Abstract
Resident integral proteins of the inner nuclear membrane (INM) are synthesized as membrane-integrated proteins on the peripheral endoplasmic reticulum (ER) and are transported to the INM throughout interphase using an unknown trafficking mechanism. To study this transport, we developed a live cell assay that measures the movement of transmembrane reporters from the ER to the INM by rapamycin-mediated trapping at the nuclear lamina. Reporter constructs with small (
| Original language | English |
|---|---|
| Pages (from-to) | 1051-62 |
| Number of pages | 12 |
| Journal | Journal of Cell Biology |
| Volume | 167 |
| Issue number | 6 |
| DOIs | |
| Publication status | Published - 2004 |
Keywords / Materials (for Non-textual outputs)
- Adenosine Triphosphate
- Endoplasmic Reticulum
- Energy Metabolism
- HeLa Cells
- Humans
- Membrane Proteins
- Nuclear Lamina
- Nuclear Pore
- Nuclear Pore Complex Proteins
- Nuclear Proteins
- Protein Transport
- Sirolimus
- Temperature
- Time Factors
Fingerprint
Dive into the research topics of 'Energy- and temperature-dependent transport of integral proteins to the inner nuclear membrane via the nuclear pore'. Together they form a unique fingerprint.Cite this
- APA
- Author
- BIBTEX
- Harvard
- Standard
- RIS
- Vancouver