Cheatham A, Sharma N, Satpute-Krishnan P
J Cell Biol. 2023; 222(10).
PMID: 37702712
PMC: 10499038.
DOI: 10.1083/jcb.202108160.
Christianson J, Jarosch E, Sommer T
Nat Rev Mol Cell Biol. 2023; 24(11):777-796.
PMID: 37528230
DOI: 10.1038/s41580-023-00633-8.
Costantini L, Snapp E
Curr Protoc Cell Biol. 2014; 60:21.7.1-21.7.29.
PMID: 24510787
PMC: 3920296.
DOI: 10.1002/0471143030.cb2107s60.
Needham P, Brodsky J
Biochim Biophys Acta. 2013; 1833(11):2447-57.
PMID: 23557783
PMC: 3723753.
DOI: 10.1016/j.bbamcr.2013.03.018.
Tyler R, Pearce M, Shaler T, Olzmann J, Greenblatt E, Kopito R
Mol Biol Cell. 2012; 23(24):4668-78.
PMID: 23097496
PMC: 3521676.
DOI: 10.1091/mbc.E12-06-0428.
Serine residues in the cytosolic tail of the T-cell antigen receptor alpha-chain mediate ubiquitination and endoplasmic reticulum-associated degradation of the unassembled protein.
Ishikura S, Weissman A, Bonifacino J
J Biol Chem. 2010; 285(31):23916-24.
PMID: 20519503
PMC: 2911338.
DOI: 10.1074/jbc.M110.127936.
Src-like adaptor protein down-regulates T cell receptor (TCR)-CD3 expression by targeting TCRzeta for degradation.
Myers M, Dragone L, Weiss A
J Cell Biol. 2005; 170(2):285-94.
PMID: 16027224
PMC: 2171412.
DOI: 10.1083/jcb.200501164.
Molecular mechanisms for the assembly of the T cell receptor-CD3 complex.
Call M, Wucherpfennig K
Mol Immunol. 2004; 40(18):1295-305.
PMID: 15072848
PMC: 4515969.
DOI: 10.1016/j.molimm.2003.11.017.
Recognition of a single transmembrane degron by sequential quality control checkpoints.
Fayadat L, Kopito R
Mol Biol Cell. 2003; 14(3):1268-78.
PMID: 12631739
PMC: 151595.
DOI: 10.1091/mbc.e02-06-0363.
The KDEL receptor mediates a retrieval mechanism that contributes to quality control at the endoplasmic reticulum.
Yamamoto K, Fujii R, TOYOFUKU Y, Saito T, Koseki H, Hsu V
EMBO J. 2001; 20(12):3082-91.
PMID: 11406585
PMC: 150210.
DOI: 10.1093/emboj/20.12.3082.
The transmembrane adaptor protein TRIM regulates T cell receptor (TCR) expression and TCR-mediated signaling via an association with the TCR zeta chain.
Kirchgessner H, Dietrich J, Scherer J, Isomaki P, Korinek V, Hilgert I
J Exp Med. 2001; 193(11):1269-84.
PMID: 11390434
PMC: 2193385.
DOI: 10.1084/jem.193.11.1269.
Selection of functional T cell receptor mutants from a yeast surface-display library.
Kieke M, Shusta E, Boder E, Teyton L, Wittrup K, Kranz D
Proc Natl Acad Sci U S A. 1999; 96(10):5651-6.
PMID: 10318939
PMC: 21915.
DOI: 10.1073/pnas.96.10.5651.
Role of dimerization of the membrane-associated growth factor kit ligand in juxtacrine signaling: the Sl17H mutation affects dimerization and stability-phenotypes in hematopoiesis.
Tajima Y, Huang E, Vosseller K, Ono M, Moore M, Besmer P
J Exp Med. 1998; 187(9):1451-61.
PMID: 9565637
PMC: 2212272.
DOI: 10.1084/jem.187.9.1451.
Novel aspects of degradation of T cell receptor subunits from the endoplasmic reticulum (ER) in T cells: importance of oligosaccharide processing, ubiquitination, and proteasome-dependent removal from ER membranes.
Yang M, Omura S, Bonifacino J, Weissman A
J Exp Med. 1998; 187(6):835-46.
PMID: 9500786
PMC: 2212191.
DOI: 10.1084/jem.187.6.835.
Aggregation as a determinant of protein fate in post-Golgi compartments: role of the luminal domain of furin in lysosomal targeting.
Wolins N, Bosshart H, Kuster H, Bonifacino J
J Cell Biol. 1998; 139(7):1735-45.
PMID: 9412468
PMC: 2132652.
DOI: 10.1083/jcb.139.7.1735.
In vitro translation and assembly of a complete T cell receptor-CD3 complex.
Huppa J, Ploegh H
J Exp Med. 1997; 186(3):393-403.
PMID: 9236191
PMC: 2198996.
DOI: 10.1084/jem.186.3.393.
Proteasome-dependent endoplasmic reticulum-associated protein degradation: an unconventional route to a familiar fate.
Werner E, Brodsky J, McCracken A
Proc Natl Acad Sci U S A. 1996; 93(24):13797-801.
PMID: 8943015
PMC: 19430.
DOI: 10.1073/pnas.93.24.13797.
Degradation of aggrecan precursors within a specialized subcompartment of the chicken chondrocyte endoplasmic reticulum.
Alonso M, Hidalgo J, Hendricks L, Velasco A
Biochem J. 1996; 316 ( Pt 2):487-95.
PMID: 8687392
PMC: 1217376.
DOI: 10.1042/bj3160487.
Assembly of ER-associated protein degradation in vitro: dependence on cytosol, calnexin, and ATP.
McCracken A, Brodsky J
J Cell Biol. 1996; 132(3):291-8.
PMID: 8636208
PMC: 2120716.
DOI: 10.1083/jcb.132.3.291.
Misfolded major histocompatibility complex class I molecules accumulate in an expanded ER-Golgi intermediate compartment.
Raposo G, van Santen H, Leijendekker R, Geuze H, Ploegh H
J Cell Biol. 1995; 131(6 Pt 1):1403-19.
PMID: 8522600
PMC: 2120650.
DOI: 10.1083/jcb.131.6.1403.