Adaptation of endoplasmic reticulum exit sites to acute and chronic increases in cargo load
Open accessAbstract
The biogenesis of endoplasmic reticulum (ER) exit sites (ERES) involves the formation of phosphatidylinositol-4 phosphate (PI4) and Sec16, but it is entirely unknown how ERES adapt to variations in cargo load. Here, we studied acute and chronic adaptive responses of ERES to an increase in cargo load for ER export. The acute response (within minutes) to increased cargo load stimulated ERES fusion events, leading to larger but less ERES. Silencing either PI4-kinase IIIalpha (PI4K-IIIalpha) or Sec16 inhibited the acute response. Overexpression of secretory cargo for 24 h induced the unfolded protein response (UPR), upregulated COPII, and the cells formed more ERES. This chronic response was insensitive to silencing PI4K-IIIalpha, but was abrogated by silencing Sec16. The UPR was required as the chronic response was absent in cells lacking inositol-requiring protein 1. Mathematical model simulations further support the notion that increasing ERES number together with COPII levels is an efficient way to enhance the secretory flux. These results indicate that chronic and acute increases in cargo load are handled differentially by ERES and are regulated by different factors.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The recruitment of ERES depends directly on ER export efficiency.
“Our observation that ERES numbers increase—even without nicotine—for enhanced ER export of nAChRs shows that the recruitment of ERES depends directly on ER export efficiency and extends previous observations that simple coexpression of membrane proteins can enhance ERES number (Farhan et al., 2008).”
From Nicotine up-regulates α4β2 nicotinic receptors and ER exit sites via stoichiometry-dependent chaperoning (2011) · cites this paper as Farhan et al., 2008
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Signal integration in the endoplasmic reticulum unfolded protein response
Ron, D., & Walter, P. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2199 · Cited by 6,308 · see citing works
THE MAMMALIAN UNFOLDED PROTEIN RESPONSE
Schröder, M., & Kaufman, R. J. (2005) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.074134 · Cited by 3,035 · see citing works
Self-citationTravers, K. J., Patil, C. K., Wodicka, L. M., Lockhart, D. J., Weissman, J. S., & Walter, P. (2000) · Cell · doi:10.1016/s0092-8674(00)80835-1 · Cited by 1,994 · see citing works
Lippincott‐Schwartz, J., Yuan, L. C., Bonifacino, J. S., & Klausner, R. D. (1989) · Cell · doi:10.1016/0092-8674(89)90685-5 · Cited by 1,688 · see citing works
IRE1 Signaling Affects Cell Fate During the Unfolded Protein Response
Lin, J. H., Li, H., Yasumura, D., Cohen, H. R., Zhang, C., Panning, B., Shokat, K. M., LaVail, M. M., & Walter, P. (2007) · Science · doi:10.1126/science.1146361 · Cited by 1,374 · see citing works
Shaffer, A. L., Shelef, M. A., Iwakoshi, N. N., Lee, A., Qian, S., Zhao, H., Yu, X., Yang, L., Tan, B. K., Rosenwald, A., et al. (2004) · Immunity · doi:10.1016/j.immuni.2004.06.010 · Cited by 1,060 · see citing works
Lee, K., Tirasophon, W., Shen, X., Michalak, M., Prywes, R., Okada, T., Yoshida, H., Mori, K., & Kaufman, R. J. (2002) · Genes & Development · doi:10.1101/gad.964702 · Cited by 1,055 · see citing works
Self-citationBI-DIRECTIONAL PROTEIN TRANSPORT BETWEEN THE ER AND GOLGI
Lee, M., Miller, E. A., Goldberg, J. D., Orci, L., & Schekman, R. W. (2004) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.20.010403.105307 · Cited by 909 · see citing works
XBP1 Controls Diverse Cell Type- and Condition-Specific Transcriptional Regulatory Networks
Acosta‐Alvear, D., Zhou, Y., Blais, A., Tsikitis, M., Lents, N. H., Arias, C., Lennon, C. J., Kluger, Y., & Dynlacht, B. D. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.06.011 · Cited by 853 · see citing works
Matsuoka, K., Orci, L., AMHERDT, M., Bednarek, S. Y., Hamamoto, S., Schekman, R. W., & Yeung, T. (1998) · Cell · doi:10.1016/s0092-8674(00)81577-9 · Cited by 631 · see citing works
Brefeldin A redistributes resident and itinerant Golgi proteins to the endoplasmic reticulum.
