一种细胞质蛋白丙酮酸激酶的糖基化、非糖基化和截短形式在细胞表面的表达。
Cell surface expression of glycosylated, nonglycosylated, and truncated forms of a cytoplasmic protein pyruvate kinase.
作者信息
Hiebert S W, Lamb R A
机构信息
Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, Illinois 60208.
出版信息
J Cell Biol. 1988 Sep;107(3):865-76. doi: 10.1083/jcb.107.3.865.
Abstract
The soluble cytoplasmic protein pyruvate kinase (PK) has been expressed at the cell surface in a membrane-anchored form (APK). The hybrid protein contains the NH2-terminal signal/anchor domain of a class II integral membrane protein (hemagglutinin/neuraminidase, of the paramyxovirus SV5) fused to the PK NH2 terminus. APK contains a cryptic site that is used for N-linked glycosylation but elimination of this site by site-specific mutagenesis does not prevent cell surface localization. Truncated forms of the APK molecule, with up to 80% of the PK region of APK removed, can also be expressed at the cell surface. These data suggest that neither the complete PK molecule nor its glycosylation are necessary for intracellular transport of PK to the cell surface, and it is possible that specific signals may not be needed in the ectodomain of this hybrid protein to specify cell surface localization.
摘要
可溶性细胞质蛋白丙酮酸激酶（PK）已以膜锚定形式（APK）在细胞表面表达。该杂合蛋白包含与PK氨基末端融合的II类整合膜蛋白（副粘病毒SV5的血凝素/神经氨酸酶）的氨基末端信号/锚定结构域。APK含有一个用于N-连接糖基化的隐蔽位点，但通过位点特异性诱变消除该位点并不妨碍其在细胞表面的定位。去除高达80%的APK的PK区域的APK分子截短形式也可在细胞表面表达。这些数据表明，完整的PK分子及其糖基化对于PK向细胞表面的细胞内运输都不是必需的，并且在这种杂合蛋白的胞外结构域中可能不需要特定信号来指定细胞表面定位。
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