DYNLL1, also known as dynein light chain 1, is a protein that has been implicated in a variety of cellular processes, including DNA repair mechanisms. It is known to interact with the MRE11 protein, which is a component of the MRN complex that plays a key role in the initial steps of DNA double-strand break (DSB) repair. DYNLL1 is recruited to DSBs by 53BP1, where it modulates the extent of DNA end resection by binding to and destabilizing the MRE11 dimer. This interaction is crucial for the regulation of DNA repair pathway choice, particularly in the context of BRCA1-deficient cells, where it limits DNA end resection and thus influences homologous recombination. Furthermore, DYNLL1 has been identified as a component of the Shieldin complex, which is involved in the protection of DNA ends during replication stress and is implicated in the recruitment process of this complex to DSBs. In terms of its biological functions, DYNLL1 is essential for development and has been shown to promote endochondral bone formation by regulating intraflagellar dynein function in primary cilia. It is also involved in the regulation of the dynein motor complex, which is important for ciliary function and associated with ciliopathies, a group of disorders that affect the structure and function of cilia.
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