Genetically Encoded Fluorescent Tools: Shining a Little Light on ER-to-Golgi Transport

Overview

Journal Free Radic Biol Med

Specialties Biochemistry
Biology
General Medicine

Date 2022 Mar 10

PMID 35272000

Authors

Danette Kowal Seiler

Jesse C Hay

Affiliations

Soon will be listed here.

Abstract

Since the first fluorescent proteins (FPs) were identified and isolated over fifty years ago, FPs have become commonplace yet indispensable tools for studying the constitutive secretory pathway in live cells. At the same time, genetically encoded chemical tags have provided a new use for much older fluorescent dyes. Innovation has also produced several specialized methods to allow synchronous release of cargo proteins from the endoplasmic reticulum (ER), enabling precise characterization of sequential trafficking steps in the secretory pathway. Without the constant innovation of the researchers who design these tools to control, image, and quantitate protein secretion, major discoveries about ER-to-Golgi transport and later stages of the constitutive secretory pathway would not have been possible. We review many of the tools and tricks, some 25 years old and others brand new, that have been successfully implemented to study ER-to-Golgi transport in intact and living cells.

Citing Articles

Steady-state regulation of COPII-dependent secretory cargo sorting by inositol trisphosphate receptors, calcium, and penta EF hand proteins.

Held A, Lapka J, Sargeant J, Hojanazarova J, Shaheen A, Galindo S J Biol Chem. 2023; 299(12):105471.

PMID: 37979918 PMC: 10750190. DOI: 10.1016/j.jbc.2023.105471.

References

Prasher D, Eckenrode V, Ward W, Prendergast F, Cormier M . Primary structure of the Aequorea victoria green-fluorescent protein. Gene. 1992; 111(2):229-33. DOI: 10.1016/0378-1119(92)90691-h. View

Casler J, Zajac A, Valbuena F, Sparvoli D, Jeyifous O, Turkewitz A . ESCargo: a regulatable fluorescent secretory cargo for diverse model organisms. Mol Biol Cell. 2020; 31(26):2892-2903. PMC: 7927198. DOI: 10.1091/mbc.E20-09-0591. View

Kolos J, Voll A, Bauder M, Hausch F . FKBP Ligands-Where We Are and Where to Go?. Front Pharmacol. 2018; 9:1425. PMC: 6290070. DOI: 10.3389/fphar.2018.01425. View

Braeckmans K, Peeters L, Sanders N, De Smedt S, Demeester J . Three-dimensional fluorescence recovery after photobleaching with the confocal scanning laser microscope. Biophys J. 2003; 85(4):2240-52. PMC: 1303450. DOI: 10.1016/S0006-3495(03)74649-9. View

Brocker C, Thompson D, Vasiliou V . The role of hyperosmotic stress in inflammation and disease. Biomol Concepts. 2012; 3(4):345-364. PMC: 3438915. DOI: 10.1515/bmc-2012-0001. View

Giannotta M, Ruggiero C, Grossi M, Cancino J, Capitani M, Pulvirenti T . The KDEL receptor couples to Gαq/11 to activate Src kinases and regulate transport through the Golgi. EMBO J. 2012; 31(13):2869-81. PMC: 3395092. DOI: 10.1038/emboj.2012.134. View

Kreis T, Lodish H . Oligomerization is essential for transport of vesicular stomatitis viral glycoprotein to the cell surface. Cell. 1986; 46(6):929-37. PMC: 7133264. DOI: 10.1016/0092-8674(86)90075-9. View

Gordon D, Bond L, Sahlender D, Peden A . A targeted siRNA screen to identify SNAREs required for constitutive secretion in mammalian cells. Traffic. 2010; 11(9):1191-204. DOI: 10.1111/j.1600-0854.2010.01087.x. View

Pollok B, HEIM R . Using GFP in FRET-based applications. Trends Cell Biol. 1999; 9(2):57-60. DOI: 10.1016/s0962-8924(98)01434-2. View

10.

Barrero J, Papanikou E, Casler J, Day K, Glick B . An improved reversibly dimerizing mutant of the FK506-binding protein FKBP. Cell Logist. 2016; 6(3):e1204848. PMC: 5058350. DOI: 10.1080/21592799.2016.1204848. View

11.

Thorn K . Genetically encoded fluorescent tags. Mol Biol Cell. 2017; 28(7):848-857. PMC: 5385933. DOI: 10.1091/mbc.E16-07-0504. View

12.

Gronemeyer T, Chidley C, Juillerat A, Heinis C, Johnsson K . Directed evolution of O6-alkylguanine-DNA alkyltransferase for applications in protein labeling. Protein Eng Des Sel. 2006; 19(7):309-16. DOI: 10.1093/protein/gzl014. View

13.

Terai T, Kohno M, Boncompain G, Sugiyama S, Saito N, Fujikake R . Artificial Ligands of Streptavidin (ALiS): Discovery, Characterization, and Application for Reversible Control of Intracellular Protein Transport. J Am Chem Soc. 2015; 137(33):10464-7. DOI: 10.1021/jacs.5b05672. View

14.

Omari S, Makareeva E, Gorrell L, Jarnik M, Lippincott-Schwartz J, Leikin S . Mechanisms of procollagen and HSP47 sorting during ER-to-Golgi trafficking. Matrix Biol. 2020; 93:79-94. PMC: 8932071. DOI: 10.1016/j.matbio.2020.06.002. View

15.

Gautier A, Juillerat A, Heinis C, Correa Jr I, Kindermann M, Beaufils F . An engineered protein tag for multiprotein labeling in living cells. Chem Biol. 2008; 15(2):128-36. DOI: 10.1016/j.chembiol.2008.01.007. View

16.

Pagano R, Sleight R . Defining lipid transport pathways in animal cells. Science. 1985; 229(4718):1051-7. DOI: 10.1126/science.4035344. View

17.

Scales S, Pepperkok R, Kreis T . Visualization of ER-to-Golgi transport in living cells reveals a sequential mode of action for COPII and COPI. Cell. 1997; 90(6):1137-48. DOI: 10.1016/s0092-8674(00)80379-7. View

18.

Griffiths G, Simons K . The trans Golgi network: sorting at the exit site of the Golgi complex. Science. 1986; 234(4775):438-43. DOI: 10.1126/science.2945253. View

19.

Sargeant J, Seiler D, Costain T, Madreiter-Sokolowski C, Gordon D, Peden A . ALG-2 and peflin regulate COPII targeting and secretion in response to calcium signaling. J Biol Chem. 2021; 297(6):101393. PMC: 8671942. DOI: 10.1016/j.jbc.2021.101393. View

20.

Shaner N, Steinbach P, Tsien R . A guide to choosing fluorescent proteins. Nat Methods. 2005; 2(12):905-9. DOI: 10.1038/nmeth819. View