Syntaxin 16’s Newly Deciphered Roles in Autophagy
Abstract
1. Introduction
2. Syntaxin 16’s Involvement in Autophagosome Formation
3. Syntaxin 16’s Involvement in Autolysosome Biogenesis
4. New Perspectives
Author Contributions
Funding
Acknowledgments
Conflicts of Interest
References
- Søreng, K.; Neufeld, T.P.; Simonsen, A. Membrane trafficking in autophagy. Int. Rev. Cell Mol. Biol. 2018, 336, 1–92. [Google Scholar] [PubMed]
- Yu, L.; Chen, Y.; Tooze, S.A. Autophagy pathway: Cellular and molecular mechanisms. Autophagy 2018, 14, 207–215. [Google Scholar] [CrossRef] [PubMed]
- Bonifacino, J.S.; Lippincott-Schwartz, J. Coat proteins: Shaping membrane transport. Nat. Rev. Mol. Cell Biol. 2003, 4, 409–414. [Google Scholar] [CrossRef] [PubMed]
- Malsam, J.; Kreye, S.; Söllner, T.H. Membrane fusion: SNAREs and regulation. Cell Mol. Life Sci. 2008, 65, 2814–2832. [Google Scholar] [CrossRef]
- Nakamura, S.; Yoshimori, T. New insights into autophagosome-lysosome fusion. J. Cell Sci. 2017, 130, 1209–1216. [Google Scholar] [CrossRef]
- Meijer, W.H.; van der Klei, I.J.; Veenhuis, M.; Kiel, J.A.K.W. ATG genes involved in non-selective autophagy are conserved from yeast to man, but the selective Cvt and pexophagy pathways also require organism-specific genes. Autophagy 2007, 3, 106–116. [Google Scholar] [CrossRef]
- Hamasaki, M.; Furuta, N.; Matsuda, A.; Nezu, A.; Yamamoto, A.; Fujita, N.; Oomori, H.; Noda, T.; Haraguchi, T.; Hiraoka, Y.; et al. Autophagosomes form at ER-mitochondria contact sites. Nature 2013, 495, 389–393. [Google Scholar] [CrossRef]
- Sanchez-Wandelmer, J.; Ktistakis, N.T.; Reggiori, F. ERES: Sites for autophagosome biogenesis and maturation? J. Cell Sci. 2015, 128, 185–192. [Google Scholar] [CrossRef]
- Ge, L.; Zhang, M.; Kenny, S.J.; Liu, D.; Maeda, M.; Saito, K.; Mathur, A.; Xu, K.; Schekman, R. Remodeling of ER-exit sites initiates a membrane supply pathway for autophagosome biogenesis. EMBO Rep. 2017, 18, 1586–1603. [Google Scholar] [CrossRef]
- Guo, Y.; Chang, C.; Huang, R.; Liu, B.; Bao, L.; Liu, W. AP1 is essential for generation of autophagosomes from the trans-Golgi network. J. Cell Sci. 2012, 125, 1706–1715. [Google Scholar] [CrossRef]
- Nascimbeni, A.C.; Giordano, F.; Dupont, N.; Grasso, D.; Vaccaro, M.I.; Codogno, P.; Morel, E. ER-plasma membrane contact sites contribute to autophagosome biogenesis by regulation of local PI3P synthesis. EMBO J. 2017, 36, 2018–2033. [Google Scholar] [CrossRef] [PubMed]
- Puri, C.; Vicinanza, M.; Ashkenazi, A.; Gratian, M.J.; Zhang, Q.; Bento, C.F.; Renna, M.; Menzies, F.M.; Rubinsztein, D.C. The RAB11A-positive compartment is a primary platform for autophagosome assembly mediated by WIPI2 recognition of PI3P-RAB11A. Dev. Cell 2018, 45, 114–131.e8. [Google Scholar] [CrossRef] [PubMed]
- Razi, M.; Chan, E.Y.W.; Tooze, S.A. Early endosomes and endosomal coatomer are required for autophagy. J. Cell Biol. 2009, 185, 305–321. [Google Scholar] [CrossRef] [PubMed]
