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A fraction of DNAJC5 is also localized to a perinuclear membrane compartment, which is largely free of LAMP1 and not stained well by a LysoTracker dye. However, this compartment can be weakly labeled by LysoTracker after prolonged staining (movie S2), suggesting that it might be a pre-lysosomal compartment. The localization of DNAJC5 to this compartment does not require its J-domain but depends on palmitoylation of DNAJC5 since both the ANCL-associated disease mutants (this study) and a CS-domain deleted mutant fail to associate with this compartment . Additionally, we identified a DNAJC5 binding partner named SLC3A2, which regulates the peri-nuclear localization of DNAJC5. SLC3A2 is a type II membrane glycoprotein capable of interacting with six light chain molecules, forming a set of amino acid transporters on the plasma membrane . Moreover, additional adaptors such as LAPTM4B can retain a SLC3A2-containing transporter in endolysosomes, regulating the amino acid balance between endolysosome and cytoplasm and thus the MTOR signaling . Whether SLC3A2-dependent regulation of the DNAJC5 localization requires additional components awaits further characterization. 1e1e36bf2d