipid domains, or rafts, within secretory granule
membranes. Lipid analysis revealed that these rafts are enriched in
glycosphingolipids and cholesterol. Pulse-chase and subcellular
fractionation experiments in AtT-20 cells show that the association of
CPE with membrane rafts occurred only after it reached the Golgi.
Cholesterol depletion resulted in dissociation of CPE from secretory
granule membranes and decreased the binding of prohormones to
membranes. In vivo cholesterol depletion using lovastatin
resulted in the lack of sorting of CPE and its cargo to the regulated
secretory pathway. We propose that the sorting receptor function of CPE
necessitates its interaction with glycosphingolipid-cholesterol rafts
at the TGN, thereby anchoring it in position to bind to its prohormone cargo.
Lipid Raft Association of Carboxypeptidase E Is Necessary for Its
Function as a Regulated Secretory Pathway Sorting Receptor*
*
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.
To whom correspondence should be addressed: Bldg. 49, Rm. 5A38,
MSC 4480, National Institutes of Health, 9000 Rockville Pike, Bethesda,
MD 20892-4480. Tel.: 301-496-3239; Fax: 301-496-9938; E-mail:
ypl@codon.nih.gov.
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