- Ge, L.; Zhang, M.; Schekman, R. Phosphatidylinositol 3-kinase and COPII generate LC3 lipidation vesicles from the ER-Golgi intermediate compartment. eLife 2014, 3, e04135. [Google Scholar] [CrossRef]
- Wang, J.; Tan, D.; Cai, Y.; Reinisch, K.M.; Walz, T.; Ferro-Novick, S. A requirement for ER-derived COPII vesicles in phagophore initiation. Autophagy 2014, 10, 708–709. [Google Scholar] [CrossRef]
- Davis, S.; Ferro-Novick, S. Ypt1 and COPII vesicles act in autophagosome biogenesis and the early secretory pathway. Biochem. Soc. Trans. 2015, 43, 92–96. [Google Scholar] [CrossRef]
- Shima, T.; Kirisako, H.; Nakatogawa, H. COPII vesicles contribute to autophagosomal membranes. J. Cell Biol. 2019, 218, 1503–1510. [Google Scholar] [CrossRef]
- Popovic, D.; Dikic, I. TBC1D5 and the AP2 complex regulate ATG9 trafficking and initiation of autophagy. EMBO Rep. 2014, 15, 392–401. [Google Scholar] [CrossRef]
- Mattera, R.; Park, S.Y.; De Pace, R.; Guardia, C.M.; Bonifacino, J.S. AP-4 mediates export of ATG9A from the trans-Golgi network to promote autophagosome formation. Proc. Natl. Acad. Sci. USA 2017, 114, E10697–E10706. [Google Scholar]
- Davies, A.K.; Itzhak, D.N.; Edgar, J.R.; Archuleta, T.L.; Hirst, J.; Jackson, L.P.; Robinson, M.S.; Borner, G.H.H. AP-4 vesicles contribute to spatial control of autophagy via RUSC-dependent peripheral delivery of ATG9A. Nat. Commun. 2018, 9, 3958. [Google Scholar] [CrossRef]
- Tan, D.; Cai, Y.; Wang, J.; Zhang, J.; Menon, S.; Chou, H.T.; Ferro-Novick, S.; Reinisch, K.M.; Walz, T. The EM structure of the TRAPPIII complex leads to the identification of a requirement for COPII vesicles on the macroautophagy pathway. Proc. Natl. Acad. Sci. USA 2013, 110, 19432–19437. [Google Scholar] [CrossRef] [PubMed]
- Stadel, D.; Millarte, V.; Tillmann, K.D.; Huber, J.; Tamin-Yecheskel, B.C.; Akutsu, M.; Demishtein, A.; Ben-Zeev, B.; Anikster, Y.; Perez, F.; et al. TECPR2 Cooperates with LC3C to Regulate COPII-Dependent ER Export. Mol. Cell 2015, 60, 89–104. [Google Scholar] [CrossRef] [PubMed]
- Lemus, L.; Ribas, J.L.; Sikorska, N.; Goder, V. An ER-Localized SNARE Protein Is Exported in Specific COPII Vesicles for Autophagosome Biogenesis. Cell Rep. 2016, 14, 1710–1722. [Google Scholar] [CrossRef] [PubMed]
- Cui, Y.; Parashar, S.; Zahoor, M.; Needham, P.G.; Mari, M.; Zhu, M.; Chen, S.; Ho, H.C.; Reggiori, F.; Farhan, H.; et al. A COPII subunit acts with an autophagy receptor to target endoplasmic reticulum for degradation. Science 2019, 365, 53–60. [Google Scholar] [CrossRef] [PubMed]
- Mari, M.; Griffith, J.; Rieter, E.; Krishnappa, L.; Klionsky, D.J.; Reggiori, F. An Atg9-containing compartment that functions in the early steps of autophagosome biogenesis. J. Cell Biol. 2010, 190, 1005–1022. [Google Scholar] [CrossRef]
- Shirahama-Noda, K.; Kira, S.; Yoshimori, T.; Noda, T. TRAPPIII is responsible for vesicular transport from early endosomes to Golgi, facilitating Atg9 cycling in autophagy. J. Cell Sci. 2013, 126, 4963–4973. [Google Scholar] [CrossRef]
- Imai, K.; Hao, F.; Fujita, N.; Tsuji, Y.; Oe, Y.; Araki, Y.; Hamasaki, M.; Noda, T.; Yoshimori, T. Atg9A trafficking through the recycling endosomes is required for autophagosome formation. J. Cell Sci. 2016, 129, 3781–3791. [Google Scholar] [CrossRef]
- Aoyagi, K.; Itakura, M.; Fukutomi, T.; Nishiwaki, C.; Nakamichi, Y.; Torii, S.; Makiyama, T.; Harada, A.; Ohara-Imaizumi, M. VAMP7 Regulates Autophagosome Formation by Supporting Atg9a Functions in Pancreatic β-Cells From Male Mice. Endocrinology 2018, 159, 3674–3688. [Google Scholar] [CrossRef]
- Judith, D.; Jefferies, H.B.J.; Boeing, S.; Frith, D.; Snijders, A.P.; Tooze, S.A. ATG9A shapes the forming autophagosome through Arfaptin 2 and phosphatidylinositol 4-kinase IIIβ. J. Cell Biol. 2019, 218, 1634–1652. [Google Scholar] [CrossRef]
- Feng, Y.; Backues, S.K.; Baba, M.; Heo, J.M.; Harper, J.W.; Klionsky, D.J. Phosphorylation of Atg9 regulates movement to the phagophore assembly site and the rate of autophagosome formation. Autophagy 2016, 12, 648–658. [Google Scholar] [CrossRef]
- Zhou, C.; Ma, K.; Gao, R.; Mu, C.; Chen, L.; Liu, Q.; Luo, Q.; Feng, D.; Zhu, Y.; Chen, Q. Regulation of mATG9 trafficking by Src- and ULK1-mediated phosphorylation in basal and starvation-induced autophagy. Cell Res. 2017, 27, 184–201. [Google Scholar] [CrossRef] [PubMed]
- Nair, U.; Jotwani, A.; Geng, J.; Gammoh, N.; Richerson, D.; Yen, W.L.; Griffith, J.; Nag, S.; Wang, K.; Moss, T.; et al. SNARE proteins are required for macroautophagy. Cell 2011, 146, 290–302. [Google Scholar] [CrossRef] [PubMed]
- Rao, Y.; Perna, M.G.; Hofmann, B.; Beier, V.; Wollert, T. The Atg1-kinase complex tethers Atg9-vesicles to initiate autophagy. Nat. Commun. 2016, 7, 10338. [Google Scholar] [CrossRef] [PubMed]
- Matscheko, N.; Mayrhofer, P.; Rao, Y.; Beier, V.; Wollert, T. Atg11 tethers Atg9 vesicles to initiate selective autophagy. PLoS Biol. 2019, 17, e3000377. [Google Scholar] [CrossRef] [PubMed]
- Kim, J.; Kundu, M.; Viollet, B.; Guan, K.L. AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1. Nat. Cell Biol. 2011, 13, 132–141. [Google Scholar] [CrossRef] [PubMed]
- Munson, M.J.; Ganley, I.G. MTOR, PIK3C3, and autophagy: Signaling the beginning from the end. Autophagy 2015, 11, 2375–2376. [Google Scholar] [CrossRef]
- Mihaylova, M.M.; Shaw, R.J. The AMPK signalling pathway coordinates cell growth, autophagy and metabolism. Nat. Cell Biol. 2011, 13, 1016–1023. [Google Scholar] [CrossRef]
- Russell, R.C.; Tian, Y.; Yuan, H.; Park, H.W.; Chang, Y.Y.; Kim, J.; Kim, H.; Neufeld, T.P.; Dillin, A.; Guan, K.L. ULK1 induces autophagy by phosphorylating Beclin-1 and activating VPS34 lipid kinase. Nat. Cell Biol. 2013, 15, 741–750. [Google Scholar] [CrossRef]
- Biazik, J.; Ylä-Anttila, P.; Vihinen, H.; Jokitalo, E.; Eskelinen, E.L. Ultrastructural relationship of the phagophore with surrounding organelles. Autophagy 2015, 11, 439–451. [Google Scholar] [CrossRef]
- Lystad, A.H.; Simonsen, A. Mechanisms and Pathophysiological Roles of the ATG8 Conjugation Machinery. Cells 2019, 8, 973. [Google Scholar] [CrossRef]
