Nuclear export signal: Difference between revisions
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Nuclear export first begins with the binding of Ran-GTP (a [[G-protein]]) to exportin. This causes a shape change in [[exportin]], increasing its affinity for the export cargo. Once the cargo is bound, the Ran-exportin-cargo complex moves out of the nucleus through the nuclear pore. [[GTPase activating protein]]s (GAPs) then hydrolyze the Ran-GTP to Ran-GDP, and this causes a shape change and subsequent exportin release. Once no longer bound to Ran, the exportin molecule loses affinity for the nuclear cargo as well, and the complex falls apart. Exportin and Ran-GDP are recycled to the nucleus separately, and [[guanine exchange factor]] (GEF) in the nucleus switches the GDP for GTP on Ran. |
Nuclear export first begins with the binding of Ran-GTP (a [[G-protein]]) to exportin. This causes a shape change in [[exportin]], increasing its affinity for the export cargo. Once the cargo is bound, the Ran-exportin-cargo complex moves out of the nucleus through the nuclear pore. [[GTPase activating protein]]s (GAPs) then hydrolyze the Ran-GTP to Ran-GDP, and this causes a shape change and subsequent exportin release. Once no longer bound to Ran, the exportin molecule loses affinity for the nuclear cargo as well, and the complex falls apart. Exportin and Ran-GDP are recycled to the nucleus separately, and [[guanine exchange factor]] (GEF) in the nucleus switches the GDP for GTP on Ran. |
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==NESbase== |
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NESbase is a database of proteins, experimentally authenticated Leucine-rich Nuclear Export Signals (NES). A research was conducted by Center for Biological Sequence Analysis, Technical University of Denmark; and Department of Protein Chemistry, University of Copenhagen to validate NESbase version 1.0. Every entry in its database includes information whether Nuclear Export Signals was sufficient for export or it was only mediated transport by CRM1, the export receptor.<ref>{{cite journal |author=Tanja la Cour, Ramneek Gupta1, Kristoffer Rapacki, Karen Skriver, Flemming M. Poulsen, Søren Brunak |title=NESbase version 1.0: a database of nuclear export signals |journal=Nucleic acids research |volume=31 |issue=1 |pages=393–396 |year=2003 |month= |pmid=12520031 |doi=10.1093/nar/gkg101 |url=http://orbit.dtu.dk/en/publications/nesbase-version-10-a-database-of-nuclear-export-signals%281d9439b8-17a4-489c-9820-3f685a0b928c%29.html}}</ref> |
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==References== |
==References== |
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Revision as of 05:08, 21 August 2013
 | This article may be confusing or unclear to readers. (December 2007) |
A nuclear export signal (NES) is a short amino acid sequence of 4 hydrophobic residues in a protein that targets it for export from the cell nucleus to the cytoplasm through the nuclear pore complex using nuclear transport. It has the opposite effect of a nuclear localization signal, which targets a protein located in the cytoplasm for import to the nucleus. The NES is recognized and bound by exportins. In silico analysis of known NESs found the most common spacing of the hydrophobic residues to be LxxxLxxLxL, where "L" is a hydrophobic residue (often leucine) and "x" is any other amino acid; the spacing of these hydrophobic residues may be explained by examination of known structures that contain an NES, as the critical residues usually lie in the same face of adjacent secondary structures within a protein, which allows them to interact with the exportin.[1] Ribonucleic acid (RNA) are composed of nucleotides, and thus, lack the nuclear export signal to move out of the nucleus. As a result, most forms of RNA will bind to a protein molecule to form a ribonucleoprotein complex to be exported from the nucleus.
Nuclear export first begins with the binding of Ran-GTP (a G-protein) to exportin. This causes a shape change in exportin, increasing its affinity for the export cargo. Once the cargo is bound, the Ran-exportin-cargo complex moves out of the nucleus through the nuclear pore. GTPase activating proteins (GAPs) then hydrolyze the Ran-GTP to Ran-GDP, and this causes a shape change and subsequent exportin release. Once no longer bound to Ran, the exportin molecule loses affinity for the nuclear cargo as well, and the complex falls apart. Exportin and Ran-GDP are recycled to the nucleus separately, and guanine exchange factor (GEF) in the nucleus switches the GDP for GTP on Ran.
NESbase
NESbase is a database of proteins, experimentally authenticated Leucine-rich Nuclear Export Signals (NES). A research was conducted by Center for Biological Sequence Analysis, Technical University of Denmark; and Department of Protein Chemistry, University of Copenhagen to validate NESbase version 1.0. Every entry in its database includes information whether Nuclear Export Signals was sufficient for export or it was only mediated transport by CRM1, the export receptor.[2]
References
- ^ la Cour T, Kiemer L, Mølgaard A, Gupta R, Skriver K, Brunak S (2004). "Analysis and prediction of leucine-rich nuclear export signals". Protein Eng. Des. Sel. 17 (6): 527–36. doi:10.1093/protein/gzh062. PMID 15314210.
{{cite journal}}: Unknown parameter|month=ignored (help)CS1 maint: multiple names: authors list (link) - ^ Tanja la Cour, Ramneek Gupta1, Kristoffer Rapacki, Karen Skriver, Flemming M. Poulsen, Søren Brunak (2003). "NESbase version 1.0: a database of nuclear export signals". Nucleic acids research. 31 (1): 393–396. doi:10.1093/nar/gkg101. PMID 12520031.
{{cite journal}}: Cite has empty unknown parameter:|month=(help)CS1 maint: multiple names: authors list (link) CS1 maint: numeric names: authors list (link)
External links
Eukaryotic Linear Motif resource motif class TRG_NES_CRM1_1
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