2002
DOI: 10.1002/jcb.10112
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Analysis of the carboxypeptidase D cytoplasmic domain: Implications in intracellular trafficking*

Abstract: Metallocarboxypeptidase D (CPD) is a type 1 transmembrane protein that functions in the processing of proteins that transit the secretory pathway. Previously, CPD was found to be enriched in the trans Golgi network (TGN) and to cycle between this compartment and the cell surface. In the present study, the roles of specific regions of the CPD cytosolic tail in intracellular trafficking were investigated in the AtT-20 cell line. When the CPD transmembrane region and cytosolic tail are attached to the C-terminus … Show more

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Cited by 39 publications
(43 citation statements)
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“…Although tetraspanins are sometimes associated with lipid rafts, the buoyant density of tetraspanins that could not be palmitoylated was no different to that of wild-type proteins, suggesting that targeting to detergent-resistant lipid rafts is not the main function of palmitoylation of these proteins (Stipp et al, 2003). Palmitoylation of carboxypeptidase D also has no effect on lipid-raft localization (Kalinina and Fricker, 2003). In the present study, we find that transfected wild-type claudin-14 is enriched in the fractions containing caveolin relative to the mutant protein.…”
Section: Discussionmentioning
confidence: 93%
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“…Although tetraspanins are sometimes associated with lipid rafts, the buoyant density of tetraspanins that could not be palmitoylated was no different to that of wild-type proteins, suggesting that targeting to detergent-resistant lipid rafts is not the main function of palmitoylation of these proteins (Stipp et al, 2003). Palmitoylation of carboxypeptidase D also has no effect on lipid-raft localization (Kalinina and Fricker, 2003). In the present study, we find that transfected wild-type claudin-14 is enriched in the fractions containing caveolin relative to the mutant protein.…”
Section: Discussionmentioning
confidence: 93%
“…1). By analogy to comparable sequences in the tetraspanins (Stipp et al, 2003) and some other integral membrane proteins (Bijlmakers and Marsh, 2003;Kalinina and Fricker, 2003), we reasoned that these cysteines might be modified by fatty-acid acylation with palmitic acid. To test this possibility, we first used [ 3 H]-palmitic acid to label endogenous claudins in MDCK cells.…”
Section: Claudins Are Palmitoylatedmentioning
confidence: 99%
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“…Palmitoylation can target proteins to rafts and thus also might sort these proteins into cholesterol-rich Golgi domains in the Golgi. Palmitoylation also enhances Golgi transport of some transmembrane proteins (van't Hof and Crystal, 2002;Kalinina and Fricker, 2003), possibly through the same mechanism.…”
Section: Golgi Transport Of Caveolin-1 Is Unusually Difficultmentioning
confidence: 98%