Doms, R. W., Russ, G., & Yewdell, J. W. (1989) · The Journal of Cell Biology · doi:10.1083/jcb.109.1.61 · Cited by 593 · see citing works
Structure of the Sec23/24–Sar1 pre-budding complex of the COPII vesicle coat
Bi, X., Corpina, R. A., & Goldberg, J. M. (2002) · Nature · doi:10.1038/nature01040 · Cited by 474 · see citing works
XBP‐1 is required for biogenesis of cellular secretory machinery of exocrine glands
Lee, A., Chu, G. C., Iwakoshi, N. N., & Glimcher, L. H. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600903 · Cited by 452 · see citing works
The unfolded protein response sensor IRE1α is required at 2 distinct steps in B cell lymphopoiesis
Zhang, K., Wong, H. N., Song, B., Miller, C. N., Scheuner, D. L., & Kaufman, R. J. (2005) · Journal of Clinical Investigation · doi:10.1172/jci21848 · Cited by 348 · see citing works
Self-citationSriburi, R., Bommiasamy, H., Buldak, G. L., Robbins, G. R., Frank, M. W., Jackowski, S., & Brewer, J. W. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609490200 · Cited by 262 · see citing works
De novo formation of transitional ER sites and Golgi structures in Pichia pastoris
Bevis, B. J., Hammond, A. T., Reinke, C., & Glick, B. S. (2002) · Nature Cell Biology · doi:10.1038/ncb852 · Cited by 241 · see citing works
Diao, A., Rahman, D., Pappin, D., Lucocq, J. M., & Lowe, M. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200207045 · Cited by 238 · see citing works
Watson, P., Townley, A. K., Koka, P., Palmer, K. J., & Stephens, D. J. (2006) · Traffic · doi:10.1111/j.1600-0854.2006.00493.x · Cited by 232 · see citing works
Role of Sec24 isoforms in selective export of membrane proteins from the endoplasmic reticulum
Wendeler, M. W., Paccaud, J., & Hauri, H. (2007) · The EMBO Reports · doi:10.1038/sj.embor.7400893 · Cited by 197 · see citing works
Self-citationSubcellular Locations of Phosphatidylinositol 4-Kinase Isoforms
Wong, K. K. Y., Meyers, R. E., & Cantley, L. C. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.20.13236 · Cited by 179 · see citing works
The Transport Signal on Sec22 for Packaging into COPII-Coated Vesicles Is a Conformational Epitope
Mancias, J. D., & Goldberg, J. D. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.03.017 · Cited by 168 · see citing works
Bhattacharyya, D., & Glick, B. S. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-08-0707 · Cited by 156 · see citing works
A Di-acidic (DXE) Code Directs Concentration of Cargo during Export from the Endoplasmic Reticulum
Nishimura, N., Bannykh, S. I., Slabough, S., Matteson, J., Altschuler, Y., Hahn, K. M., & Balch, W. E. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.22.15937 · Cited by 154 · see citing works
Secretory Cargo Regulates the Turnover of COPII Subunits at Single ER Exit Sites
Forster, R. A., Weiß, M., Zimmermann, T., Reynaud, E. G., Verı́ssimo, F., Stephens, D. J., & Pepperkok, R. (2006) · Current Biology · doi:10.1016/j.cub.2005.11.076 · Cited by 138 · see citing works
Mezzacasa, A., & Helenius, A. (2002) · Traffic · doi:10.1034/j.1600-0854.2002.31108.x · Cited by 125 · see citing works
COPII coat subunit interactions: Sec24p and Sec23p bind to adjacent regions of Sec16p.
