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Vol. 10, Issue 2, 455-469, February 1999
Department of Microbiology and Immunology, University of Tennessee
Health Science Center, Memphis, Tennessee 38163
Chicken erythroid AE1 anion exchangers receive endoglycosidase F
(endo F)-sensitive sugar modifications in their initial transit through
the secretory pathway. After delivery to the plasma membrane, anion
exchangers are internalized and recycled to the Golgi where they
acquire additional N-linked modifications that are resistant to endo F. During recycling, some of the anion exchangers become detergent
insoluble. The acquisition of detergent insolubility correlates with
the association of the anion exchanger with cytoskeletal ankyrin.
Reagents that inhibit different steps in the endocytic pathway,
including 0.4 M sucrose, ammonium chloride, and brefeldin A,
block the acquisition of endo F-resistant sugars and the acquisition of
detergent insolubility by newly synthesized anion exchangers. The
inhibitory effects of ammonium chloride on anion exchanger processing
are rapidly reversible. Furthermore, AE1 anion exchangers become
detergent insoluble more rapidly than they acquire endo F-resistant
modifications in cells recovering from an ammonium chloride block. This
suggests that the cytoskeletal association of the recycling anion
exchangers occurs after release from the compartment where they
accumulate due to ammonium chloride treatment, and prior to their
transit through the Golgi. The recycling pool of newly synthesized
anion exchangers is reflected in the steady-state distribution of the
polypeptide. In addition to plasma membrane staining, anion exchanger
antibodies stain a perinuclear compartment in erythroid cells. This
perinuclear AE1-containing compartment is also stained by ankyrin
antibodies and partially overlaps the membrane compartment stained by
NBD C6-ceramide, a Golgi marker. Detergent
extraction of erythroid cells in situ has suggested that a substantial
fraction of the perinuclear pool of AE1 is cytoskeletal associated. The
demonstration that erythroid anion exchangers interact with elements of
the cytoskeleton during recycling to the Golgi suggests the
cytoskeleton may be involved in the post-Golgi trafficking of this
membrane transporter.
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