PEST sequence

A PEST sequence is a peptide sequence which 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; hence, it is hypothesized that the PEST sequence acts as a signal peptide for protein degradation.^[1]

The degradation may be mediated possibly via the proteosome^[2]^[3] or calpain^[4].

References

^ Rogers S, Wells R, Rechsteiner M (1986). "Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis". Science. 234 (4774): 364–8. doi:10.1126/science.2876518. PMID 2876518.{{cite journal}}: CS1 maint: multiple names: authors list (link)
^ 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.{{cite journal}}: CS1 maint: multiple names: authors list (link)
^ 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.{{cite journal}}: CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link)
^ Shumway SD, Maki M, Miyamoto S (1999). "The PEST domain of IkappaBalpha 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.{{cite journal}}: CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link)

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