Ontology highlight
ABSTRACT:
SUBMITTER: Meister-Broekema M
PROVIDER: S-EPMC6297355 | biostudies-literature | 2018 Dec
REPOSITORIES: biostudies-literature
Meister-Broekema Melanie M Freilich Rebecca R Jagadeesan Chandhuru C Rauch Jennifer N JN Bengoechea Rocio R Motley William W WW Kuiper E F Elsiena EFE Minoia Melania M Furtado Gabriel V GV van Waarde Maria A W H MAWH Bird Shawn J SJ Rebelo Adriana A Zuchner Stephan S Pytel Peter P Scherer Steven S SS Morelli Federica F FF Carra Serena S Weihl Conrad C CC Bergink Steven S Gestwicki Jason E JE Kampinga Harm H HH
Nature communications 20181217 1
BAG3 is a multi-domain hub that connects two classes of chaperones, small heat shock proteins (sHSPs) via two isoleucine-proline-valine (IPV) motifs and Hsp70 via a BAG domain. Mutations in either the IPV or BAG domain of BAG3 cause a dominant form of myopathy, characterized by protein aggregation in both skeletal and cardiac muscle tissues. Surprisingly, for both disease mutants, impaired chaperone binding is not sufficient to explain disease phenotypes. Recombinant mutants are correctly folded ...[more]