CARP/Ankrd1 Interacting Proteins in mouse heart
Ontology highlight
ABSTRACT:
INSTRUMENT(S): QSTAR
ORGANISM(S): Mus Musculus (mouse)
TISSUE(S): Heart, Cardiac Muscle Cell
SUBMITTER: 
Stephan Lange
LAB HEAD: Stephan Lange
PROVIDER: PXD017426 | Pride | 2022-05-19
REPOSITORIES: Pride
Publications
Molecular Characterisation of Titin N2A and Its Binding of CARP Reveals a Titin/Actin Cross-linking Mechanism.
Zhou Tiankun T Fleming Jennifer R JR Lange Stephan S Hessel Anthony L AL Bogomolovas Julius J Stronczek Chiara C Grundei David D Ghassemian Majid M Biju Andrea A Börgeson Emma E Bullard Belinda B Linke Wolfgang A WA Chen Ju J Kovermann Michael M Mayans Olga O
Journal of molecular biology 20210227 9
Striated muscle responds to mechanical overload by rapidly up-regulating the expression of the cardiac ankyrin repeat protein, CARP, which then targets the sarcomere by binding to titin N2A in the I-band region. To date, the role of this interaction in the stress response of muscle remains poorly understood. Here, we characterise the molecular structure of the CARP-receptor site in titin (UN2A) and its binding of CARP. We find that titin UN2A contains a central three-helix bundle fold (ca 45 res ...[more]
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