Hydrogen/Deuterium Exchange Mass Spectrometry Provides Insights into the Role of Drosophila Testis-Specific Myosin VI Light Chain AndroCaM.

ABSTRACT: In Drosophila testis, myosin VI plays a special role, distinct from its motor function, by anchoring components to the unusual actin-based structures (cones) that are required for spermatid individualization. For this, the two calmodulin (CaM) light-chain molecules of myosin VI are replaced by androcam (ACaM), a related protein with 67% identity to CaM. Although ACaM has a similar bi-lobed structure to CaM, with two EF hand-type Ca²⁺ binding sites per lobe, only one functional Ca²⁺ binding site operates in the amino-terminus. To understand this light chain substitution, we used hydrogen-deuterium exchange mass spectrometry (HDX-MS) to examine dynamic changes in ACaM and CaM upon Ca²⁺ binding and interaction with the two CaM binding motifs of myosin VI (inse

SUBMITTER: Li J 

PROVIDER: S-EPMC10932932 | biostudies-literature | 2024 Mar

REPOSITORIES: biostudies-literature