Mortalin's machinery
College
College of Science
Department/Unit
Biology
Document Type
Book Review
Source Title
Mortalin Biology: Life, Stress and Death
First Page
21
Last Page
30
Publication Date
2012
Place of Publication
Dordrecht
Publisher
Springer
Abstract
Mortalin/mtHsp70 performs a wide array of cellular functions and has been implicated in aging, cancer and neurodegenerative diseases. Similar to other Hsp70s, its ability to chaperone misfolded proteins and bind to a myriad of clients is derived from its N-terminal nucleotide-binding domain (NBD) regulating substrate affinity of the C-terminal substrate-binding domain (SBD) in a nucleotide- and co-chaperone-dependent mechanism. To understand the structural dynamics of its allostery making this relevant to mortalin’s cellular function, this chapter describes key structural features of these two domains as well as provide an appreciation as to possibly how a single amino acid change, Gly to Arg in the SBD that can be viewed so minor, is able to metamorphose from a life-extending species of mortalin (mot-2) into one that induces senescence and even inhibits tumor growth (mot-1).
html
Recommended Citation
Deocaris, C. C., Kaul, S. C., & Wadhwa, R. (2012). Mortalin's machinery. Mortalin Biology: Life, Stress and Death, 21-30. Retrieved from https://animorepository.dlsu.edu.ph/faculty_research/5457
Disciplines
Cancer Biology
Keywords
Tumor suppressor proteins; Molecular chaperones; Protein binding
Upload File
wf_no
