Structural insights into the activation mechanisms of human HtrA serine proteases
Dorota Żurawa-Janicka , Tomasz Wenta , Mirosław Jarząb , Joanna Skórko-Glonek , Przemysław Glaza , Artur Giełdoń , Jerzy Ciarkowski , Barbara Lipińska
AbstractHuman HtrA1-4 proteins belong to the HtrA family of evolutionarily conserved serine proteases and function as important modulators of many physiological processes, including maintenance of mitochondrial homeostasis, cell signaling and apoptosis. Disturbances in their action are linked to severe diseases, including oncogenesis and neurodegeneration. The HtrA1-4 proteins share structural and functional features of other members of the HtrA protein family, however there are several significant differences in structural architecture and mechanisms of action which makes each of them unique. Our goal is to present recent studies regarding human HtrAs. We focus on their physiological functions, structure and regulation, and describe current models of activation mechanisms. Knowledge of molecular basis of the human HtrAs' action is a subject of great interest; it is crucial for understanding their relevance in cellular physiology and pathogenesis as well as for using them as targets in future therapies of diseases such as neurodegenerative disorders and cancer.
|Journal series||Archives of Biochemistry and Biophysics, ISSN 0003-9861, (A 30 pkt)|
|Publication size in sheets||0.85|
|Keywords in English||HtrA proteins, serine proteases, allosteric regulation, PDZ domain|
|Score|| = 30.0, 20-12-2017, ArticleFromJournal|
= 30.0, 20-12-2017, ArticleFromJournal
|Publication indicators||: 2016 = 3.165 (2) - 2016=2.974 (5)|
* presented citation count is obtained through Internet information analysis and it is close to the number calculated by the Publish or Perish system.