| Literature DB >> 21777386 |
Péter Rapali1, Áron Szenes, László Radnai, Anita Bakos, Gábor Pál, László Nyitray.
Abstract
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.Entities:
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Year: 2011 PMID: 21777386 DOI: 10.1111/j.1742-4658.2011.08254.x
Source DB: PubMed Journal: FEBS J ISSN: 1742-464X Impact factor: 5.542