Dynein light chain LC8 is a dimerization hub essential in diverse protein networks.
The operations within a living cell depend on the collective activity of networks of proteins, sometimes termed "interactomes". Within these networks, most proteins interact with few partners, while a small proportion of proteins, called hubs, participate in a large number of interactions and play a central role in organizing these interactomes. LC8 was first discovered as an essential component of the microtubule-based molecular motor dynein and as such is involved in fundamental processes, including retrograde vesicular trafficking, ciliary/flagellar motility, and cell division. More recently, evidence has accumulated that LC8 also interacts with proteins that are not clearly connected with dynein or microtubule-based transport, including some with roles in apoptosis, viral pathogenesis, enzyme regulation, and kidney development. Here, we introduce the idea that LC8 is a hub protein essential in diverse protein networks, and its function as a dynein light chain is but one of many. We further propose that the crucial regulatory roles of LC8 in various systems are due to its ability to promote dimerization of partially disordered proteins.
Barbar
Elisar
E
Department of Biochemistry and Biophysics, Oregon State University, Corvallis, Oregon 97331, USA. barbare@science.oregonstate.edu
D048868:Adaptor Proteins, Signal Transducing / Q000737:chemistry / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D019281:Dimerization; D004398:Dyneins / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D011485:Protein Binding
D048868:Adaptor Proteins, Signal Transducing; D004398:Dyneins