Abstract
Secretory proteins are transported to the Golgi complex in vesicles that bud from the endoplasmic reticulum. The cytoplasmic coat protein complex II (COPII) is responsible for cargo sorting and vesicle morphogenesis. COPII was first described in Saccharomyces cerevisiae, but its basic function is conserved throughout all eukaryotes. Nevertheless, the COPII coat has adapted to the higher complexity of mammalian physiology, achieving more sophisticated levels of secretory regulation. In this review we cover aspects of mammalian COPII-mediated regulation of secretion, in particular related to the function of COPII paralogues, the spatial organization of cargo export and the role of accessory proteins.
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Change history
06 January 2012
In the version of this review initially published online and in print, the key in figure 2 was incorrect. These errors have been corrected in the HTML and PDF versions of the article.
References
Barlowe, C. et al. COPII: a membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum. Cell 77, 895–907 (1994).
Orci, L. et al. Mammalian Sec23p homologue is restricted to the endoplasmic reticulum transitional cytoplasm. Proc. Natl Acad. Sci. USA 88, 8611–8615 (1991).
Bannykh, S. I., Rowe, T. & Balch, W. E. The organization of endoplasmic reticulum export complexes. J. Cell Biol. 135, 19–35 (1996).
Goldberg, J. Structural basis for activation of ARF GTPase: mechanisms of guanine nucleotide exchange and GTP-myristoyl switching. Cell 95, 237–248 (1998).
Huang, M. et al. Crystal structure of Sar1-GDP at 1.7 Å resolution and the role of the NH2 terminus in ER export. J. Cell Biol. 155, 937–948 (2001).
Bi, X., Corpina, R. A. & Goldberg, J. Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coat. Nature 419, 271–277 (2002).
Rao, Y. et al. An open conformation of switch I revealed by Sar1-GDP crystal structure at low Mg2+. Biochem. Biophys. Res. Commun. 348, 908–915 (2006).
Antonny, B., Beraud-Dufour, S., Chardin, P. & Chabre, M. N-terminal hydrophobic residues of the G-protein ADP-ribosylation factor-1 insert into membrane phospholipids upon GDP to GTP exchange. Biochemistry 36, 4675–4684 (1997).
Matsuoka, K. et al. COPII-coated vesicle formation reconstituted with purified coat proteins and chemically defined liposomes. Cell 93, 263–275 (1998).
Lee, M. C. et al. Sar1p N-terminal helix initiates membrane curvature and completes the fission of a COPII vesicle. Cell 122, 605–617 (2005).
Miller, E., Antonny, B., Hamamoto, S. & Schekman, R. Cargo selection into COPII vesicles is driven by the Sec24p subunit. EMBO J. 21, 6105–6113 (2002).
Matsuoka, K., Schekman, R., Orci, L. & Heuser, J. E. Surface structure of the COPII-coated vesicle. Proc. Natl Acad. Sci. USA 98, 13705–13709 (2001).
Fath, S., Mancias, J. D., Bi, X. & Goldberg, J. Structure and organization of coat proteins in the COPII cage. Cell 129, 1325–1336 (2007).
Stagg, S. M. et al. Structure of the Sec13/31 COPII coat cage. Nature 439, 234–238 (2006).
Stagg, S. M. et al. Structural basis for cargo regulation of COPII coat assembly. Cell 134, 474–484 (2008).
Antonny, B., Madden, D., Hamamoto, S., Orci, L. & Schekman, R. Dynamics of the COPII coat with GTP and stable analogues. Nat. Cell Biol. 3, 531–537 (2001).
Sato, K. & Nakano, A. Dissection of COPII subunit-cargo assembly and disassembly kinetics during Sar1p-GTP hydrolysis. Nat. Struct. Mol. Biol. 12, 167–174 (2005).
Forster, R. et al. Secretory cargo regulates the turnover of COPII subunits at single ER exit sites. Curr. Biol. 16, 173–179 (2006).
Cai, H. et al. TRAPPI tethers COPII vesicles by binding the coat subunit Sec23. Nature 445, 941–944 (2007).
Lord, C. et al. Sequential interactions with Sec23 control the direction of vesicle traffic. Nature 473, 181–186 (2011).
Bi, X., Mancias, J. D. & Goldberg, J. Insights into COPII coat nucleation from the structure of Sec23.Sar1 complexed with the active fragment of Sec31. Dev. Cell 13, 635–645 (2007).
