真核微生物的蛋白质合成与分泌资料.pptVIP

Representation of N-glycosylation events in the ER (upper part) and the Golgi (lower part). The ER events also include a simplified version of the quality control cycle. After partial deglucosylation of protein-bound N-glycans by glucosidases I and II, the unfolded protein interacts with the membrane-bound lectin chaperone calnexin (there is no calreticulin in yeast and fungal systems) via its monoglucosylated structures. Upon final deglucosylation via glucosidase II, the glycoprotein is released from calnexin. If incompletely folded, its N-glycans are reglucosylated by UGGT so that the underlying glycoprotein can interact again with the lectin chaperone. Note that there is no UGGT in S. cerevisiae, but orthologues of the S. pombe protein were identified in the aspergilli. If the protein fails to fold after several rounds of de- and reglucosylation, its N-glycans will eventually be trimmed by ER-resident a-1,2-mannosidases (e.g. Mns1p in S. cerevisiae or its orthologues in the aspergilli). ER-localized lectin-like proteins recognizing these trimmed N-glycans (e.g. Hml1p/Mnl1p in S. cerevisae or its orthologues in the aspergilli) and target these unfolded proteins for ERAD. In contrast, when a glycoprotein is completely folded, it will not undergo reglucosylation by UGGT. After trimming of the high-mannose N-glycans by ER-resident a-1,2-mannosidases, the glycoprotein migrates to the Golgi apparatus via vesicular transport. In most yeast species, the N-glycans—upon entry into the Golgi—predominantly have the Man8GlcNAc2 (isomer B) structure. In S. cerevisiae, this structure can be further modified as represented in the lower part of the figure. Underlined are the names of the proteins involved in Nglycosylation and quality control. 3）由高尔基体到细胞外的分泌最终是如何发生的？ 1) 提出了两种模型：小泡穿梭和潴泡推进。但这两种模型都有待实验的验证。 小泡穿梭的问题是鉴定不到特异的受体和小泡外被蛋白。 潴泡推进模型认为新潴泡产生在顺面膜囊，旧潴泡在反面囊膜破裂。有一些实验现象的支持，但如何解释不同潴泡所含的蛋白不同是一个难题。 到底如何运输？ Thanks ! 人有了知识，就会具备各种分析能力， 明辨是非的能力。 所以我们要勤恳读书，广泛阅读， 古人说“书中自有黄金屋。 ”通过阅读科技书籍，我们能丰富知