Trafficking of tail-anchored proteins: transport from the endoplasmic reticulum to the plasma membrane and sorting between surface domains in polarised epithelial cells - PubMed (original) (raw)
. 2002 Apr 15;115(Pt 8):1689-702.
doi: 10.1242/jcs.115.8.1689.
Affiliations
- PMID: 11950887
- DOI: 10.1242/jcs.115.8.1689
Trafficking of tail-anchored proteins: transport from the endoplasmic reticulum to the plasma membrane and sorting between surface domains in polarised epithelial cells
Alessandra Bulbarelli et al. J Cell Sci. 2002.
Abstract
Tail-anchored (TA) proteins, which are defined by an N-terminal cytosolic region and a C-terminal transmembrane domain (TMD), provide useful models for studying the role of the TMD in sorting within the exo-endocytic system. Previous work has shown that a short TMD is required to keep ER-resident TA proteins from escaping to downstream compartments of the secretory pathway. To investigate the role of the TMD in TA protein sorting, we used model constructs, which consisted of GFP linked at its C-terminus to the tail region of cytochrome b(5) with TMDs of differing length or hydrophobicity. Expression of these constructs in CV-1 cells demonstrated that the feature determining exit from the ER is hydrophobicity and that if exit occurs, at least a part of the protein reaches the cell surface. To investigate which pathway to the surface is followed by plasma-membrane-directed TA constructs, we expressed the TA constructs in polarised Madin Darby Canine Kidney (MDCK) cells. The constructs with 22 and 25 residue TMDs were localised basolaterally, but addition at the C-terminus of a 20-residue peptide containing an N-glycosylation site resulted in glycosylation-dependent relocation of approximately 50% of the protein to the apical surface. This result suggests that TA proteins may reach the basolateral surface without a signal or that our constructs contain a weak basolateral determinant that is recessive to the apical information carried by the glycan. To assess the effect of the TMDs of endogenous TA proteins, GFP was linked to the tails of syntaxin 3 and 4, which localise to the apical and basolateral surface, respectively, of MDCK cells. The two GFP fusion proteins showed a different surface distribution, which is consistent with a role for the two syntaxin TMDs in polarised sorting.
Similar articles
- Targeting of a tail-anchored protein to endoplasmic reticulum and mitochondrial outer membrane by independent but competing pathways.
Borgese N, Gazzoni I, Barberi M, Colombo S, Pedrazzini E. Borgese N, et al. Mol Biol Cell. 2001 Aug;12(8):2482-96. doi: 10.1091/mbc.12.8.2482. Mol Biol Cell. 2001. PMID: 11514630 Free PMC article. - Three-dimensional analysis of post-Golgi carrier exocytosis in epithelial cells.
Kreitzer G, Schmoranzer J, Low SH, Li X, Gan Y, Weimbs T, Simon SM, Rodriguez-Boulan E. Kreitzer G, et al. Nat Cell Biol. 2003 Feb;5(2):126-36. doi: 10.1038/ncb917. Nat Cell Biol. 2003. PMID: 12545172 - SNARE protein trafficking in polarized MDCK cells.
Steegmaier M, Lee KC, Prekeris R, Scheller RH. Steegmaier M, et al. Traffic. 2000 Jul;1(7):553-60. doi: 10.1034/j.1600-0854.2000.010705.x. Traffic. 2000. PMID: 11208143 - Apical protein transport.
Delacour D, Jacob R. Delacour D, et al. Cell Mol Life Sci. 2006 Nov;63(21):2491-505. doi: 10.1007/s00018-006-6210-8. Cell Mol Life Sci. 2006. PMID: 16927027 Free PMC article. Review. - Looking for a safe haven: tail-anchored proteins and their membrane insertion pathways.
Mehlhorn DG, Asseck LY, Grefen C. Mehlhorn DG, et al. Plant Physiol. 2021 Dec 4;187(4):1916-1928. doi: 10.1093/plphys/kiab298. Plant Physiol. 2021. PMID: 35235667 Free PMC article. Review.
Cited by
- Syntaxin-1A modulates vesicle fusion in mammalian neurons via juxtamembrane domain dependent palmitoylation of its transmembrane domain.
Vardar G, Salazar-Lázaro A, Zobel S, Trimbuch T, Rosenmund C. Vardar G, et al. Elife. 2022 May 31;11:e78182. doi: 10.7554/eLife.78182. Elife. 2022. PMID: 35638903 Free PMC article. - Fur4-mediated uracil-scavenging to screen for surface protein regulators.
Paine KM, Ecclestone GB, MacDonald C. Paine KM, et al. Traffic. 2021 Nov;22(11):397-408. doi: 10.1111/tra.12815. Epub 2021 Sep 23. Traffic. 2021. PMID: 34498791 Free PMC article. - The dynamic Nexus: gap junctions control protein localization and mobility in distinct and surprising ways.
McCutcheon S, Stout RF Jr, Spray DC. McCutcheon S, et al. Sci Rep. 2020 Oct 12;10(1):17011. doi: 10.1038/s41598-020-73892-6. Sci Rep. 2020. PMID: 33046777 Free PMC article. - Selective clearance of the inner nuclear membrane protein emerin by vesicular transport during ER stress.
Buchwalter A, Schulte R, Tsai H, Capitanio J, Hetzer M. Buchwalter A, et al. Elife. 2019 Oct 10;8:e49796. doi: 10.7554/eLife.49796. Elife. 2019. PMID: 31599721 Free PMC article. - The Ways of Tails: the GET Pathway and more.
Borgese N, Coy-Vergara J, Colombo SF, Schwappach B. Borgese N, et al. Protein J. 2019 Jun;38(3):289-305. doi: 10.1007/s10930-019-09845-4. Protein J. 2019. PMID: 31203484 Review.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources