The Myotubularin Related Proteins and the Untapped Interaction Potential of Their Disordered C-Terminal Regions.

ABSTRACT: Intrinsically disordered regions (IDRs) of proteins remain understudied with enigmatic sequence features relevant to their functions. Members of the myotubularin-related protein (MTMR) family contain uncharacterized IDRs. After decades of research on their phosphatase activity, recent work on the C-terminal IDRs of MTMR7 revealed new interactions and important new functions beyond the phosphatase function. Here we take a broader look at the C-terminal domains (CTDs) of 14 human MTMRs and use bioinformatic tools and biophysical methods to ask which other functions may be probable in this protein family. The predictions show that the CTDs are disordered and carry short linear motifs (SLiMs) important for targeting of MTMRs to defined subcellular compartments and implicating them in signaling

SUBMITTER: Saar D 

PROVIDER: S-EPMC11878207 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature