DYNLL2 is a small protein, consisting of 89 amino acids, and shares a high degree of similarity with its paralog, DYNLL1 . It acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex. This complex functions as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules .
The primary role of DYNLL2 is to link dynein to its cargo and adapter proteins, thereby regulating dynein function. It is involved in various cellular pathways, including mitotic spindle formation and transport to the Golgi apparatus .
DYNLL2 plays a crucial role in maintaining the spatial distribution of cytoskeletal structures. It is predicted to enable dynein intermediate chain binding activity and dynein light intermediate chain binding activity . Additionally, it is involved in cilium assembly and is active in glutamatergic synapses and postsynapses .
Recombinant DYNLL2 is produced using recombinant DNA technology, which involves cloning the DYNLL2 gene into an expression vector, transforming it into a suitable host cell (such as E. coli), and purifying the expressed protein. This recombinant protein is used in various research applications to study its function and interactions with other proteins.
Research on DYNLL2 has provided insights into its role in mitochondrial mobility within axons. For instance, studies have shown that DYNLL2 regulates syntaphilin-mediated mitochondrial docking in axons by binding to syntaphilin, thus enhancing the syntaphilin-microtubule docking interaction . This interaction is crucial for proper transport and distribution of mitochondria within neurons, which is essential for neuronal function .