Fromme, J. C. et al. The genetic basis of a craniofacial disease provides insight into COPII coat assembly. Dev. Cell 13, 623–634 (2007).
Fromme, J. C., Orci, L. & Schekman, R. Coordination of COPII vesicle trafficking by Sec23. Trends Cell Biol. 18, 330–336 (2008).
Lang, M. R., Lapierre, L. A., Frotscher, M., Goldenring, J. R. & Knapik, E. W. Secretory COPII coat component Sec23a is essential for craniofacial chondrocyte maturation. Nat. Genet. 38, 1198–1203 (2006).
Bianchi, P. et al. Congenital dyserythropoietic anemia type II (CDAII) is caused by mutations in the SEC23B gene. Hum. Mutat. 30, 1292–1298 (2009).
Schwarz, K. et al. Mutations affecting the secretory COPII coat component SEC23B cause congenital dyserythropoietic anemia type II. Nat. Genet. 41, 936–940 (2009).
Miller, E. A. et al. Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles. Cell 114, 497–509 (2003).
Wendeler, M. W., Paccaud, J. P. & Hauri, H. P. Role of Sec24 isoforms in selective export of membrane proteins from the endoplasmic reticulum. EMBO Rep. 8, 258–264 (2007).
Demmel, L. et al. Differential selection of Golgi proteins by COPII Sec24 isoforms in procyclic T. brucei. Traffic 12, 1575–1591 (2011).
Mancias, J. D. & Goldberg, J. The transport signal on Sec22 for packaging into COPII-coated vesicles is a conformational epitope. Mol. Cell 26, 403–414 (2007).
Mancias, J. D. & Goldberg, J. Structural basis of cargo membrane protein discrimination by the human COPII coat machinery. EMBO J. 27, 2918–2928 (2008).
Mossessova, E., Bickford, L. C. & Goldberg, J. SNARE selectivity of the COPII coat. Cell 114, 483–495 (2003).
Sucic, S. et al. The serotonin transporter is an exclusive client of the coat protein complex II (COPII) component SEC24C. J. Biol. Chem. 286, 16482–16490 (2011).
Farhan, H. et al. Concentrative export from the endoplasmic reticulum of the gamma-aminobutyric acid transporter 1 requires binding to SEC24D. J. Biol. Chem. 282, 7679–7689 (2007).
Merte, J. et al. Sec24b selectively sorts Vangl2 to regulate planar cell polarity during neural tube closure. Nat. Cell Biol. 12, 41–46 (2010).
Wansleeben, C. et al. Planar cell polarity defects and defective Vangl2 trafficking in mutants for the COPII gene Sec24b. Development 137, 1067–1073 (2010).
Zeuschner, D. et al. Immuno-electron tomography of ER exit sites reveals the existence of free COPII-coated transport carriers. Nat. Cell Biol. 8, 377–383 (2006).
Appenzeller-Herzog, C. & Hauri, H. P. The ER-Golgi intermediate compartment (ERGIC): in search of its identity and function. J. Cell Sci. 119, 2173–2183 (2006).
Novick, P., Field, C. & Schekman, R. Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway. Cell 21, 205–215 (1980).
Connerly, P. L. et al. Sec16 is a determinant of transitional ER organization. Curr. Biol. 15, 1439–1447 (2005).
Watson, P., Townley, A. K., Koka, P., Palmer, K. J. & Stephens, D. J. Sec16 defines endoplasmic reticulum exit sites and is required for secretory cargo export in mammalian cells. Traffic 7, 1678–1687 (2006).
Iinuma, T. et al. Mammalian Sec16/p250 plays a role in membrane traffic from the endoplasmic reticulum. J. Biol. Chem. 282, 17632–17639 (2007).
Bhattacharyya, D. & Glick, B. S. Two mammalian Sec16 homologues have nonredundant functions in endoplasmic reticulum (ER) export and transitional ER organization. Mol. Biol. Cell 18, 839–849 (2007).
Shindiapina, P. & Barlowe, C. Requirements for transitional endoplasmic reticulum site structure and function in Saccharomyces cerevisiae. Mol. Biol. Cell 21, 1530–1545 (2010).
Hughes, H. et al. Organisation of human ER-exit sites: requirements for the localisation of Sec16 to transitional ER. J. Cell Sci. 122, 2924–2934 (2009).
