Golgi complex–plasma membrane trafficking directed by an autonomous, tribasic Golgi export signal
| Autor: | FuiBoon Kai, Hirendrasinh B. Parmar, Christopher Barry, Roy Duncan |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2014 |
| Předmět: |
Endosome
Recombinant Fusion Proteins Amino Acid Motifs Molecular Sequence Data Golgi Apparatus Biology Protein Sorting Signals Endoplasmic Reticulum Reoviridae Quail 03 medical and health sciences symbols.namesake Viral Proteins Cell Line Tumor Chlorocebus aethiops Animals Molecular Biology Vero Cells Secretory pathway 030304 developmental biology 0303 health sciences 030302 biochemistry & molecular biology Cell Membrane Cell Biology Articles Golgi apparatus Cell biology Cytosol Protein Transport Membrane Gene Expression Regulation Membrane Trafficking symbols Signal Transduction |
| Zdroj: | Molecular Biology of the Cell |
| ISSN: | 1939-4586 1059-1524 |
| Popis: | The first example of a cytosolic, membrane-proximal, tribasic motif required for Golgi export to the plasma membrane is identified and characterized. This novel Golgi export signal can also mediate trafficking of a heterologous Golgi-resident protein, indicating that it functions as an autonomous Golgi export signal. Although numerous linear motifs that direct protein trafficking within cells have been identified, there are few examples of linear sorting signals mediating directed export of membrane proteins from the Golgi complex to the plasma membrane. The reovirus fusion-associated small transmembrane proteins are simple, single-pass transmembrane proteins that traffic through the endoplasmic reticulum–Golgi pathway to the plasma membrane, where they induce cell–cell membrane fusion. Here we show that a membrane-proximal, polybasic motif (PBM) in the cytosolic tail of p14 is essential for efficient export of p14 from the Golgi complex to the plasma membrane. Extensive mutagenic analysis reveals that the number, but not the identity or position, of basic residues present in the PBM dictates p14 export from the Golgi complex, with a minimum of three basic residues required for efficient Golgi export. Results further indicate that the tribasic motif does not affect plasma membrane retention of p14. Furthermore, introduction of the tribasic motif into a Golgi-localized, chimeric ERGIC-53 protein directs export from the Golgi complex to the plasma membrane. The p14 PBM is the first example of an autonomous, tribasic signal required for Golgi export to the plasma membrane. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|