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Sci. Signal., 25 November 2008
Vol. 1, Issue 47, p. pe51
[DOI: 10.1126/scisignal.147pe51]


Dynein-Independent Functions of DYNLL1/LC8: Redox State Sensing and Transcriptional Control

Stephen M. King*

Department of Molecular, Microbial and Structural Biology, University of Connecticut Health Center, 263 Farmington Avenue, Farmington, CT 06030–3305, USA.

Abstract: The highly conserved DYNLL/LC8 proteins promote dimerization of a broad range of targets and are essential for the integrity, activity, or both, of many subcellular systems, such as dyneins, myosin V, and apoptotic factors. Defects in DYNLL/LC8 function lead to severe cellular and developmental phenotypes in multicellular organisms, whereas loss-of-function alleles are lethal. DYNLL/LC8 dimer formation may be controlled by various signaling inputs (including pH changes and phosphorylation), and dimerization has been linked to alterations in the enzymatic activity of neuronal nitric oxide synthase and apoptotic control. A recent report now proposes that DYNLL/LC8-driven interactions are also regulated by changes in cellular redox state, which lead to intermonomer disulfide bond formation and ultimately activation of the transcription factor NF-{kappa}B.

* Telephone, 860-679-3347; fax, 860-679-3408; e-mail, king{at}

Citation: S. M. King, Dynein-Independent Functions of DYNLL1/LC8: Redox State Sensing and Transcriptional Control. Sci. Signal. 1, pe51 (2008).

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