- Schaaf, M.B.E.; Keulers, T.G.; Vooijs, M.A.; Rouschop, K.M.A. LC3/GABARAP family proteins: Autophagy-(un)related functions. FASEB J. 2016, 30, 3961–3978. [Google Scholar] [CrossRef] [PubMed]
- Nakatogawa, H. Two ubiquitin-like conjugation systems that mediate membrane formation during autophagy. Essays Biochem. 2013, 55, 39–50. [Google Scholar] [PubMed]
- Hanada, T.; Noda, N.N.; Satomi, Y.; Ichimura, Y.; Fujioka, Y.; Takao, T.; Inagaki, F.; Ohsumi, Y. The Atg12-Atg5 conjugate has a novel E3-like activity for protein lipidation in autophagy. J. Biol. Chem. 2007, 282, 37298–37302. [Google Scholar] [CrossRef] [PubMed]
- Tanida, I.; Ueno, T.; Kominami, E. LC3 and Autophagy. Methods Mol. Biol. 2008, 445, 77–88. [Google Scholar]
- Weidberg, H.; Shvets, E.; Shpilka, T.; Shimron, F.; Shinder, V.; Elazar, Z. LC3 and GATE-16/GABARAP subfamilies are both essential yet act differently in autophagosome biogenesis. EMBO J. 2010, 29, 1792–1802. [Google Scholar] [CrossRef]
- Johansen, T.; Lamark, T. Selective autophagy: ATG8 family proteins, LIR motifs and cargo receptors. J. Mol. Biol. 2019. [Google Scholar] [CrossRef]
- Peng, H.; Yang, J.; Li, G.; You, Q.; Han, W.; Li, T.; Gao, D.; Xie, X.; Lee, B.H.; Du, J.; et al. Ubiquitylation of p62/sequestosome1 activates its autophagy receptor function and controls selective autophagy upon ubiquitin stress. Cell Res. 2017, 27, 657–674. [Google Scholar] [CrossRef]
- Nguyen, T.N.; Padman, B.S.; Usher, J.; Oorschot, V.; Ramm, G.; Lazarou, M. Atg8 family LC3/GABARAP proteins are crucial for autophagosome-lysosome fusion but not autophagosome formation during PINK1/Parkin mitophagy and starvation. J. Cell Biol. 2016, 215, 857–874. [Google Scholar] [CrossRef]
- Moreau, K.; Renna, M.; Rubinsztein, D.C. Connections between SNAREs and autophagy. Trends Biochem. Sci. 2013, 38, 57–63. [Google Scholar] [CrossRef]
- Itakura, E.; Mizushima, N. Syntaxin 17: The autophagosomal SNARE. Autophagy 2013, 9, 917–919. [Google Scholar] [CrossRef]
- Hegedűs, K.; Takáts, S.; Kovács, A.L.; Juhász, G. Evolutionarily conserved role and physiological relevance of a STX17/Syx17 (syntaxin 17)-containing SNARE complex in autophagosome fusion with endosomes and lysosomes. Autophagy 2013, 9, 1642–1646. [Google Scholar] [CrossRef]
- Itakura, E.; Kishi-Itakura, C.; Mizushima, N. The hairpin-type tail-anchored SNARE syntaxin 17 targets to autophagosomes for fusion with endosomes/lysosomes. Cell 2012, 151, 1256–1269. [Google Scholar] [CrossRef] [PubMed]
- Takáts, S.; Nagy, P.; Varga, Á.; Pircs, K.; Kárpáti, M.; Varga, K.; Kovács, A.L.; Hegedűs, K.; Juhász, G. Autophagosomal Syntaxin17-dependent lysosomal degradation maintains neuronal function in Drosophila. J. Cell Biol. 2013, 201, 531–539. [Google Scholar] [CrossRef] [PubMed]
- Diao, J.; Liu, R.; Rong, Y.; Zhao, M.; Zhang, J.; Lai, Y.; Zhou, Q.; Wilz, L.M.; Li, J.; Vivona, S.; et al. ATG14 promotes membrane tethering and fusion of autophagosomes to endolysosomes. Nature 2015, 520, 563–566. [Google Scholar] [CrossRef] [PubMed]