Gimeno, R. E., Espenshade, P. J., & Kaiser, C. A. (1996) · Molecular Biology of the Cell · doi:10.1091/mbc.7.11.1815 · Cited by 123 · see citing works
Phosphatidylinositol 4-Phosphate Formation at ER Exit Sites Regulates ER Export
Blumental‐Perry, A., Haney, C. J., Weixel, K. M., Watkins, S. C., Weisz, O. A., & Aridor, M. (2006) · Developmental Cell · doi:10.1016/j.devcel.2006.09.001 · Cited by 110 · see citing works
De novo formation, fusion and fission of mammalian COPII‐coated endoplasmic reticulum exit sites
Stephens, D. J. (2003) · EMBO Reports · doi:10.1038/sj.embor.embor736 · Cited by 101 · see citing works
Farhan, H., Reiterer, V., Korkhov, V. M., Schmid, J. A., Freissmuth, M., & Sitte, H. H. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609720200 · Cited by 100 · see citing works
Self-citationCOPII–Golgi protein interactions regulate COPII coat assembly and Golgi size
Guo, Y., & Linstedt, A. D. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200604058 · Cited by 87 · see citing works
Hanton, S. L., Châtre, L., Renna, L., Matheson, L. A., & Brandizzí, F. (2007) · PLANT PHYSIOLOGY · doi:10.1104/pp.106.094110 · Cited by 85 · see citing works
Identification of the putative mammalian orthologue of Sec31P, a component of the COPII coat
Shugrue, C., Kolen, E. R., Peters, H. I., Czernik, A., Kaiser, C. A., Matovcik, L. M., Hubbard, A. L., & Gorelick, F. S. (1999) · Journal of Cell Science · doi:10.1242/jcs.112.24.4547 · Cited by 81 · see citing works
Mammalian Sec16/p250 Plays a Role in Membrane Traffic from the Endoplasmic Reticulum
Iinuma, T., Shiga, A., Nakamoto, K., O'Brien, M. B., Aridor, M., Arimitsu, N. N., Tagaya, M., & Tani, K. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m611237200 · Cited by 77 · see citing works
Self-citationA model for the self-organization of exit sites in the endoplasmic reticulum
Heinzer, S., Wörz, S., Kalla, C., Rohr, K., & Weiß, M. (2007) · Journal of Cell Science · doi:10.1242/jcs.013383 · Cited by 37 · see citing works
Sato, M., Sato, K., & Nakano, A. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)00922-1 · Cited by 29 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Phosphoinositides: Tiny Lipids With Giant Impact on Cell Regulation
Balla, T. (2013) · Physiological Reviews · doi:10.1152/physrev.00028.2012 · Cited by 1,638 · see citing works
Organization of the ER–Golgi interface for membrane traffic control
Brandizzí, F., & Barlowe, C. K. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3588 · Cited by 523 · see citing works
COPII and the regulation of protein sorting in mammals
Zanetti, G., Pahuja, K. B., Studer, S., Shim, S., & Schekman, R. W. (2011) · Nature Cell Biology · doi:10.1038/ncb2390 · Cited by 379 · see citing works
Secretory Protein Biogenesis and Traffic in the Early Secretory Pathway
Barlowe, C. K., & Miller, E. A. (2013) · Genetics · doi:10.1534/genetics.112.142810 · Cited by 321 · see citing works
Protein Sorting Receptors in the Early Secretory Pathway
Dancourt, J., & Barlowe, C. K. (2010) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061608-091319 · Cited by 299 · see citing works
Roulin, P. S., Lötzerich, M., Torta, F. T., Tanner, L. B., van Kuppeveld, F. J. M., Wenk, M. R., & Greber, U. F. (2014) · Cell Host & Microbe · doi:10.1016/j.chom.2014.10.003 · Cited by 222 · see citing works
Architecture of the Mammalian GolgiPreprint
Klumperman, J. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a005181 · Cited by 209 · see citing works
Local Zones of Endoplasmic Reticulum Complexity Confine Cargo in Neuronal Dendrites
Wang, T., Hanus, C., Cui, T., Helton, T. D., Bourne, J. N., Watson, D. J., Harris, K. M., & Ehlers, M. (2012) · Cell · doi:10.1016/j.cell.2011.11.056 · Cited by 200 · see citing works
MAPK signaling to the early secretory pathway revealed by kinase/phosphatase functional screening
Farhan, H., Wendeler, M. W., Mitrović, S., Fava, E., Silberberg, Y., Sharan, R., Zerial, M., & Hauri, H. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.200912082 · Cited by 198 · see citing works
Self-citationCargo Capture and Bulk Flow in the Early Secretory Pathway
Barlowe, C. K., & Helenius, A. (2016) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-111315-125016 · Cited by 197 · see citing works
TFG-1 function in protein secretion and oncogenesis
Witte, K., Schuh, A. L., Hegermann, J., Sarkeshik, A., Mayers, J. R., Schwarze, K., Yates, J. R., Eimer, S., & Audhya, A. (2011) · Nature Cell Biology · doi:10.1038/ncb2225 · Cited by 185 · see citing works
Srinivasan, R., Pantoja, R., Moss, F. J., Mackey, E. D. W., Son, C. D., Miwa, J., & Lester, H. A. (2011) · Journal of General Physiology · doi:10.1085/jgp.201010532 · Cited by 169 · see citing works
