Journal
FEBS JOURNAL
Volume 278, Issue 17, Pages 2980-2996Publisher
WILEY
DOI: 10.1111/j.1742-4658.2011.08254.x
Keywords
dynein; hub protein; intracellular transport; linear motif; protein-protein interactions
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Funding
- Hungarian Scientific Research Fund (OTKA) [K81784, NK81950, K68408]
- European Union
- European Social Fund (TAMOP) [4.2.1./B-09/KMR-2010-0003]
- Janos Bolyai Research Fellowship
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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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