- Jiang, P.; Nishimura, T.; Sakamaki, Y.; Itakura, E.; Hatta, T.; Natsume, T.; Mizushima, N. The HOPS complex mediates autophagosome-lysosome fusion through interaction with syntaxin 17. Mol. Biol. Cell 2014, 25, 1327–1337. [Google Scholar] [CrossRef]
- Takáts, S.; Pircs, K.; Nagy, P.; Varga, Á.; Kárpáti, M.; Hegedűs, K.; Kramer, H.; Kovács, A.L.; Sass, M.; Juhász, G. Interaction of the HOPS complex with Syntaxin 17 mediates autophagosome clearance in Drosophila. Mol. Biol. Cell 2014, 25, 1338–1354. [Google Scholar]
- Kumar, S.; Jain, A.; Farzam, F.; Jia, J.; Gu, Y.; Choi, S.W.; Mudd, M.H.; Claude-Taupin, A.; Wester, M.J.; Lidke, K.A.; et al. Mechanism of Stx17 recruitment to autophagosomes via IRGM and mammalian Atg8 proteins. J. Cell Biol. 2018, 217, 997–1013. [Google Scholar] [CrossRef]
- Kumar, S.; Gu, Y.; Abudu, Y.P.; Bruun, J.A.; Jain, A.; Farzam, F.; Mudd, M.; Anonsen, J.H.; Rusten, T.E.; Kasof, G.; et al. Phosphorylation of Syntaxin 17 by TBK1 controls autophagy initiation. Dev. Cell 2019, 49, 130–144.e6. [Google Scholar] [CrossRef]
- Gao, J.; Reggiori, F.; Ungermann, C. A novel in vitro assay reveals SNARE topology and the role of Ykt6 in autophagosome fusion with vacuoles. J. Cell Biol. 2018, 217, 3670–3682. [Google Scholar] [CrossRef]
- Takáts, S.; Glatz, G.; Szenci, G.; Boda, A.; Horváth, G.V.; Hegedűs, K.; Kovács, A.L.; Juhász, G. Non-canonical role of the SNARE protein Ykt6 in autophagosome-lysosome fusion. PLoS Genet. 2018, 14, e1007359. [Google Scholar] [CrossRef]
- Bas, L.; Papinski, D.; Licheva, M.; Torggler, R.; Rohringer, S.; Schuschnig, M.; Kraft, C. Reconstitution reveals Ykt6 as the autophagosomal SNARE in autophagosome-vacuole fusion. J. Cell Biol. 2018, 217, 3656–3669. [Google Scholar] [CrossRef] [PubMed]
- Matsui, T.; Jiang, P.; Nakano, S.; Sakamaki, Y.; Yamamoto, H.; Mizushima, N. Autophagosomal YKT6 is required for fusion with lysosomes independently of syntaxin 17. J. Cell Biol. 2018, 217, 2633–2645. [Google Scholar] [CrossRef] [PubMed]
- Tang, B.L.; Low, D.Y.; Lee, S.S.; Tan, A.E.; Hong, W. Molecular cloning and localization of human syntaxin 16, a member of the syntaxin family of SNARE proteins. Biochem. Biophys. Res. Commun. 1998, 242, 673–679. [Google Scholar] [CrossRef] [PubMed]
- Simonsen, A.; Bremnes, B.; Rønning, E.; Aasland, R.; Stenmark, H. Syntaxin-16, a putative Golgi t-SNARE. Eur. J. Cell Biol. 1998, 75, 223–231. [Google Scholar] [CrossRef]
- Mallard, F.; Tang, B.L.; Galli, T.; Tenza, D.; Saint-Pol, A.; Yue, X.; Antony, C.; Hong, W.; Goud, B.; Johannes, L. Early/recycling endosomes-to-TGN transport involves two SNARE complexes and a Rab6 isoform. J. Cell Biol. 2002, 156, 653–664. [Google Scholar] [CrossRef]
- Amessou, M.; Fradagrada, A.; Falguières, T.; Lord, J.M.; Smith, D.C.; Roberts, L.M.; Lamaze, C.; Johannes, L. Syntaxin 16 and syntaxin 5 are required for efficient retrograde transport of several exogenous and endogenous cargo proteins. J. Cell Sci. 2007, 120, 1457–1468. [Google Scholar] [CrossRef]
