The transmembrane segment of the human Na,K-ATPase beta-subunit acts as the membrane incorporation signal.
The human Na,K-ATPase beta-subunit is anchored to the membrane by a single stretch of 28 hydrophobic amino acids; the hydrophilic amino terminus faces the cytoplasm and the carboxyl terminus is exoplasmic. Glycosylation and insertion of the Na,K-ATPase beta-subunit into the endoplasmic reticulum membrane are shown to be co-translational and SRP-dependent. The hydrophilic amino terminus is not required for the membrane insertion. The membrane-anchor domain is necessary for membrane insertion, and a 16 amino acid stretch has been identified as an element sufficient for the insertion.
Kawakami
K
K
Department of Biology, Jichi Medical School, Tochigi.
Nagano
K
K
D004262:DNA Restriction Enzymes; D004721:Endoplasmic Reticulum / Q000201:enzymology*; D006031:Glycosylation; D006801:Humans; D046911:Macromolecular Substances; D010957:Plasmids; D014176:Protein Biosynthesis; D011499:Protein Processing, Post-Translational; D012156:Reticulocytes / Q000378:metabolism; D000254:Sodium-Potassium-Exchanging ATPase / Q000235:genetics* / Q000378:metabolism; D014158:Transcription, Genetic
D046911:Macromolecular Substances; D004262:DNA Restriction Enzymes; D000254:Sodium-Potassium-Exchanging ATPase