{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\n DYNLL2 is a highly conserved, small dynein light chain that functions as a versatile hub protein by reversibly binding short linear motifs present in a wide range of partner proteins. Through these interactions, DYNLL2 not only promotes dimerization and stabilizes the structure of its partners but also contributes to the organization and function of motor protein complexes. For instance, by binding to a specific site on the myosin Va heavy chain—whose effective engagement is controlled by alternative splicing elements—DYNLL2 acts as an adaptor that links myosin Va to its cargo and modulates the coiled‐coil conformation of the heavy chain, thereby potentially governing cargo transport dynamics in cells."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n In addition, within the dynein motor system the incorporation of DYNLL2 (in conjunction with its isoform DYNLL1) into larger complexes is critical for proper retrograde trafficking in cilia, underscoring its role in organizing the dynein‐2 complex."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "3"}]}, {"type": "t", "text": " Moreover, detailed kinetic and thermodynamic analyses have revealed that DYNLL2 binds target peptides with affinities in the micromolar to subnanomolar range, and that binding is finely tuned by residues both within and outside its conserved recognition motif."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "4"}]}, {"type": "t", "text": "\n "}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n In neuronal contexts, DYNLL2 plays additional regulatory roles. It participates in the formation and stabilization of multiprotein complexes at synapses by interacting with scaffold proteins, thereby enhancing NMDA receptor–mediated signaling."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "6"}]}, {"type": "t", "text": " DYNLL2 has also been implicated in modulating apoptosis by affecting the oligomerization and stability of pro‐apoptotic proteins such as Bim and Bmf"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "8"}]}, {"type": "t", "text": ", and it may furthermore contribute to the reorganization of postsynaptic protein complexes in response to sustained neuronal activity.\n "}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n The importance of DYNLL2 is not confined to neurons. In parasitic protozoa such as Neospora caninum, a homologous DYNLL2 has been characterized as a secreted factor that can modulate host immune responses"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "9"}]}, {"type": "t", "text": ", while recent bioinformatics‐driven studies have also identified alterations in DYNLL2 expression as a potential prognostic marker in osteosarcoma."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "10"}]}, {"type": "t", "text": " Finally, in the hypothalamus, DYNLL2 appears to participate in synaptic reorganization associated with NMDA receptor trafficking in oxytocin neurons, thereby linking its function to the regulation of feeding‐related neuronal circuits."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "11"}]}, {"type": "t", "text": "\n "}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n Collectively, these findings portray DYNLL2 as a multifaceted regulator that integrates motor function, cargo transport, and signal transduction across diverse cell types by orchestrating protein–protein interactions critical for subcellular organization and cellular homeostasis.\n "}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Wolfgang Wagner, Elfrieda Fodor, Ann Ginsburg, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The binding of DYNLL2 to myosin Va requires alternatively spliced exon B and stabilizes a portion of the myosin's coiled-coil domain."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochemistry (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1021/bi061142u"}], "href": "https://doi.org/10.1021/bi061142u"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16981716"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16981716"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Andrea Bodor, László Radnai, Csaba Hetényi, et al. "}, {"type": "b", "children": [{"type": "t", "text": "DYNLL2 dynein light chain binds to an extended linear motif of myosin 5a tail that has structural plasticity."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochemistry (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1021/bi500574z"}], "href": "https://doi.org/10.1021/bi500574z"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25312846"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25312846"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Yuta Tsurumi, Yuki Hamada, Yohei Katoh, et al. 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