- Struthers, M.S.; Shanks, S.G.; MacDonald, C.; Carpp, L.N.; Drozdowska, A.M.; Kioumourtzoglou, D.; Furgason, M.L.M.; Munson, M.; Bryant, N.J. Functional homology of mammalian syntaxin 16 and yeast Tlg2p reveals a conserved regulatory mechanism. J. Cell Sci. 2009, 122, 2292–2299. [Google Scholar] [CrossRef]
- Gu, Y.; Princely Abudu, Y.; Kumar, S.; Bissa, B.; Choi, S.W.; Jia, J.; Lazarou, M.; Eskelinen, E.L.; Johansen, T.; Deretic, V. Mammalian Atg8 proteins regulate lysosome and autolysosome biogenesis through SNAREs. EMBO J. 2019, e101994. [Google Scholar] [CrossRef]
- Aoyagi, K.; Ohara-Imaizumi, M.; Itakura, M.; Torii, S.; Akimoto, Y.; Nishiwaki, C.; Nakamichi, Y.; Kishimoto, T.; Kawakami, H.; Harada, A.; et al. VAMP7 regulates autophagy to maintain mitochondrial homeostasis and to control insulin secretion in pancreatic β-cells. Diabetes 2016, 65, 1648–1659. [Google Scholar] [CrossRef]
- Rossi, V.; Banfield, D.K.; Vacca, M.; Dietrich, L.E.P.; Ungermann, C.; D’Esposito, M.; Galli, T.; Filippini, F. Longins and their longin domains: Regulated SNAREs and multifunctional SNARE regulators. Trends Biochem. Sci. 2004, 29, 682–688. [Google Scholar] [CrossRef]
- Pryor, P.R.; Jackson, L.; Gray, S.R.; Edeling, M.A.; Thompson, A.; Sanderson, C.M.; Evans, P.R.; Owen, D.J.; Luzio, J.P. Molecular basis for the sorting of the SNARE VAMP7 into endocytic clathrin-coated vesicles by the ArfGAP Hrb. Cell 2008, 134, 817–827. [Google Scholar] [CrossRef] [PubMed]
- Birgisdottir, Å.B.; Lamark, T.; Johansen, T. The LIR motif - crucial for selective autophagy. J. Cell Sci. 2013, 126, 3237–3247. [Google Scholar] [PubMed]
- Hatsuzawa, K.; Hirose, H.; Tani, K.; Yamamoto, A.; Scheller, R.H.; Tagaya, M. Syntaxin 18, a SNAP receptor that functions in the endoplasmic reticulum, intermediate compartment, and cis-Golgi vesicle trafficking. J. Biol. Chem. 2000, 275, 13713–13720. [Google Scholar] [CrossRef] [PubMed]
- Bennett, M.K.; García-Arrarás, J.E.; Elferink, L.A.; Peterson, K.; Fleming, A.M.; Hazuka, C.D.; Scheller, R.H. The syntaxin family of vesicular transport receptors. Cell 1993, 74, 863–873. [Google Scholar] [CrossRef]
- Shewan, A.M.; van Dam, E.M.; Martin, S.; Luen, T.B.; Hong, W.; Bryant, N.J.; James, D.E. GLUT4 recycles via a trans-Golgi network (TGN) subdomain enriched in Syntaxins 6 and 16 but not TGN38: Involvement of an acidic targeting motif. Mol. Biol. Cell 2003, 14, 973–986. [Google Scholar] [CrossRef] [PubMed]
- Chua, C.E.L.; Tang, B.L. Syntaxin 16 is enriched in neuronal dendrites and may have a role in neurite outgrowth. Mol. Membr. Biol. 2008, 25, 35–45. [Google Scholar] [CrossRef]
- Gee, H.Y.; Tang, B.L.; Kim, K.H.; Lee, M.G. Syntaxin 16 binds to cystic fibrosis transmembrane conductance regulator and regulates its membrane trafficking in epithelial cells. J. Biol. Chem. 2010, 285, 35519–35527. [Google Scholar] [CrossRef]
- Chen, Y.; Gan, B.Q.; Tang, B.L. Syntaxin 16: Unraveling cellular physiology through a ubiquitous SNARE molecule. J. Cell Physiol. 2010, 225, 326–332. [Google Scholar] [CrossRef]
- Neto, H.; Kaupisch, A.; Collins, L.L.; Gould, G.W. Syntaxin 16 is a master recruitment factor for cytokinesis. Mol. Biol. Cell 2013, 24, 3663–3674. [Google Scholar] [CrossRef]
