PEST sequences in calmodulin-binding proteins

Junor A. Barnes, Aldrin V Gomes

Research output: Contribution to journalArticlepeer-review

54 Scopus citations


Many short-lived proteins which are devoid of proteolytic activity contain PEST sequences which are segments along the polypeptide chain that are rich in proline (P), glutamate (E), serine (S) and threonine (T). These designated PEST sequences are believed to be putative intramolecular signals for rapid proteolytic degradation. Calmodulin is a ubiquitous, 17kDa, acidic Ca2+-binding protein which plays an important role in the regulation of many physiological processes through its interaction with a wide range of calmodulin-binding proteins. Several calmodulin-binding proteins are known to contain PEST sequences and are susceptible to proteolysis by endogenous neutral proteases such as calpain I and calpain II. In this report, we discuss the functions of PEST sequences in calmodulin-binding proteins and assess the correlation between calmodulin-binding proteins and PEST sequences.

Original languageEnglish (US)
Pages (from-to)17-27
Number of pages11
JournalMolecular and Cellular Biochemistry
Issue number1
StatePublished - Aug 1995
Externally publishedYes


  • calmodulin-binding proteins
  • calpain
  • PEST sequences
  • ubiquitin

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics
  • Clinical Biochemistry
  • Cell Biology


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