Asset Details
Do you wish to reserve the book?
Endosomal Arl4A attenuates EGFR degradation by binding to the ESCRT-II component VPS36
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Endosomal Arl4A attenuates EGFR degradation by binding to the ESCRT-II component VPS36
Do you wish to request the book?
Endosomal Arl4A attenuates EGFR degradation by binding to the ESCRT-II component VPS36
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Endosomal Arl4A attenuates EGFR degradation by binding to the ESCRT-II component VPS36
2023
Overview
Ligand-induced epidermal growth factor receptor (EGFR) endocytosis followed by endosomal EGFR signaling and lysosomal degradation plays important roles in controlling multiple biological processes. ADP-ribosylation factor (Arf)-like protein 4 A (Arl4A) functions at the plasma membrane to mediate cytoskeletal remodeling and cell migration, whereas its localization at endosomal compartments remains functionally unknown. Here, we report that Arl4A attenuates EGFR degradation by binding to the endosomal sorting complex required for transport (ESCRT)-II component VPS36. Arl4A plays a role in prolonging the duration of EGFR ubiquitinylation and deterring endocytosed EGFR transport from endosomes to lysosomes under EGF stimulation. Mechanistically, the Arl4A-VPS36 direct interaction stabilizes VPS36 and ESCRT-III association, affecting subsequent recruitment of deubiquitinating-enzyme USP8 by CHMP2A. Impaired Arl4A-VPS36 interaction enhances EGFR degradation and clearance of EGFR ubiquitinylation. Together, we discover that Arl4A negatively regulates EGFR degradation by binding to VPS36 and attenuating ESCRT-mediated late endosomal EGFR sorting.
Endosomal EGFR signaling and lysosomal degradation play important roles in controlling numerous biological processes. Here, the authors show that Arl4A negatively regulates EGFR degradation by binding to VPS36 and attenuating ESCRT-mediated late endosomal EGFR sorting.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 13/1
/ 14
/ 14/63
/ 38
/ 38/70
/ 42/89
/ 631/45
/ 96
/ 96/44
/ Binding
/ Endosomal Sorting Complexes Required for Transport - genetics
/ Endosomal Sorting Complexes Required for Transport - metabolism
/ Epidermal growth factor receptors
/ Humanities and Social Sciences
/ Humans
/ Ligands
/ Medicine
/ Protein Transport - physiology
/ Proteins
/ Science