Ivan, V. et al. Drosophila Sec16 mediates the biogenesis of tER sites upstream of Sar1 through an arginine-rich motif. Mol. Biol. Cell 19, 4352–4365 (2008).
Espenshade, P., Gimeno, R. E., Holzmacher, E., Teung, P. & Kaiser, C. A. Yeast SEC16 gene encodes a multidomain vesicle coat protein that interacts with Sec23p. J. Cell Biol. 131, 311–324 (1995).
Gimeno, R. E., Espenshade, P. & Kaiser, C. A. COPII coat subunit interactions: Sec24p and Sec23p bind to adjacent regions of Sec16p. Mol. Biol. Cell 7, 1815–1823 (1996).
Shaywitz, D. A., Espenshade, P. J., Gimeno, R. E. & Kaiser, C. A. COPII subunit interactions in the assembly of the vesicle coat. J. Biol. Chem. 272, 25413–25416 (1997).
Whittle, J. R. & Schwartz, T. U. Structure of the Sec13-Sec16 edge element, a template for assembly of the COPII vesicle coat. J. Cell Biol. 190, 347–361 (2010).
Supek, F., Madden, D. T., Hamamoto, S., Orci, L. & Schekman, R. Sec16p potentiates the action of COPII proteins to bud transport vesicles. J. Cell Biol. 158, 1029–1038 (2002).
Hughes, H. & Stephens, D. J. Sec16A defines the site for vesicle budding from the endoplasmic reticulum on exit from mitosis. J. Cell Sci. 123, 4032–4038 (2010).
Witte, K. et al. TFG-1 function in protein secretion and oncogenesis. Nat. Cell Biol. 13, 550–558 (2011).
Yonekawa, S. et al. Sec16B is involved in the endoplasmic reticulum export of the peroxisomal membrane biogenesis factor peroxin 16 (Pex16) in mammalian cells. Proc. Natl Acad Sci USA 108, 12746–12751 (2011).
Pathre, P. et al. Activation of phospholipase D by the small GTPase Sar1p is required to support COPII assembly and ER export. EMBO J. 22, 4059–4069 (2003).
Blumental-Perry, A. et al. Phosphatidylinositol 4-phosphate formation at ER exit sites regulates ER export. Dev. Cell 11, 671–682 (2006).
Shimoi, W. et al. p125 is localized in endoplasmic reticulum exit sites and involved in their organization. J. Biol. Chem. 280, 10141–10148 (2005).
Ong, Y. S., Tang, B. L., Loo, L. S. & Hong, W. p125A exists as part of the mammalian Sec13/Sec31 COPII subcomplex to facilitate ER–Golgi transport. J. Cell Biol. 190, 331–345 (2010).
Farhan, H., Weiss, M., Tani, K., Kaufman, R. J. & Hauri, H. P. Adaptation of endoplasmic reticulum exit sites to acute and chronic increases in cargo load. EMBO J. 27, 2043–2054 (2008).
Presley, J. F. et al. ER-to-Golgi transport visualized in living cells. Nature 389, 81–85 (1997).
Lippincott-Schwartz, J., Cole, N. B., Marotta, A., Conrad, P. A. & Bloom, G. S. Kinesin is the motor for microtubule-mediated Golgi-to-ER membrane traffic. J. Cell Biol. 128, 293–306 (1995).
Scales, S. J., Pepperkok, R. & Kreis, T. E. Visualization of ER-to-Golgi transport in living cells reveals a sequential mode of action for COPII and COPI. Cell 90, 1137–1148 (1997).
Hammond, A. T. & Glick, B. S. Dynamics of transitional endoplasmic reticulum sites in vertebrate cells. Mol. Biol. Cell 11, 3013–3030 (2000).
Watson, P., Forster, R., Palmer, K. J., Pepperkok, R. & Stephens, D. J. Coupling of ER exit to microtubules through direct interaction of COPII with dynactin. Nat. Cell Biol. 7, 48–55 (2005).
Heinzer, S., Worz, S., Kalla, C., Rohr, K. & Weiss, M. A model for the self-organization of exit sites in the endoplasmic reticulum. J. Cell Sci. 121, 55–64 (2008).
Srinivasan, R. et al. Nicotine up-regulates alpha4beta2 nicotinic receptors and ER exit sites via stoichiometry-dependent chaperoning. J. Gen. Physiol. 137, 59–79 (2011).
