Nilsson T, Hoe M H, Slusarewicz P, Rabouille C, Watson R, Hunte F, Watzele G, Berger E G, Warren G
Cell Biology Laboratory, Imperial Cancer Research Fund, London, UK.
EMBO J. 1994 Feb 1;13(3):562-74. doi: 10.1002/j.1460-2075.1994.tb06294.x.
The medial Golgi enzymes, N-acetylglucosaminyltransferase I (NAGT I) and mannosidase II (Mann II), and the trans Golgi enzyme, beta-1,4-galactosyltransferase (GalT) were each retained in the endoplasmic reticulum (ER) by grafting on the cytoplasmic tail of the p33 invariant chain. Transient and stable expression of p33/NAGT I in HeLa cells caused relocation of endogenous Mann II to the ER and transient expression of p33/Mann II had a similar effect on endogenous NAGT I. Neither of these endogenous medial enzymes were affected by transient expression of p33/GalT. These data provide strong evidence for kin recognition between medial Golgi enzymes and suggest a role for them in the organization of the Golgi stack.
内侧高尔基体酶N-乙酰葡糖胺基转移酶I（NAGT I）和甘露糖苷酶II（Mann II），以及反式高尔基体酶β-1,4-半乳糖基转移酶（GalT），通过嫁接到p33恒定链的细胞质尾部，各自保留在内质网（ER）中。HeLa细胞中p33/NAGT I的瞬时和稳定表达导致内源性Mann II重新定位到内质网，p33/Mann II的瞬时表达对内源性NAGT I有类似影响。这两种内源性内侧酶均不受p33/GalT瞬时表达的影响。这些数据为内侧高尔基体酶之间的亲属识别提供了有力证据，并表明它们在高尔基体堆叠的组织中发挥作用。
