ER export: More than one way out
نویسنده
چکیده
Protein export from the ER is mediated by COPII vesicles. Glycosylphosphatidylinositol-linked proteins seem to be segregated from other cargo proteins during ER export, suggesting that ER membranes produce more than one type of vesicle.
منابع مشابه
Seeking a way out: export of proteins from the plant endoplasmic reticulum.
The functionality of the secretory pathway relies on the efficient transfer of cargo molecules from their site of synthesis in the endoplasmic reticulum (ER) to successive compartments within the pathway. Although transport mechanisms of secretory proteins have been studied in detail in various non-plant systems, it is only recently that our knowledge of secretory routes in plants has expanded ...
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Export of many secretory proteins from the endoplasmic reticulum (ER) relies on signal-mediated sorting into ER-derived transport vesicles. Recent work on the coat protein complex II (COPII) provides new insight into the mechanisms and signals that govern this selective export process. Conserved di-acidic and di-hydrophobic motifs found in specific transmembrane cargo proteins are required for ...
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Protein sorting to plant vacuoles is known to be dependent on a considerable variety of protein motifs recognized by a family of sorting receptors. This can involve either traffic from the endoplasmic reticulum (ER) through the Golgi apparatus or direct ER-to-vacuole transport. Barley aspartic protease (Phytepsin) was shown previously to reach the vacuole via trafficking through the Golgi appar...
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December 2007 | Volume 5 | Issue 12 | e330 As far as molecular celebrity goes, messenger RNAs (mRNAs) no longer command the spotlight, especially compared with the smoking hot gene-regulating microRNAs or the Piwiinteracting RNAs, with their steamy role in spermatogenesis. As the intermediary between the gene blueprint and the protein end product, mRNAs certainly play a role of fundamental impo...
متن کاملRegulation of coat assembly--sorting things out at the ER.
The small GTPase Sar1 resides at the core of a regulatory cycle that controls protein export from the ER in COPII vesicles. Recent advances in minimally reconstituted systems indicate continual flux of Sar1 through GTPase cycles facilitates cargo concentration into forming vesicles that ultimately bud from membranes. During export from ER membranes, this GTPase cycle is harnessed through the co...
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ورودعنوان ژورنال:
- Current Biology
دوره 11 شماره
صفحات -
تاریخ انتشار 2001