RT Journal Article
SR Electronic
T1 Dynein-Independent Functions of DYNLL1/LC8: Redox State Sensing and Transcriptional Control
JF Science Signaling
JO Sci. Signal.
FD American Association for the Advancement of Science
SP pe51
OP pe51
DO 10.1126/scisignal.147pe51
VO 1
IS 47
A1 King, Stephen M.
YR 2008
UL http://stke.sciencemag.org/content/1/47/pe51.abstract
AB 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-κB.