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PEST sequences in calmodulin-binding proteins

  • Chapter
Signal Transduction Mechanisms

Part of the book series: Developments in Molecular and Cellular Biochemistry ((DMCB,volume 15))

Abstract

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, 17 kDa, 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.

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Authors and Affiliations

  1. Department of Biochemistry, Faculty of Medical Sciences, The University of The West Indies, St. Augustine, Trinidad and Tobago, West Indies, Caribbean

    Junor A. Barnes & Aldrin V. Gomes

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  1. Junor A. Barnes
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  1. Department of Biochemistry, University of West Indies, St. Augustine, Trinidad, West Indies, Caribbean

    Junor A. Barnes  & Haldane G. Coore  & 

  2. Department of Geriatric Medicine, Karolinska Institute, Stockholm, Sweden

    Abdul H. Mohammed

  3. Department of Pathology College of Medicine Saskatoon Cancer Center, University of Saskatoon, Saskatoon, Saskatchewan, Canada

    Rajendra K. Sharma

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Barnes, J.A., Gomes, A.V. (1995). PEST sequences in calmodulin-binding proteins. In: Barnes, J.A., Coore, H.G., Mohammed, A.H., Sharma, R.K. (eds) Signal Transduction Mechanisms. Developments in Molecular and Cellular Biochemistry, vol 15. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2015-3_2

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  • DOI: https://doi.org/10.1007/978-1-4615-2015-3_2

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