Jip3 might supply a link between lysosomes and dynein through its interaction with DLIC. We demonstrated that direct interaction of Lonafarnib SCH66336 JNK and Jip3 was essential to prevent pJNK accumulation and the axon terminal swellings characteristic of the mutant but had no effect on lysosome accumulation. Furthermore, exogenous expression of activated JNK phenocopied the jip3nl7 mutant axon terminal swellings but didn’t cause lysosome accumulation, providing evidence that high levels of active JNK cause this phenotype in a lysosome independent manner. Eventually, our cotransport research suggested that Jip3 right caused lysosome connection with the dynein motor through binding for the accessory protein DLIC. Given the decline in frequency of cargo movement, the normal distribution of dynein components in jip3nl7 mutant axon terminals, and the high rate of Jip3 lysosome and Jip3 JNK3 denver transportation, we posit that Jip3 probably acts as an adapter protein that mediates attachment of these cargos for the dynein motor. Jip3 is implicated in anterograde axonal transport in several studies through its relationship with equally Kinesin light Carcinoid chain and Kinesin heavy chain components of the Kinesin 1 motor. We became involved specifically in Jip3s purpose in retrograde transport as jip3nl7 demonstrated the unusual quality of intense swellings in axon terminals, the end of the line for anterograde transport. A function for Jip3 in retrograde transport has certainly been posited by Cavalli et al. Because they demonstrated that Jip3 co localized with pJNK distal to nerve ligation and co purified from similar GW9508 clinical trial membrane fractions as dynein components, however, our study is the first to offer conclusive evidence that Jip3 is required for retrograde transport of pJNK, as pJNK accumulates in axon terminals in jip3nl7 mutants, Jip3 and JNK3 are co transported, and direct Jip3 JNK interaction is functionally required for pJNK retrograde transport. Ergo, our work determines pJNK as a Jip3 dependent retrograde cargo. Additionally, through the implementation of our in vivo imaging approach, we discovered that the frequency of retrograde JNK3 transport was reduced with loss of Jip3, but the processivity of the motor and velocity of motion were unchanged. This data, in combination with previous biochemical studies of Jip3 JNK and Jip3 dynein interaction, provide strong evidence that Jip3 functions as an adapter for pJNK, linking it towards the dynein complex for transport, without affecting motor movement itself. Utilizing a combination of immunolabeling and in vivo imaging techniques, we further show that Jip3 is necessary for retrograde transport of lysosomes through interaction with the dynein accessory protein DLIC. DLIC has been shown to be a crucial mediator of dynein based movement in culture systems and was shown to biochemically communicate with Jip3 in yet another system.