ARF6, RAB5, and RAB7 were reported to be involved in traffic...
| created | [InstanceEdit:9935564] Orlic-Milacic, Marija, 2025-01-15 |
| dbId | 9935565 |
| displayName | ARF6, RAB5, and RAB7 were reported to be involved in traffic... |
| literatureReference |
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| modified | [InstanceEdit:9936239] Orlic-Milacic, Marija, 2025-01-22 |
| schemaClass | Summation |
| text | ARF6, RAB5, and RAB7 were reported to be involved in trafficking of a recombinant mouse CDH1 (E-cadherin) to lysosome for degradation in MDCK cells upon SRC-facilitated tyrosine phosphorylation and ubiquitination of CDH1 (Palacios et al. 2005). In the human breast cancer cell line MCF7, CBLL1 (Hakai)-mediated CDH1 ubiquitination and internalization leads to lysosome-dependent degradation of CDH1, while the proteasome does not appear to play a significant role (Shen et al. 2008). In the human hepatocellular carcinoma cell line HepG2, CBLL1-facilitated CDH1 ubiquitination and internalization was reported to lead to CDH1 degradation through both proteasomal and lysosomal routes (Chen et al. 2009). The integrin-interacting protein BSG (also known as besigin or CD147) was reported to promote lysosomal localization and degradation of CDH1 in HepG2 cells (Lu et al. 2018). In a study in which recombinant mouse CDH1 constructs, either full-length or just involving the juxtamembrane domain (JMD) of CDH1, were expressed in the canine MDCK cell line, it was found that proteasome is at least partially responsible for degradation of the ubiquitinated CDH1 (Hartsock and Nelson 2012). In the human colon carcinoma cell line T84, IFNG (interferon-gamma)-stimulated internalization of CDH1 is dependent on FYN kinase and CBLL1, and both lysosome and proteasome contribute to degradation of internalized CDH1 (Smyth et al. 2012). RAF kinase may promote the sorting of internalized CDH1 from the endosome to the lysosome compartment rather than to the recycling route (Janda et al. 2006). |
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