Key result
LC8 light chains function as regulatory hub proteins that promote dimerization of their binding partners by interacting with short linear motifs in intrinsically disordered protein segments.
This review highlights the structural and functional aspects of LC8 light chains as regulatory hub proteins rather than just cargo adapters.
Supports LC8 reclassification as hubs; leaves open validation in disease models.
The LC8 family members of dynein light chains (DYNLL1 and DYNLL2 in vertebrates) are highly conserved ubiquitous eukaryotic homodimer proteins that interact, besides dynein and myosin 5a motor proteins, with a large (and still incomplete) number of proteins involved in diverse biological functions. Despite an earlier suggestion that LC8 light chains function as cargo adapters of the above molecular motors, they are now recognized as regulatory hub proteins that interact with short linear motifs located in intrinsically disordered protein segments. The most prominent LC8 function is to promote dimerization of their binding partners that are often scaffold proteins of various complexes, including the intermediate chains of the dynein motor complex. Structural and functional aspects of this intriguing hub protein will be highlighted in this minireview.
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Rapali et al. (2011) reported a review. DYNLL/LC8 was evaluated. LC8 light chains function as regulatory hub proteins that promote dimerization of their binding partners by interacting with short linear motifs in intrinsically disordered protein segments.
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