Farhan, H. et al. MAPK signaling to the early secretory pathway revealed by kinase/phosphatase functional screening. J. Cell Biol. 189, 997–1011 (2010).
Zacharogianni, M. et al. ERK7 is a negative regulator of protein secretion in response to amino-acid starvation by modulating Sec16 membrane association. EMBO J. 30, 3684–3700 (2011).
Aridor, M. & Fish, K. N. Selective targeting of ER exit sites supports axon development. Traffic 10, 1669–1684 (2009).
Kamiya, Y. et al. Molecular basis of sugar recognition by the human L-type lectins ERGIC-53, VIPL, and VIP36. J. Biol. Chem. 283, 1857–1861 (2008).
Moussalli, M. et al. Mannose-dependent endoplasmic reticulum (ER)–Golgi intermediate compartment-53-mediated ER to Golgi trafficking of coagulation factors V and VIII. J. Biol. Chem. 274, 32539–32542 (1999).
Zhang, B. et al. Bleeding due to disruption of a cargo-specific ER-to-Golgi transport complex. Nat. Genet. 34, 220–225 (2003).
Nyfeler, B., Zhang, B., Ginsburg, D., Kaufman, R. J. & Hauri, H. P. Cargo selectivity of the ERGIC-53/MCFD2 transport receptor complex. Traffic 7, 1473–1481 (2006).
Nyfeler, B. et al. Identification of ERGIC-53 as an intracellular transport receptor of alpha1-antitrypsin. J. Cell Biol. 180, 705–712 (2008).
Bonnon, C., Wendeler, M. W., Paccaud, J. P. & Hauri, H. P. Selective export of human GPI-anchored proteins from the endoplasmic reticulum. J. Cell Sci. 123, 1705–1715 (2010).
Castillon, G. A. et al. The yeast p24 complex regulates GPI-anchored protein transport and quality control by monitoring anchor remodeling. Mol. Biol. Cell 22, 2924–2936 (2011).
Fujita, M. et al. Sorting of GPI-anchored proteins into ER exit sites by p24 proteins is dependent on remodeled GPI. J. Cell Biol. 194, 61–75 (2011).
Takida, S., Maeda, Y. & Kinoshita, T. Mammalian GPI-anchored proteins require p24 proteins for their efficient transport from the ER to the plasma membrane. Biochem. J. 409, 555–562 (2008).
Springer, S. et al. The p24 proteins are not essential for vesicular transport in Saccharomyces cerevisiae. Proc. Natl Acad. Sci. USA 97, 4034–4039 (2000).
Denzel, A. et al. The p24 family member p23 is required for early embryonic development. Curr. Biol. 10, 55–58 (2000).
Lambert, G. et al. Control of cystic fibrosis transmembrane conductance regulator expression by BAP31. J. Biol. Chem. 276, 20340–20345 (2001).
Abe, F., Van Prooyen, N., Ladasky, J. J. & Edidin, M. Interaction of Bap31 and MHC class I molecules and their traffic out of the endoplasmic reticulum. J. Immunol. 182, 4776–4783 (2009).
Annaert, W. G., Becker, B., Kistner, U., Reth, M. & Jahn, R. Export of cellubrevin from the endoplasmic reticulum is controlled by BAP31. J. Cell Biol. 139, 1397–1410 (1997).
Brown, M. S. & Goldstein, J. L. Cholesterol feedback: from Schoenheimer's bottle to Scap's MELADL. J. Lipid Res. 50, Suppl. S15–S27 (2009).
Yang, T. et al. Crucial step in cholesterol homeostasis: sterols promote binding of SCAP to INSIG-1, a membrane protein that facilitates retention of SREBPs in ER. Cell 110, 489–500 (2002).
Espenshade, P. J., Li, W. P. & Yabe, D. Sterols block binding of COPII proteins to SCAP, thereby controlling SCAP sorting in ER. Proc. Natl Acad. Sci. USA 99, 11694–11699 (2002).
Sun, L. P., Seemann, J., Goldstein, J. L. & Brown, M. S. Sterol-regulated transport of SREBPs from endoplasmic reticulum to Golgi: Insig renders sorting signal in Scap inaccessible to COPII proteins. Proc. Natl Acad. Sci. USA 104, 6519–6526 (2007).
