%0 Journal Article %1 Axe:2008:J-Cell-Biol:18725538 %A Axe, E L %A Walker, S A %A Manifava, M %A Chandra, P %A Roderick, H L %A Habermann, A %A Griffiths, G %A Ktistakis, N T %D 2008 %J J Cell Biol %K imported %N 4 %P 685-701 %R 10.1083/jcb.200803137 %T Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum %U http://www.ncbi.nlm.nih.gov/pubmed/18725538?dopt=Abstract %V 182 %X Autophagy is the engulfment of cytosol and organelles by double-membrane vesicles termed autophagosomes. Autophagosome formation is known to require phosphatidylinositol 3-phosphate (PI(3)P) and occurs near the endoplasmic reticulum (ER), but the exact mechanisms are unknown. We show that double FYVE domain-containing protein 1, a PI(3)P-binding protein with unusual localization on ER and Golgi membranes, translocates in response to amino acid starvation to a punctate compartment partially colocalized with autophagosomal proteins. Translocation is dependent on Vps34 and beclin function. Other PI(3)P-binding probes targeted to the ER show the same starvation-induced translocation that is dependent on PI(3)P formation and recognition. Live imaging experiments show that this punctate compartment forms near Vps34-containing vesicles, is in dynamic equilibrium with the ER, and provides a membrane platform for accumulation of autophagosomal proteins, expansion of autophagosomal membranes, and emergence of fully formed autophagosomes. This PI(3)P-enriched compartment may be involved in autophagosome biogenesis. Its dynamic relationship with the ER is consistent with the idea that the ER may provide important components for autophagosome formation.

@article{Axe:2008:J-Cell-Biol:18725538, abstract = {Autophagy is the engulfment of cytosol and organelles by double-membrane vesicles termed autophagosomes. Autophagosome formation is known to require phosphatidylinositol 3-phosphate (PI(3)P) and occurs near the endoplasmic reticulum (ER), but the exact mechanisms are unknown. We show that double FYVE domain-containing protein 1, a PI(3)P-binding protein with unusual localization on ER and Golgi membranes, translocates in response to amino acid starvation to a punctate compartment partially colocalized with autophagosomal proteins. Translocation is dependent on Vps34 and beclin function. Other PI(3)P-binding probes targeted to the ER show the same starvation-induced translocation that is dependent on PI(3)P formation and recognition. Live imaging experiments show that this punctate compartment forms near Vps34-containing vesicles, is in dynamic equilibrium with the ER, and provides a membrane platform for accumulation of autophagosomal proteins, expansion of autophagosomal membranes, and emergence of fully formed autophagosomes. This PI(3)P-enriched compartment may be involved in autophagosome biogenesis. Its dynamic relationship with the ER is consistent with the idea that the ER may provide important components for autophagosome formation.}, added-at = {2008-11-05T11:01:57.000+0100}, author = {Axe, E L and Walker, S A and Manifava, M and Chandra, P and Roderick, H L and Habermann, A and Griffiths, G and Ktistakis, N T}, biburl = {https://www.bibsonomy.org/bibtex/24f38de5d831480cd2779b05ceab09f43/ben8bibsonomy}, description = {Autophagosome formation from membrane compartments...[J Cell Biol. 2008] - PubMed Result}, doi = {10.1083/jcb.200803137}, interhash = {01e4c73e7a35e2c2d955ff8ced75a71b}, intrahash = {4f38de5d831480cd2779b05ceab09f43}, journal = {J Cell Biol}, keywords = {imported}, month = Aug, number = 4, pages = {685-701}, pmid = {18725538}, timestamp = {2008-11-05T11:01:57.000+0100}, title = {Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum}, url = {http://www.ncbi.nlm.nih.gov/pubmed/18725538?dopt=Abstract}, volume = 182, year = 2008 }