- Solinger, J.A.; Spang, A. Tethering complexes in the endocytic pathway: CORVET and HOPS. FEBS J. 2013, 280, 2743–2757. [Google Scholar] [CrossRef]
- Balderhaar, H.J.K.; Ungermann, C. CORVET and HOPS tethering complexes - coordinators of endosome and lysosome fusion. J. Cell Sci. 2013, 126, 1307–1316. [Google Scholar] [CrossRef] [PubMed]
- Pols, M.S.; van Meel, E.; Oorschot, V.; ten Brink, C.; Fukuda, M.; Swetha, M.G.; Mayor, S.; Klumperman, J. hVps41 and VAMP7 function in direct TGN to late endosome transport of lysosomal membrane proteins. Nat. Commun. 2013, 4, 1361. [Google Scholar] [CrossRef] [PubMed]
- Korolchuk, V.I.; Saiki, S.; Lichtenberg, M.; Siddiqi, F.H.; Roberts, E.A.; Imarisio, S.; Jahreiss, L.; Sarkar, S.; Futter, M.; Menzies, F.M.; et al. Lysosomal positioning coordinates cellular nutrient responses. Nat. Cell Biol. 2011, 13, 453–460. [Google Scholar] [CrossRef] [PubMed]
- Sancak, Y.; Bar-Peled, L.; Zoncu, R.; Markhard, A.L.; Nada, S.; Sabatini, D.M. Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids. Cell 2010, 141, 290–303. [Google Scholar] [CrossRef] [PubMed]
- Tian, X.; Zheng, P.; Zhou, C.; Wang, X.; Ma, H.; Ma, W.; Zhou, X.; Teng, J.; Chen, J. DIPK2A promotes STX17- and VAMP7-mediated autophagosome-lysosome fusion by binding to VAMP7B. Autophagy 2019. [Google Scholar] [CrossRef]
- Viret, C.; Faure, M. Regulation of Syntaxin 17 during autophagosome maturation. Trends Cell Biol. 2019, 29, 1–3. [Google Scholar] [CrossRef]
- Fasshauer, D.; Sutton, R.B.; Brunger, A.T.; Jahn, R. Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs. Proc. Natl. Acad. Sci. USA 1998, 95, 15781–15786. [Google Scholar] [CrossRef]
- Steegmaier, M.; Yang, B.; Yoo, J.S.; Huang, B.; Shen, M.; Yu, S.; Luo, Y.; Scheller, R.H. Three novel proteins of the syntaxin/SNAP-25 family. J. Biol. Chem. 1998, 273, 34171–34179. [Google Scholar] [CrossRef]
- Ding, X.; Jiang, X.; Tian, R.; Zhao, P.; Li, L.; Wang, X.; Chen, S.; Zhu, Y.; Mei, M.; Bao, S.; et al. RAB2 regulates the formation of autophagosome and autolysosome in mammalian cells. Autophagy 2019, 15, 1774–1786. [Google Scholar] [CrossRef]
- Arasaki, K.; Shimizu, H.; Mogari, H.; Nishida, N.; Hirota, N.; Furuno, A.; Kudo, Y.; Baba, M.; Baba, N.; Cheng, J.; et al. A role for the ancient SNARE syntaxin 17 in regulating mitochondrial division. Dev. Cell 2015, 32, 304–317. [Google Scholar] [CrossRef]
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Tang, B.L. Syntaxin 16’s Newly Deciphered Roles in Autophagy. Cells 2019, 8, 1655. https://doi.org/10.3390/cells8121655
Tang BL. Syntaxin 16’s Newly Deciphered Roles in Autophagy. Cells. 2019; 8(12):1655. https://doi.org/10.3390/cells8121655
Chicago/Turabian StyleTang, Bor Luen. 2019. "Syntaxin 16’s Newly Deciphered Roles in Autophagy" Cells 8, no. 12: 1655. https://doi.org/10.3390/cells8121655
APA StyleTang, B. L. (2019). Syntaxin 16’s Newly Deciphered Roles in Autophagy. Cells, 8(12), 1655. https://doi.org/10.3390/cells8121655