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J. Biol. Chem., Vol. 269, Issue 3, 1668-1673, 01, 1994
GM Preston, JS Jung, WB Guggino and P Agre
CHIP is the archetypal member of the aquaporins, a widely expressed family
of membrane water channels. The NH2- and COOH-terminal halves of CHIP are
sequence-related, and hydropathy analysis predicted six membrane-spanning
domains with five connecting loops (A-E). Here, we determined the membrane
topology of CHIP expressed in Xenopus oocytes using biologically active
recombinant channels. CHIP is glycosylated at Asn-42, indicating loop A is
exofacial. An epitope from the coronavirus E1 glycoprotein was inserted
into CHIP and localized to the outer or inner leaflet of the membrane by
alpha-chymotrypsin digestion of intact oocytes or inside-out membrane
vesicles. The E1 epitope at Thr-120 was protease-sensitive in intact
oocytes, indicating that loop C is exofacial. The E1 epitope at Lys-6,
Arg-162, or Lys-267 was protease- sensitive in inside-out membrane
vesicles, confirming the cytoplasmic location of the NH2 and COOH termini
and loop D. Insertions into loops B and E did not produce active water
channels, but their cleavage patterns were consistent with inner (loop B)
and outer (loop E) leaflet locations. This study indicates that the
functional CHIP molecule is a unique structure with two internal repeats
oriented 180 degrees to each other within the membrane.
Membrane topology of aquaporin CHIP. Analysis of functional epitope- scanning mutants by vectorial proteolysis
Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
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