Jip3 could give a link between lysosomes and dynein through its interaction with DLIC. We demonstrated that direct interaction of Imatinib price JNK and Jip3 was necessary to prevent pJNK accumulation and the axon terminal swellings characteristic of the jip3nl7 mutant but had no influence on accumulation. Also, exogenous expression of activated JNK phenocopied the jip3nl7 mutant axon final swellings but did not cause lysosome accumulation, giving evidence that high degrees of active JNK cause this phenotype in a lysosome independent manner. Eventually, our cotransport research suggested that Jip3 right assisted lysosome relationship with the dynein motor through binding for the accessory protein DLIC. Given the decrease in frequency of cargo movement, the normal distribution of dynein elements in jip3nl7 mutant axon terminals, and the higher rate of Jip3 lysosome and Jip3 JNK3 co move, we posit that Jip3 probably serves as an adapter protein that mediates attachment of those cargos for the dynein motor. Jip3 has been implicated in anterograde axonal transport in several studies through its relationship with equally Kinesin light Endosymbiotic theory chain and Kinesin heavy chain aspects of the Kinesin 1 motor. We became interested specifically in purpose in retrograde transport as jip3nl7 demonstrated the strange quality of intense swellings in axon terminals, the end-of the line for anterograde transport. A function for Jip3 in retrograde transport has indeed been posited by Cavalli et al. as they demonstrated that Jip3 co localized with pJNK distal to nerve ligation and co purified from similar Erlotinib price membrane fractions as dynein elements, however, our study is the first to ever provide 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. Thus, our work recognizes pJNK being a Jip3 dependent retrograde freight. Additionally, through the implementation of our in vivo imaging approach, we found that the frequency of retrograde JNK3 transport was decreased with loss of Jip3, but the processivity of the motor and velocity of movement were unchanged. This information, in conjunction 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. Employing a combination of in and immunolabeling vivo imaging practices, we further show that Jip3 is necessary for retrograde transport of lysosomes through interaction with the dynein accessory protein DLIC. DLIC continues to be shown to be a crucial mediator of dynein based lysosome action in culture techniques and was shown to biochemically interact with Jip3 in yet another program.