ER exit sites – Localization and control of COPII vesicle formation
Budnik, A., & Stephens, D. J. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.10.038 · Cited by 167 · see citing works
Vesicle-mediated export from the ER: COPII coat function and regulation
D’Arcangelo, J. G., Stahmer, K. R., & Miller, E. A. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.02.003 · Cited by 147 · see citing works
Signalling to and from the secretory pathway
Farhan, H., & Rabouille, C. (2010) · Journal of Cell Science · doi:10.1242/jcs.076455 · Cited by 148 · see citing works
Self-citationRNAi screening reveals a large signaling network controlling the Golgi apparatus in human cells
Chia, J., Goh, G. Y. L., Racine, V., Ng, S., Kumar, P., & Bard, F. (2012) · Molecular Systems Biology · doi:10.1038/msb.2012.59 · Cited by 132 · see citing works
Organelle biogenesis in the endoplasmic reticulum
Joshi, A. S., Zhang, H., & Prinz, W. (2017) · Nature Cell Biology · doi:10.1038/ncb3579 · Cited by 120 · see citing works
Riguet, N., Mahul-Mellier, A.-L., Maharjan, N., Burtscher, J., Croisier, M., Knott, G., Hastings, J., Patin, A., Reiterer, V., Farhan, H., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-26684-z · Cited by 118 · see citing works
Self-citationBellucci, A., Zaltieri, M., Navarria, L., Grigoletto, J., Missale, C., & Spano, P. (2012) · Brain Research · doi:10.1016/j.brainres.2012.04.014 · Cited by 110 · see citing works
Molecular signal networks and regulating mechanisms of the unfolded protein response
Gong, J., Wang, X., Wang, T., Chen, J., Xie, X., Hu, H. Z., Yu, F., Liu, H., Jiang, X., & Fan, H. (2017) · Journal of Zhejiang University SCIENCE B · doi:10.1631/jzus.b1600043 · Cited by 109 · see citing works
Zacharogianni, M., Kondylis, V., Tang, Y., Farhan, H., Xanthakis, D., Fuchs, F., Boutros, M., & Rabouille, C. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.253 · Cited by 101 · see citing works
Self-citationCOPII collar defines the boundary between ER and ER exit site and does not coat cargo containers
Shomron, O., Nevo-Yassaf, I., Aviad, T., Yaffe, Y., Zahavi, E. E., Dukhovny, A., Perlson, E., Brodsky, I. B., Yeheskel, A., Pasmanik‐Chor, M., et al. (2021) · The Journal of Cell Biology · doi:10.1083/jcb.201907224 · Cited by 103 · see citing works
Regulation of coat assembly—sorting things out at the ER
Miller, E. A., & Barlowe, C. K. (2010) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2010.04.003 · Cited by 102 · see citing works
Zhou, X., Wu, W., Huang, L., Cheng, Y., Wei, N., Zong, J., Feng, X., Xie, Z., Chen, D., Manley, J. L., et al. (2014) · Nucleic Acids Research · doi:10.1093/nar/gkt1387 · Cited by 100 · see citing works
Lim, Y.-S., & Hwang, S. B. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.194472 · Cited by 99 · see citing works
Cracking the Glycome Encoder: Signaling, Trafficking, and Glycosylation
Bard, F., & Chia, J. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.12.004 · Cited by 98 · see citing works
Retrograde Traffic from the Golgi to the Endoplasmic ReticulumPreprint
Spang, A. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a013391 · Cited by 98 · see citing works
Cinderella story: PI4P goes from precursor to key signaling molecule
Tan, J. D., & Brill, J. A. (2013) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2013.853024 · Cited by 95 · see citing works
TANGO1 recruits Sec16 to coordinately organize ER exit sites for efficient secretion
Maeda, M., Katada, T., & Saito, K. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201703084 · Cited by 91 · see citing works
Tunnels for Protein Export from the Endoplasmic Reticulum
Raote, I., & Malhotra, V. (2021) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-080120-022017 · Cited by 82 · see citing works
Subramanian, A., Capalbo, A., Iyengar, N. R., Rizzo, R., Campli, A. D., Martino, R. D., Monte, M. L., Beccari, A. R., Yerudkar, A., Vecchio, C. D., et al. (2019) · Cell · doi:10.1016/j.cell.2019.01.035 · Cited by 81 · see citing works
Roles of SAM and DDHD domains in mammalian intracellular phospholipase A1 KIAA0725p
Inoue, H., Baba, T., Sato, S., Ohtsuki, R., Takemori, A., Watanabe, T., Tagaya, M., & Tani, K. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.02.002 · Cited by 81 · see citing works
Self-citationImpact of Lipotoxicity on Tissue “Cross Talk” and Metabolic Regulation
Montgomery, M. K., Nardo, W. D., & Watt, M. J. (2019) · Physiology · doi:10.1152/physiol.00037.2018 · Cited by 78 · see citing works
Control of Organelle Size: The Golgi Complex
Sengupta, D., & Linstedt, A. D. (2011) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100109-104003 · Cited by 73 · see citing works
Exiting the ER: what we know and what we don't.
