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DYNLL/LC8: a light chain subunit of the dynein motor complex and beyond
Author(s) -
Rapali Péter,
Szenes Áron,
Radnai László,
Bakos Anita,
Pál Gábor,
Nyitray László
Publication year - 2011
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2011.08254.x
Subject(s) - dynein , immunoglobulin light chain , motor protein , protein subunit , molecular motor , myosin , dynactin , function (biology) , heavy chain , microbiology and biotechnology , biology , kinesin , computational biology , chemistry , biophysics , genetics , microtubule , gene , antibody
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.