Open AccessCalmodulin binds the N-terminus of the functional amyloid Orb2A inhibiting fibril formation
Author(s) -
Maria A. Soria,
Silvia A. Cervantes,
Ansgar B. Siemer
Publication year - 2022
Publication title -
plos one
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 332
ISSN - 1932-6203
DOI - 10.1371/journal.pone.0259872
Subject(s) - fibril , calmodulin , n terminus , chemistry , c terminus , biochemistry , biophysics , cytoplasm , gene isoform , microbiology and biotechnology , amyloid (mycology) , peptide sequence , biology , amino acid , inorganic chemistry , gene , enzyme
The cytoplasmic polyadenylation element-binding protein Orb2 is a key regulator of long-term memory (LTM) in Drosophila . The N-terminus of the Orb2 isoform A is required for LTM and forms cross-β fibrils on its own. However, this N-terminus is not part of the core found in ex vivo fibrils. We previously showed that besides forming cross-β fibrils, the N-terminus of Orb2A binds anionic lipid membranes as an amphipathic helix. Here, we show that the Orb2A N-terminus can similarly interact with calcium activated calmodulin (CaM) and that this interaction prevents fibril formation. Because CaM is a known regulator of LTM, this interaction could potentially explain the regulatory role of Orb2A in LTM.