Venditti, R., Wilson, C., & Matteis, M. D. D. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2013.08.005 · Cited by 72 · see citing works
SEC16 in COPII coat dynamics at ER exit sites
Sprangers, J., & Rabouille, C. (2015) · Biochemical Society Transactions · doi:10.1042/bst20140283 · Cited by 66 · see citing works
Silencing of Mammalian Sar1 Isoforms Reveals COPII ‐Independent Protein Sorting and Transport
Cutrona, M. B., Beznoussenko, G. V., Fusella, A., Martella, O., Moral, P., & Aa, M. (2013) · Traffic · doi:10.1111/tra.12060 · Cited by 63 · see citing works
Dynamic organization of COPII coat proteins at endoplasmic reticulum export sites in plant cells
Hanton, S. L., Matheson, L. A., Châtre, L., & Brandizzí, F. (2008) · The Plant Journal · doi:10.1111/j.1365-313x.2008.03740.x · Cited by 65 · see citing works
On vesicle formation and tethering in the ER–Golgi shuttle
Spang, A. (2009) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.03.003 · Cited by 64 · see citing works
Mechanobiology of organelles: illuminating their roles in mechanosensing and mechanotransduction
Phuyal, S., Romani, P., Dupont, S., & Farhan, H. (2023) · Trends in Cell Biology · doi:10.1016/j.tcb.2023.05.001 · Cited by 62 · see citing works
Self-citationShindiapina, P., & Barlowe, C. K. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-07-0605 · Cited by 62 · see citing works
Sec16 influences transitional ER sites by regulating rather than organizing COPII
Bharucha, N., Liu, Y., Papanikou, E., McMahon, C. T., Esaki, M., Jeffrey, P. D., Hughson, F. M., & Glick, B. S. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-04-0185 · Cited by 59 · see citing works
Evaluation of Phosphatidylinositol-4-Kinase IIIα as a Hepatitis C Virus Drug Target
Vaillancourt, F. H., Brault, M., Pilote, L., Uyttersprot, N., Gaillard, E. T., Stoltz, J. H., Knight, B. L., Pantages, L., McFarland, M., Breitfelder, S., et al. (2012) · Journal of Virology · doi:10.1128/jvi.01320-12 · Cited by 58 · see citing works
Exit from the trans-Golgi network: from molecules to mechanisms
Anitei, M., & Hoflack, B. (2011) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2011.03.013 · Cited by 57 · see citing works
COPII-mediated traffic in plants
Marti, L., Fornaciari, S., Renna, L., Stefano, G., & Brandizzí, F. (2010) · Trends in Plant Science · doi:10.1016/j.tplants.2010.05.010 · Cited by 56 · see citing works
Selective Targeting of ER Exit Sites Supports Axon Development
Aridor, M., & Fish, K. N. (2009) · Traffic · doi:10.1111/j.1600-0854.2009.00974.x · Cited by 56 · see citing works
Phosphoinositides in the Hepatitis C Virus Life Cycle
Bishé, B., Syed, G. H., & Siddiqui, A. (2012) · Viruses · doi:10.3390/v4102340 · Cited by 55 · see citing works
Balla, T., Sengupta, N., & Kim, Y. J. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2019.05.005 · Cited by 55 · see citing works
Cargo crowding contributes to sorting stringency in COPII vesicles
Gómez‐Navarro, N., Melero, A., Li, X., Jérôme Boulanger, A., Kukulski, W., & Miller, E. A. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.201806038 · Cited by 51 · see citing works
Dynamic Glycosylation Governs the Vertebrate COPII Protein Trafficking Pathway
Cox, N. J., Ünlü, G., Bisnett, B. J., Meister, T. R., Condon, B. M., Luo, P. M., Smith, T. J., Hanna, M., Chhetri, A., Soderblom, E. J., et al. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b00870 · Cited by 50 · see citing works
Sec16A is critical for both conventional and unconventional secretion of CFTR
Piao, H., Kim, J., Noh, S. H., Kweon, H., Kim, J. Y., & Lee, M. G. (2017) · Scientific Reports · doi:10.1038/srep39887 · Cited by 46 · see citing works
ER exit sites in Drosophila display abundant ER-Golgi vesicles and pearled tubes but no megacarriers
Yang, K. L., Liu, M., Feng, Z. J., Rojas, M., Zhou, L., Ke, H., & Pastor-Pareja, J. C. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109707 · Cited by 46 · see citing works
The cell biology of hepatitis C virus
Joyce, M., & Tyrrell, D. L. (2010) · Microbes and Infection · doi:10.1016/j.micinf.2009.12.012 · Cited by 45 · see citing works
