2026/05/20 by Jakob Schneider, Undina Guillerm, Caroline Simões Pereira +2
Biochemistry, Genetics and Molecular Biology · #Mitochondrial Function and Pathology #Nuclear Structure and Function #Photosynthetic Processes and Mechanisms
paper · doi:10.1002/pro.70630
openalex publication_date 2026/05/20 · openalex created_date 2026/05/21 · openalex updated_date 2026/07/27
The import of proteins into mitochondria poses fundamental mechanistic challenges: aggregation-prone precursor proteins must be maintained in aqueous compartments and threaded through narrow pores without becoming stuck or mislocalized. Recent evidence from mitochondrial protein import studies and other chaperone systems underscores the critical role of dynamics in balancing sufficiently tight binding, promiscuity, specificity, and release. Dynamic binding of client precursor proteins to import machinery components arises naturally from the avidity of their interactions. Conformational entropy enhances their stability, while the multivalent nature of these interactions ensures that client transfer to downstream insertases occurs without a substantial energy barrier. Here, we discuss this emerging paradigm of dynamic protein handling, using examples where dynamic structures have been resolved and highlight outstanding questions.