PEST sequence
A PEST sequence is a peptide sequence that is rich in proline (P), glutamic acid (E), serine (S), and threonine (T). This sequence is associated with proteins that have a short intracellular half-life; therefore, it is hypothesized that the PEST sequence acts as a signal peptide for protein degradation.[1]
This protein degradation may be mediated via the proteasome[2][3] or calpain.[4]
Other signals thought to identify proteins for degradation include cyclin destruction boxes, which are amino acid sequences that mark cell-cycle proteins for destruction.
References
- ^ Rogers S, Wells R, Rechsteiner M (1986). "Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis". Science. 234 (4774): 364–8. Bibcode:1986Sci...234..364R. doi:10.1126/science.2876518. PMID 2876518.
- ^ Reverte CG, Ahearn MD, Hake LE (2001). "CPEB degradation during Xenopus oocyte maturation requires a PEST domain and the 26S proteasome". Dev. Biol. 231 (2): 447–58. doi:10.1006/dbio.2001.0153. PMID 11237472.
- ^ Spencer ML, Theodosiou M, Noonan DJ (2004). "NPDC-1, a novel regulator of neuronal proliferation, is degraded by the ubiquitin/proteasome system through a PEST degradation motif". J. Biol. Chem. 279 (35): 37069–78. doi:10.1074/jbc.M402507200. PMID 15229225.
- ^ Shumway SD, Maki M, Miyamoto S (1999). "The PEST Domain of IκBα is necessary and sufficient for in vitro degradation by mu-calpain". J. Biol. Chem. 274 (43): 30874–81. doi:10.1074/jbc.274.43.30874. PMID 10521480.
 | This molecular or cell biology article is a stub. You can help Wikipedia by expanding it. |