PEST sequences in calmodulin-binding proteins
Monography
em En
| MedCarib
| ID: med-16674
Biblioteca responsável:
TT5
Localização: TT5; QP 517 C45 I575 1994
ABSTRACT
Many short-lived proteins which are devoid of proteolytic activity contain PEST sequences which are segments along 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-building 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 (AU)
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Coleções:
01-internacional
Base de dados:
MedCarib
Assunto principal:
Serina
/
Treonina
/
Proteínas de Ligação a Calmodulina
/
Prolina
/
Calpaína
/
Ácido Glutâmico
/
Ubiquitina
Limite:
Animals
/
Humans
Idioma:
En
Tipo de documento:
Congress and conference
/
Monography