EGF and non-small cell lung carcinoma: Tid1-L has a greater cytosolic stability and reduced rate of mitochondrial import compared with Tid1-S, resulting in higher levels of Tid1-L in the cytoplasm.11 Tid1-L, but not Tid1-S, interacts with EGFR/HSP70/HSP90 through the DnaJ domain, and this has been shown to counteract the ability of HSP90 to regulate EGFR by triggering the ubiquitinylation and proteasomal degradation of EGFR.17 In this work, we demonstrate that Tid1-S, but not Tid1-L, is involved in the EGF-stimulated translocation of EGFR into mitochondria in NSCLC cells.