Regulation of AMPA receptor trafficking and exit from the endoplasmic reticulum
Pick, J. E., & Ziff, E. B. (2018) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2018.03.004 · Cited by 44 · see citing works
Shaheen, A. (2018) · Cell Stress and Chaperones · doi:10.1007/s12192-018-0905-2 · Cited by 45 · see citing works
Faso, C., Konrad, C., Schraner, E. M., & Hehl, A. B. (2012) · Cellular Microbiology · doi:10.1111/cmi.12054 · Cited by 44 · see citing works
Pearse, B. R., Tamura, T., Sunryd, J. C., Grabowski, G. A., Kaufman, R. J., & Hebert, D. N. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.200912105 · Cited by 44 · see citing works
Self-citationPERK-Mediated Unfolded Protein Response Activation and Oxidative Stress in PARK20 Fibroblasts
Amodio, G., Moltedo, O., Fasano, D., Zerillo, L., Oliveti, M., Pietro, P. D., Faraonio, R., Barone, P., Pellecchia, M. T., Rosa, A. D., et al. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00673 · Cited by 43 · see citing works
A cascade of ER exit site assembly that is regulated by p125A and lipid signals
Klinkenberg, D., Long, K. R., Shome, K., Watkins, S. C., & Aridor, M. (2014) · Journal of Cell Science · doi:10.1242/jcs.138784 · Cited by 42 · see citing works
Dual function of cTAGE5 in collagen export from the endoplasmic reticulum
Tanabe, T., Maeda, M., Saito, K., & Katada, T. (2016) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-03-0180 · Cited by 42 · see citing works
Regulation of Sec16 levels and dynamics links proliferation and secretion
Tillmann, K. D., Reiterer, V., Baschieri, F., Hoffmann, J., Millarte, V., Hauser, M. A., Mazza, A., Atias, N., Legler, D. F., Sharan, R., et al. (2014) · Journal of Cell Science · doi:10.1242/jcs.157115 · Cited by 39 · see citing works
Self-citationCOPII gets in shape: Lessons derived from morphological aspects of early secretion
Aridor, M. (2018) · Traffic · doi:10.1111/tra.12603 · Cited by 40 · see citing works
Regulation of CFTR Biogenesis by the Proteostatic Network and Pharmacological Modulators
Estabrooks, S. K., & Brodsky, J. L. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21020452 · Cited by 40 · see citing works
Traffic of p24 Proteins and COPII Coat Composition Mutually Influence Membrane Scaffolding
D’Arcangelo, J. G., Crissman, J. R., Pagant, S., Čopič, A., Latham, C. F., Snapp, E. L., & Miller, E. A. (2015) · Current Biology · doi:10.1016/j.cub.2015.03.029 · Cited by 40 · see citing works
Mechanical strain stimulates COPII‐dependent secretory trafficking via Rac1
Phuyal, S., Djaerff, E., Roux, A. L., Baker, M. J., Fankhauser, D., Mahdizadeh, S. J., Reiterer, V., Parizadeh, A., Felder, E., Kahlhofer, J., et al. (2022) · The EMBO Journal · doi:10.15252/embj.2022110596 · Cited by 39 · see citing works
Self-citationEndoplasmic Reticulum stress reduces COPII vesicle formation and modifies Sec23a cycling at ERESs
Amodio, G., Venditti, R., Matteis, M. A. D., Moltedo, O., Pignataro, P., & Remondelli, P. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.08.021 · Cited by 39 · see citing works
Spatial Modeling of Vesicle Transport and the Cytoskeleton: The Challenge of Hitting the Right Road
Klann, M., Koeppl, H., & Reuss, M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0029645 · Cited by 36 · see citing works
TANGO1 membrane helices create a lipid diffusion barrier at curved membranes
Raote, I., Ernst, A. M., Campelo, F., Rothman, J. E., Pincet, F., & Malhotra, V. (2020) · eLife · doi:10.7554/elife.57822 · Cited by 36 · see citing works
Liu, F., Lu, Y., Pieuchot, L., Dhavale, T., & Jedd, G. (2011) · Developmental Cell · doi:10.1016/j.devcel.2011.08.004 · Cited by 35 · see citing works
Hanna, M. G., Peotter, J. L., Frankel, E. B., & Audhya, A. (2018) · BioEssays · doi:10.1002/bies.201800004 · Cited by 35 · see citing works
Emergent properties of proteostasis-COPII coupled systems in human health and disease
Routledge, K. E., Gupta, V. R., & Balch, W. E. (2010) · Molecular Membrane Biology · doi:10.3109/09687688.2010.524894 · Cited by 33 · see citing works
