Two birds with one stone: A novel motif for ACh receptor assembly quality control

Trends in Neurosciences

Volumn 26, Issue 4, 2003, Pages 178-181

  Mei, Lin ^a   Xiong, Wen C ^b  

^a UNIVERSITY OF ALABAMA AT BIRMINGHAM   (United States)

^b University of Alabama at Birmingham   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; ALPHA BUNGAROTOXIN; CHAPERONE; CHOLINERGIC RECEPTOR; NICOTINIC RECEPTOR; POTASSIUM CHANNEL; PROTEIN SUBUNIT; TRANSMEMBRANE CONDUCTANCE REGULATOR; TUBOCURARINE CHLORIDE; VIRUS GLYCOPROTEIN;

ADDICTION; ALPHA CHAIN; AMINO ACID SUBSTITUTION; BETA CHAIN; CARBOXY TERMINAL SEQUENCE; CELL MEMBRANE; CELL SURFACE; DISULFIDE BOND; ENDOPLASMIC RETICULUM; EPILEPSY; HUMAN; IMMUNOPRECIPITATION; MEMORY; MUTATION; NEUROMUSCULAR SYNAPSE; NEUROTRANSMISSION; NOCICEPTION; PARKINSON DISEASE; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN GLYCOSYLATION; PROTEIN MOTIF; PROTEIN STRUCTURE; QUALITY CONTROL; REVIEW; SEQUENCE ANALYSIS; WILD TYPE;

EID: 0037385161     PISSN: 01662236     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-2236(03)00036-5     Document Type: Review

References (23)

1. Fewell S.W., et al. The action of molecular chaperones in the early secretory pathway. Annu. Rev. Genet. 35:2001;149-191.
2. Nilsson T., Warren G. Retention and retrieval in the endoplasmic reticulum and the Golgi apparatus. Curr. Opin. Cell. Biol. 6:1994;517-521.
3. Ellgaard L., et al. Setting the standards: quality control in the secretory pathway. Science. 286:1999;1882-1888.
4. McCracken A.A., Brodsky J.L. Assembly of ER-associated protein degradation in vitro: dependence on cytosol, calnexin, and ATP. J. Cell. Biol. 132:1996;291-298.
5. Bonifacino J.S., Lippincott-Schwartz J. Degradation of proteins within the endoplasmic reticulum. Curr. Opin. Cell. Biol. 3:1991;592-600.
6. Teasdale R.D., Jackson M.R. Signal-mediated sorting of membrane proteins between the endoplasmic reticulum and the Golgi apparatus. Annu. Rev. Cell Dev. Biol. 12:1996;27-54.
7. Letourneur F., et al. Coatomer is essential for retrieval of dilysine-tagged proteins to the endoplasmic reticulum. Cell. 79:1994;1199-1207.
8. Ossipov D., et al. Yeast ER-Golgi v-SNAREs Bos1p and Bet1p differ in steady-state localization and targeting. J. Cell. Sci. 112:1999;4135-4142.
9. Zerangue N., et al. Analysis of endoplasmic reticulum trafficking signals by combinatorial screening in mammalian cells. Proc. Natl. Acad. Sci. U. S. A. 98:2001;2431-2436.
10. Chang X.B., et al. Removal of multiple arginine-framed trafficking signals overcomes misprocessing of delta F508 CFTR present in most patients with cystic fibrosis. Mol. Cell. 4:1999;137-142.
11. Karlin A. Emerging structure of the nicotinic acetylcholine receptors. Nat. Rev. Neurosci. 3:2002;102-114.
12. Unwin N. Acetylcholine receptor channel imaged in the open state. Nature. 373:1995;37-43.
13. Keller S.H., Taylor P. Determinants responsible for assembly of the nicotinic acetylcholine receptor. J. Gen. Physiol. 113:1999;171-176.
14. Green W.N. Ion channel assembly: creating structures that function. J. Gen. Physiol. 113:1999;163-170.
15. Smith M.M., et al. Formation of the α-bungarotoxin binding site and assembly of the nicotinic acetylcholine receptor subunits occur in the endoplasmic reticulum. J. Biol. Chem. 262:1987;4367-4376.
16. Keller S.H., et al. Adjacent basic amino acid residues recognized by the COP I complex and ubiquitination govern endoplasmic reticulum to cell surface trafficking of the nicotinic acetylcholine receptor α-subunit. J. Biol. Chem. 276:2001;18384-18391.
17. Wang J.M., et al. A transmembrane motif governs the surface trafficking of nicotinic acetylcholine receptors. Nat. Neurosci. 5:2002;963-970.
18. Wang Z.Z., et al. Assembly of the nicotinic acetylcholine receptor. The first transmembrane domains of truncated alpha and delta subunits are required for heterodimer formation in vivo. J. Biol. Chem. 271:1996;27575-27584.
19. Nishimura N., Balch W.E. A di-acidic signal required for selective export from the endoplasmic reticulum. Science. 277:1997;556-558.
20. Lopes C.M., et al. Block of Kcnk3 by protons. Evidence that 2-P-domain potassium channel subunits function as homodimers. J. Biol. Chem. 276:2001;24449-24452.
21. O'Kelly I., et al. Forward transport. 14-3-3 binding overcomes retention in endoplasmic reticulum by dibasic signals. Cell. 111:2002;577-588.
22. Jeanclos E.M., et al. The chaperone protein 14-3-3η interacts with the nicotinic acetylcholine receptor α4 subunit. Evidence for a dynamic role in subunit stabilization. J. Biol. Chem. 276:2001;28281-28290.
23. Verrall S., Hall Z.W. The N-terminal domains of acetylcholine receptor subunits contain recognition signals for the initial steps of receptor assembly. Cell. 68:1992;23-31.