DeBose-Boyd, R. A. et al. Transport-dependent proteolysis of SREBP: relocation of site-1 protease from Golgi to ER obviates the need for SREBP transport to Golgi. Cell 99, 703–712 (1999).
Kuwana, T., Peterson, P. A. & Karlsson, L. Exit of major histocompatibility complex class II-invariant chain p35 complexes from the endoplasmic reticulum is modulated by phosphorylation. Proc. Natl Acad. Sci. USA 95, 1056–1061 (1998).
O'Kelly, I., Butler, M. H., Zilberberg, N. & Goldstein, S. A. Forward transport. 14-3-3 binding overcomes retention in endoplasmic reticulum by dibasic signals. Cell 111, 577–588 (2002).
Chen, Y. T., Stewart, D. B. & Nelson, W. J. Coupling assembly of the E-cadherin/beta-catenin complex to efficient endoplasmic reticulum exit and basal-lateral membrane targeting of E-cadherin in polarized MDCK cells. J. Cell Biol. 144, 687–699 (1999).
Nakamura, T. et al. PX-RICS mediates ER-to-Golgi transport of the N-cadherin/beta-catenin complex. Genes Dev. 22, 1244–1256 (2008).
Wang, J. et al. Dishevelled genes mediate a conserved mammalian PCP pathway to regulate convergent extension during neurulation. Development 133, 1767–1778 (2006).
Simons, M. et al. Electrochemical cues regulate assembly of the Frizzled/Dishevelled complex at the plasma membrane during planar epithelial polarization. Nat. Cell Biol. 11, 286–294 (2009).
Das, S. et al. ERp29 restricts Connexin43 oligomerization in the endoplasmic reticulum. Mol. Biol. Cell 20, 2593–2604 (2009).
Aryal, R. P., Ju, T. & Cummings, R. D. The endoplasmic reticulum chaperone Cosmc directly promotes in vitro folding of T-synthase. J. Biol. Chem. 285, 2456–2462 (2010).
Schindler, A. J. & Schekman, R. In vitro reconstitution of ER-stress induced ATF6 transport in COPII vesicles. Proc. Natl Acad. Sci. USA 106, 17775–17780 (2009).
Shen, J., Chen, X., Hendershot, L. & Prywes, R. ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals. Dev. Cell 3, 99–111 (2002).
Saito, K. et al. TANGO1 facilitates cargo loading at endoplasmic reticulum exit sites. Cell 136, 891–902 (2009).
Bachinger, H. P., Doege, K. J., Petschek, J. P., Fessler, L. I. & Fessler, J. H. Structural implications from an electronmicroscopic comparison of procollagen V with procollagen I, pC-collagen I, procollagen IV, and a Drosophila procollagen. J. Biol. Chem. 257, 14590–14592 (1982).
Zilversmit, D. B. Formation and transport of chylomicrons. Fed. Proc. 26, 1599–1605 (1967).
Aridor, M., Bannykh, S. I., Rowe, T. & Balch, W. E. Sequential coupling between COPII and COPI vesicle coats in endoplasmic reticulum to Golgi transport. J. Cell Biol. 131, 875–893 (1995).
Bonfanti, L. et al. Procollagen traverses the Golgi stack without leaving the lumen of cisternae: evidence for cisternal maturation. Cell 95, 993–1003 (1998).
Townley, A. K. et al. Efficient coupling of Sec23–Sec24 to Sec13–Sec31 drives COPII-dependent collagen secretion and is essential for normal craniofacial development. J. Cell Sci. 121, 3025–3034 (2008).
Wilson, D. G. et al. Global defects in collagen secretion in a Mia3/TANGO1 knockout mouse. J. Cell Biol. 193, 935–951 (2011).
Saito, K. et al. cTAGE5 mediates collagen secretion through interaction with TANGO1 at endoplasmic reticulum exit sites. Mol. Biol. Cell 22, 2301–2308 (2011).
Malhotra, V. & Erlmann, P. Protein export at the ER: loading big collagens into COPII carriers. EMBO J. 30, 3475–3480 (2011).
Boyadjiev, S. A. et al. A novel dysmorphic syndrome with open calvarial sutures and sutural cataracts maps to chromosome 14q13–q21. Hum. Genet. 113, 1–9 (2003).
