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J. Biol. Chem., Vol. 276, Issue 52, 49221-49227, December 28, 2001
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From the The NHE6 protein is a unique
Na+/H+ exchanger isoform believed
to localize in mitochondria. It possesses a hydrophilic N-terminal portion that is rich in positively charged residues and many
hydrophobic segments. In the present study, signal sequences in the
NHE6 molecule were examined for organelle localization and membrane
topogenesis. When the full-length protein was expressed in COS7 cells,
it localized in the endoplasmic reticulum and on the cell surface.
Furthermore, the protein was fully N-glycosylated. When
green fluorescent protein was fused after the second (H2) or third (H3)
hydrophobic segment, the fusion proteins were targeted to the
endoplasmic reticulum (ER) membrane. The localization pattern
was the same as that of fusion proteins in which green fluorescent
protein was fused after H2 of NHE1. In an in vitro system,
H1 behaved as a signal peptide that directs the translocation of the
following polypeptide chain and is then processed off. The next
hydrophobic segment (H2) halted translocation and eventually became a
transmembrane segment. The N-terminal hydrophobic segment (H1) of NHE1
also behaved as a signal peptide. Cell fractionation studies using
antibodies against the 15 C-terminal residues indicated that NHE6
protein localized in the microsomal membranes of rat liver cells. All
of the NHE6 molecules in liver tissue possess an endoglycosidase
H-resistant sugar chain. These findings indicate that NHE6 protein is
targeted to the ER membrane via the N-terminal signal peptide and is
sorted to organelle membranes derived from the ER membrane.
The nucleotide sequence(s) reported in this paper has been
submitted to the DDBJ/GenBankTM/EMBL Data Bank with
accession number(s) AB074255 for NHE6.1.
NHE6 Protein Possesses a Signal Peptide Destined for Endoplasmic
Reticulum Membrane and Localizes in Secretory Organelles of the
Cell*
,§,
Department of Molecular Biology, Graduate
School of Medical Science, Kyushu University, 3-1-1 Maidashi,
Higashi-ku, Fukuoka 812-8582 and the ¶ Department of Molecular
Physiology, National Cardiovascular Center Research Institute,
Fujishiro-dai 5-7-1, Suita, Osaka 565-8565, Japan
*
This work was supported in part by grants-in-aid for
scientific research from the Ministry of Education, Science, Sports, and Culture of Japan (to M. S. and K. M.) and by grants from the Human Frontier Science Program and Core Research from Evolutional Science and Technology (to K. M.).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.
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