Dopey1-Mon2 complex binds to dual-lipids and recruits kinesin-1 for membrane trafficking
Mahajan, D., Tie, H. C., Chen, B., & Lü, L. (2019) · Nature Communications · doi:10.1038/s41467-019-11056-5 · Cited by 32 · see citing works
Export Control: Post-transcriptional Regulation of the COPII Trafficking Pathway
Bisnett, B. J., Condon, B. M., Lamb, C. H., Georgiou, G. R., & Boyce, M. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.618652 · Cited by 30 · see citing works
Sec16 alternative splicing dynamically controls COPII transport efficiency
Wilhelmi, I., Kanski, R., Neumann, A., Herdt, O., Hoff, F., Jacob, R., Preußner, M., & Heyd, F. (2016) · Nature Communications · doi:10.1038/ncomms12347 · Cited by 31 · see citing works
Crosstalk of Autophagy and the Secretory Pathway and Its Role in Diseases
Zahoor, M., & Farhan, H. (2018) · International review of cytology · doi:10.1016/bs.ircmb.2017.12.004 · Cited by 30 · see citing works
Self-citationA tango for coats and membranes: New insights into ER-to-Golgi traffic
Aridor, M. (2022) · Cell Reports · doi:10.1016/j.celrep.2021.110258 · Cited by 29 · see citing works
Ilboudo, A., Nault, J., Dubois‐Pot‐Schneider, H., Corlu, A., Zucman‐Rossi, J., Samson, M., & Seyec, J. L. (2014) · BMC Cancer · doi:10.1186/1471-2407-14-7 · Cited by 29 · see citing works
Poliovirus Infection Transiently Increases COPII Vesicle Budding
Trahey, M., Oh, H. S., Cameron, C. E., & Hay, J. (2012) · Journal of Virology · doi:10.1128/jvi.01159-12 · Cited by 27 · see citing works
Li, Z., Tang, X., Li, J., & He, Y. (2021) · Functional & Integrative Genomics · doi:10.1007/s10142-021-00779-8 · Cited by 26 · see citing works
Want to leave the ER? We offer vesicles, tubules, and tunnels
Phuyal, S., & Farhan, H. (2021) · The Journal of Cell Biology · doi:10.1083/jcb.202104062 · Cited by 25 · see citing works
Self-citationER arrival sites for COPI vesicles localize to hotspots of membrane trafficking
Schröter, S., Beckmann, S., & Schmitt, H. D. (2016) · The EMBO Journal · doi:10.15252/embj.201592873 · Cited by 22 · see citing works
Millarte, V., Boncompain, G., Tillmann, K. D., Perez, F., Sztul, E. S., & Farhan, H. (2015) · Molecular Biology of the Cell · doi:10.1091/mbc.e15-03-0178 · Cited by 19 · see citing works
Self-citationStrub, M. D., & McCray, P. B. (2020) · Genes · doi:10.3390/genes11050546 · Cited by 17 · see citing works
Shi, H., Yuan, M., Cai, J., Lan, L., Wang, Y., Wang, W., Zhou, J., Wang, B., Yu, W., Dong, Z., et al. (2024) · Journal of Translational Medicine · doi:10.1186/s12967-024-05098-7 · Cited by 18 · see citing works
Sec16 Determines the Size and Functioning of the Golgi in the Protist Parasite, Trypanosoma brucei
Sealey‐Cardona, M., Schmidt, K., Demmel, L., Hirschmugl, T., Gesell, T., Dong, G., & Warren, G. (2014) · Traffic · doi:10.1111/tra.12170 · Cited by 18 · see citing works
New approaches for solving old problems in neuronal protein trafficking
Bourke, A. M., Bowen, A. B., & Kennedy, M. J. (2018) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2018.04.004 · Cited by 16 · see citing works
A Modeling Approach to the Self-Assembly of the Golgi Apparatus
Kühnle, J., Shillcock, J. C., Mouritsen, O. G., & Weiß, M. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2010.03.035 · Cited by 17 · see citing works
Proximity Profiling of the CFTR Interaction Landscape in Response to Orkambi
Iazzi, M., Astori, A., St‐Germain, J. R., Raught, B., & Gupta, G. D. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23052442 · Cited by 16 · see citing works
ER exit in physiology and disease
Robinson, C. M., Duggan, A., & Forrester, A. R. (2024) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2024.1352970 · Cited by 15 · see citing works
Yonemura, Y., Li, X., Müller, K., Krämer, A., Atigbire, P., Mentrup, T., Feuerhake, T., Kroll, T. C., Shomron, O., Nohl, R., et al. (2016) · Journal of Cell Science · doi:10.1242/jcs.186163 · Cited by 16 · see citing works
