Asset Details
Do you wish to reserve the book?
Insights into autophagosome biogenesis from structural and biochemical analyses of the ATG2A-WIPI4 complex
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?
Insights into autophagosome biogenesis from structural and biochemical analyses of the ATG2A-WIPI4 complex
Do you wish to request the book?
Insights into autophagosome biogenesis from structural and biochemical analyses of the ATG2A-WIPI4 complex
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
Insights into autophagosome biogenesis from structural and biochemical analyses of the ATG2A-WIPI4 complex
2018
Overview
Autophagy is an enigmatic cellular process in which double-membrane compartments, called “autophagosomes, form de novo adjacent to the endoplasmic reticulum (ER) and package cytoplasmic contents for delivery to lysosomes. Expansion of the precursor membrane phagophore requires autophagy-related 2 (ATG2), which localizes to the PI3P-enriched ER–phagophore junction. We combined single-particle electron microscopy, chemical cross-linking coupled with mass spectrometry, and biochemical analyses to characterize human ATG2A in complex with the PI3P effector WIPI4. ATG2A is a rod-shaped protein that can bridge neighboring vesicles through interactions at each of its tips. WIPI4 binds to one of the tips, enabling the ATG2A-WIPI4 complex to tether a PI3P-containing vesicle to another PI3P-free vesicle. These data suggest that the ATG2A-WIPI4 complex mediates ER–phagophore association and/or tethers vesicles to the ER–phagophore junction, establishing the required organization for phagophore expansion via the transfer of lipid membranes from the ER and/or the vesicles to the phagophore.
Publisher
National Academy of Sciences
Subject
/ Autophagy-Related Proteins - chemistry
/ Autophagy-Related Proteins - metabolism
/ Endoplasmic Reticulum - metabolism
/ Humans
/ Lipids
/ Membrane Proteins - chemistry
/ Membrane Proteins - metabolism
/ Multiprotein Complexes - chemistry
/ Multiprotein Complexes - metabolism
/ Phosphatidylinositol Phosphates - chemistry
/ Phosphatidylinositol Phosphates - metabolism
/ Proteins
/ Tethers
/ Tips
/ Vesicles
