Lei, KuiDavis, Roger J.2022-08-232022-08-232003-02-202009-04-02<p>Proc Natl Acad Sci U S A. 2003 Mar 4;100(5):2432-7. Epub 2003 Feb 18. <a href="http://dx.doi.org/10.1073/pnas.0438011100">Link to article on publisher's site</a></p>0027-8424 (Print)10.1073/pnas.043801110012591950https://hdl.handle.net/20.500.14038/38943The c-Jun NH(2)-terminal kinase (JNK) is activated when cells are exposed to environmental stress, including UV radiation. Gene disruption studies demonstrate that JNK is essential for UV-stimulated apoptosis mediated by the mitochondrial pathway by a Bax/Bak-dependent mechanism. Here, we demonstrate that JNK phosphorylates two members of the BH3-only subgroup of Bcl2-related proteins (Bim and Bmf) that are normally sequestered by binding to dynein and myosin V motor complexes. Phosphorylation by JNK causes release from the motor complexes. These proapoptotic BH3-only proteins therefore provide a molecular link between the JNK signal transduction pathway and the Bax/Bak-dependent mitochondrial apoptotic machinery.en-US*Adaptor Proteins, Signal Transducing*ApoptosisApoptosis Regulatory ProteinsCarrier ProteinsCell LineDNA Mutational AnalysisDNA, ComplementaryFibroblastsHumans*Membrane ProteinsMitochondriaModels, BiologicalNeuronsPhosphorylationPlasmidsProtein BindingProtein IsoformsProto-Oncogene ProteinsProto-Oncogene Proteins c-bcl-2Signal TransductionThreoninebcl-2-Associated X ProteinLife SciencesMedicine and Health SciencesJournal Articlehttps://escholarship.umassmed.edu/oapubs/1773808538oapubs/1773