PEST sequence

In this article, we will thoroughly explore the topic of PEST sequence and analyze its impact on different aspects of society. From its origin to its current evolution, PEST sequence has been the subject of debate and fascination for experts and fans alike. Throughout history, PEST sequence has played a crucial role in forming opinions, making decisions, and shaping various situations. Through a comprehensive analysis, we will attempt to shed light on the complexities of PEST sequence and examine its influence in diverse contexts, from the personal to the global level. We hope that this article provides an enriching and stimulating perspective on PEST sequence, inviting readers to reflect and delve deeper into this fascinating topic.

Peptide sequence in short-lived proteins

A PEST sequence is a peptide sequence that is rich in proline (P), glutamic acid (E), serine (S) and threonine (T). It is associated with proteins that have a short intracellular half-life, so might act as a signal peptide for protein degradation. This may be mediated via the proteasome or calpain.

References

1. ^ 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.
2. ^ 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.
3. ^ 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.
4. ^ 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.

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