Boyadjiev, S. A. et al. Cranio-lenticulo-sutural dysplasia is caused by a SEC23A mutation leading to abnormal endoplasmic-reticulum-to-Golgi trafficking. Nat. Genet. 38, 1192–1197 (2006).
Saito, A. et al. Regulation of endoplasmic reticulum stress response by a BBF2H7-mediated Sec23a pathway is essential for chondrogenesis. Nat. Cell Biol. 11, 1197–1204 (2009).
Mironov, A. A. et al. ER-to-Golgi carriers arise through direct en bloc protrusion and multistage maturation of specialized ER exit domains. Dev. Cell 5, 583–594 (2003).
Jones, B. et al. Mutations in a Sar1 GTPase of COPII vesicles are associated with lipid absorption disorders. Nat. Genet. 34, 29–31 (2003).
Treepongkaruna, S. et al. Novel missense mutations of SAR1B gene in an infant with chylomicron retention disease. J. Pediatr. Gastroenterol. Nutr. 48, 370–373 (2009).
Silvain, M. et al. Anderson's disease (chylomicron retention disease): a new mutation in the SARA2 gene associated with muscular and cardiac abnormalities. Clin. Genet. 74, 546–552 (2008).
Levy, E. et al. Expression of Sar1b enhances chylomicron assembly and key components of the coat protein complex ii system driving vesicle budding. Arterioscler. Thromb. Vasc. Biol. 31, 2692–2699 (2011).
Siddiqi, S. A., Gorelick, F. S., Mahan, J. T. & Mansbach, C. M. II COPII proteins are required for Golgi fusion but not for endoplasmic reticulum budding of the pre-chylomicron transport vesicle. J. Cell Sci. 116, 415–427 (2003).
Siddiqi, S. et al. A novel multiprotein complex is required to generate the prechylomicron transport vesicle from intestinal ER. J. Lipid Res. 51, 1918–1928 (2010).
Siddiqi, S., Siddiqi, S. A. & Mansbach, C. M. II Sec24C is required for docking the prechylomicron transport vesicle with the Golgi. J. Lipid Res. 51, 1093–1100 (2010).
Bacia, K. et al. Multibudded tubules formed by COPII on artificial liposomes. Sci. Rep. 1, 17 (2011).
O'Donnell, J., Maddox, K. & Stagg, S. The structure of a COPII tubule. J. Struct. Biol. 173, 358–364 (2011).
Kim, W. et al. Systematic and quantitative assessment of the ubiquitin-modified proteome. Mol. Cell 44, 325–340 (2011).
la Cour, J. M., Mollerup, J. & Berchtold, M. W. ALG-2 oscillates in subcellular localization, unitemporally with calcium oscillations. Biochem. Biophys. Res. Commun. 353, 1063–1067 (2007).
Yamasaki, A., Tani, K., Yamamoto, A., Kitamura, N. & Komada, M. The Ca2+-binding protein ALG-2 is recruited to endoplasmic reticulum exit sites by Sec31A and stabilizes the localization of Sec31A. Mol. Biol. Cell 17, 4876–4887 (2006).
Bentley, M. et al. Vesicular calcium regulates coat retention, fusogenicity, and size of pre-Golgi intermediates. Mol. Biol. Cell 21, 1033–1046 (2010).
Shibata, H. et al. The ALG-2 binding site in Sec31A influences the retention kinetics of Sec31A at the endoplasmic reticulum exit sites as revealed by live-cell time-lapse imaging. Biosci. Biotechnol. Biochem. 74, 1819–1826 (2010).
Shibata, H., Suzuki, H., Yoshida, H. & Maki, M. ALG-2 directly binds Sec31A and localizes at endoplasmic reticulum exit sites in a Ca2+-dependent manner. Biochem. Biophys. Res. Commun. 353, 756–763 (2007).
Acknowledgements
We thank S. K. Lam, A. Fernandes and J. McKenzie for critical reading of the manuscript and discussions. G.Z. and K.B.P. are Human Frontier Science Program postdoctoral fellows. R.S. is a Senior Fellow of the UC Berkeley Miller Institute and is supported as an Investigator of the Howard Hughes Medical Institute.
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Zanetti, G., Pahuja, K., Studer, S. et al. COPII and the regulation of protein sorting in mammals. Nat Cell Biol 14, 20–28 (2012). https://doi.org/10.1038/ncb2390
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