Amodio, G., Margarucci, L., Moltedo, O., Casapullo, A., & Remondelli, P. (2017) · The Open Biochemistry Journal · doi:10.2174/1874091x01711010036 · Cited by 16 · see citing works
Yeong, F. M. (2013) · BioEssays · doi:10.1002/bies.201200144 · Cited by 16 · see citing works
On the nature of the plant ER exit sites
McGinness, A. J., Schoberer, J., Pain, C., Brandizzí, F., & Kriechbaumer, V. (2022) · Frontiers in Plant Science · doi:10.3389/fpls.2022.1010569 · Cited by 15 · see citing works
Wong, M.-T., & Chen, S. S. (2017) · Journal of Virology · doi:10.1128/jvi.00355-17 · Cited by 14 · see citing works
Towards a unified framework for the function of endoplasmic reticulum exit sites
Farhan, H., Raote, I., Campelo, F., Ge, L., Hirschberg, K., Forrester, A. R., Zanetti, G., Lippincott‐Schwartz, J., Pastor-Pareja, J. C., Perez, F., et al. (2025) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-025-00899-0 · Cited by 12 · see citing works
Self-citationWu, Y. L., Guo, X. P., Kanemoto, S., Maeoka, Y., Saito, A., Asada, R., Matsuhisa, K., Ohtake, Y., Imaizumi, K., & Kaneko, M. (2018) · PLoS ONE · doi:10.1371/journal.pone.0190407 · Cited by 13 · see citing works
Regulation of traffic and organelle architecture of the ER-Golgi interface by signal transduction
Tillmann, K. D., Millarte, V., & Farhan, H. (2013) · Histochemistry and Cell Biology · doi:10.1007/s00418-013-1118-5 · Cited by 12 · see citing works
Self-citationRagagnin, A., Sundaramoorthy, V., Farzana, F., Gautam, S., Saravanabavan, S., Takalloo, Z., Mehta, P. M., Do‐Ha, D., Parakh, S., Shadfar, S., et al. (2023) · Scientific Reports · doi:10.1038/s41598-023-46802-9 · Cited by 11 · see citing works
Allmen, E. U.-V., Rippl, A., Farhan, H., & Legler, D. F. (2018) · Journal of Leukocyte Biology · doi:10.1002/jlb.2vma1217-492r · Cited by 11 · see citing works
Self-citationqTAG: an adaptable plasmid scaffold for CRISPR-based endogenous tagging
Philip, R., Sharma, A., Matellan, L., Erpf, A. C., Hsu, W.-H., Tkach, J. M., Wyatt, H. D. M., & Pelletier, L. (2024) · The EMBO Journal · doi:10.1038/s44318-024-00337-5 · Cited by 10 · see citing works
- Authors
- Farhan, H., Weiss, M., Tani, K., Kaufman, R. J., & Hauri, H.
- Affiliations
- University of Basel (CH)
- German Cancer Research Center (DE)
- Tokyo University of Pharmacy and Life Sciences (JP)
- Howard Hughes Medical Institute (US)
- Corresponding author
- Hauri, Hans‐Peter
- Venue
- The EMBO Journal
- Published
- 2008-07-24
- Volume
- 27
- Issue
- 15
- Pages
- 2043-2054
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC2516884
- OpenAlex
- W2163308914
- Cited by
- 138
- References
- 35
- Citations by year
- 2026: 3 · 2025: 5 · 2024: 9 · 2023: 9 · 2022: 8 · 2021: 10 · 2020: 4 · 2019: 7 · 2018: 8 · 2017: 7 · 2016: 8 · 2015: 7 · 2014: 6 · 2013: 12 · 2012: 10
- FWCI
- 3.65
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- The EMBO Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Deep Blue (University of Michigan) (submittedVersion)
- Funders
- National Science Foundation
- Howard Hughes Medical Institute
- Yale University
- Universität Basel
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung
- Austrian Science Fund
- Universität Wien
- Medizinische Universität Wien
- National Institutes of Health (HL052173, DK042394)
- National Heart, Lung, and Blood Institute (R01HL052173, P01HL057346)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK042394, R37DK042394)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
- Life Sciences › Neuroscience › Sensory Systems › Ion Channels and Receptors
- Keywords
- endoplasmic reticulum exit sites, cargo load, phosphatidylinositol 4-phosphate, Sec16, PI4KIIIα, unfolded protein response, COPII, mathematical modeling, ER export
- MeSH terms
- Endoplasmic Reticulum, Golgi Apparatus, HeLa Cells, Humans, Intracellular Membranes, Models, Biological, Signal Transduction, Minor Histocompatibility Antigens, Protein Folding, Phosphotransferases (Alcohol Group Acceptor), Phosphatidylinositol Phosphates, Protein Transport, Secretory Vesicles, COP-Coated Vesicles, Vesicular Transport Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
