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Vol. 11, Issue 2, 531-542, February 2000
Centro di Endocrinologia ed Oncologia Sperimentale del Consiglio
Nazionale delle Ricerche-Dipartimento di Biologia e Patologia
Cellulare e Molecolare, Università degli Studi di Napoli
"Federico II," 80131 Napoli, Italy
In contrast to Madin-Darby canine kidney cells, Fischer rat
thyroid cells deliver the majority of endogenous glycosylphosphatidyl inositol (GPI)-anchored proteins to the basolateral surface.
However, we report here that the GPI proteins Placental Alkaline
Phosphatase (PLAP) and Neurotrophin Receptor-Placental Alkaline
Phosphatase (NTR-PLAP) are apically localized in transfected Fischer
rat thyroid cells. In agreement with the "raft hypothesis," which
postulates the incorporation of GPI proteins into glycosphingolipids
and cholesterol-enriched rafts, we found that both of these proteins were insoluble in Triton X-100 and floated into the lighter fractions of sucrose density gradients. However, disruption of lipid rafts by
removal of cholesterol did not cause surface missorting of PLAP and
NTR-PLAP, and the altered surface sorting of these proteins after
Fumonisin B1 treatment did not correlate with reduced levels in Triton
X-100 -insoluble fractions. Furthermore, in contrast to the
GPI-anchored forms of both of these proteins, the secretory and
transmembrane forms (in the absence of a basolateral cytoplasmic signal) were sorted to the apical surface without association with
lipid microdomains. Together, these data demonstrate that the GPI
anchor is required to mediate raft association but is not sufficient to
determine apical sorting. They also suggest that signals present in the
ectodomain of the proteins play a major role and that lipid rafts may
facilitate the recognition of these signals in the
trans-Golgi network, even though they are not required
for apical sorting.
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