The endoplasmic reticulum retention signal of the E3/19K protein of adenovirus type 2 consists of three separate amino acid segments at the carboxy terminus
- PMID: 2146274
- PMCID: PMC2116308
- DOI: 10.1083/jcb.111.5.1803
The endoplasmic reticulum retention signal of the E3/19K protein of adenovirus type 2 consists of three separate amino acid segments at the carboxy terminus
Abstract
The E3/19K protein of adenovirus type 2 is a resident of the ER. Immediately after synthesis it binds to human major histocompatibility complex class I antigens and prevents their departure from the ER compartment. The ER retention signal of the E3/19K protein is contained within the 15 amino acids that protrude on the cytoplasmic side at the carboxy terminus of the protein. To define the ER retention sequence in more detail, we have generated 10 mutants of the E3/19K protein that differ only within this segment. Analysis of the rate of intracellular transport and cell surface expression of HLA antigens associated to these mutants, show that the sequences Ser-Phe-Ile, located in the middle of the 15-residue segment and Met-Pro, at the extreme carboxy terminus, are crucial for retention. Four charged residues, Asp-Glu-Lys-Lys, are located between these two retention elements but are of little or no importance. The basic cluster of amino acids close to the membrane also has some effect on retention. Thus, the retention signal of the E3/19K protein is not a contiguous sequence of amino acids but has a complex spatial arrangement.
Similar articles
-
Requirements for the association of adenovirus type 2 E3/19K wild-type and mutant proteins with HLA antigens.J Virol. 1990 Aug;64(8):3679-85. doi: 10.1128/JVI.64.8.3679-3685.1990. J Virol. 1990. PMID: 2142509 Free PMC article.
-
Determinants of the endoplasmic reticulum (ER) lumenal-domain of the adenovirus serotype 2 E3-19K protein for association with and ER-retention of major histocompatibility complex class I molecules.Mol Immunol. 2011 Jan;48(4):532-8. doi: 10.1016/j.molimm.2010.10.017. Epub 2010 Nov 20. Mol Immunol. 2011. PMID: 21094528 Free PMC article.
-
The transmembrane domain of the adenovirus E3/19K protein acts as an endoplasmic reticulum retention signal and contributes to intracellular sequestration of major histocompatibility complex class I molecules.J Virol. 2013 Jun;87(11):6104-17. doi: 10.1128/JVI.03391-12. Epub 2013 Mar 20. J Virol. 2013. PMID: 23514889 Free PMC article.
-
Role of the adenovirus E3-19k conserved region in binding major histocompatibility complex class I molecules.J Virol. 1992 Aug;66(8):4778-83. doi: 10.1128/JVI.66.8.4778-4783.1992. J Virol. 1992. PMID: 1385834 Free PMC article.
-
The retention signal for soluble proteins of the endoplasmic reticulum.Trends Biochem Sci. 1990 Dec;15(12):483-6. doi: 10.1016/0968-0004(90)90303-s. Trends Biochem Sci. 1990. PMID: 2077689 Review.
Cited by
-
Retention of adenovirus E19 glycoprotein in the endoplasmic reticulum is essential to its ability to block antigen presentation.J Exp Med. 1991 Dec 1;174(6):1629-37. doi: 10.1084/jem.174.6.1629. J Exp Med. 1991. PMID: 1836014 Free PMC article.
-
The adenovirus E3 14.5-kilodalton protein, which is required for down-regulation of the epidermal growth factor receptor and prevention of tumor necrosis factor cytolysis, is an integral membrane protein oriented with its C terminus in the cytoplasm.J Virol. 1992 Mar;66(3):1665-73. doi: 10.1128/JVI.66.3.1665-1673.1992. J Virol. 1992. PMID: 1531370 Free PMC article.
-
Activation of transcription factor NF-kappaB by the adenovirus E3/19K protein requires its ER retention.J Cell Biol. 1996 Feb;132(4):511-22. doi: 10.1083/jcb.132.4.511. J Cell Biol. 1996. PMID: 8647884 Free PMC article.
-
Immunomodulatory functions encoded by the E3 transcription unit of adenoviruses.Virus Genes. 2000;21(1-2):13-25. Virus Genes. 2000. PMID: 11022786 Review.
-
Conserved cysteine residues within the E3/19K protein of adenovirus type 2 are essential for binding to major histocompatibility complex antigens.J Virol. 1994 Sep;68(9):5423-32. doi: 10.1128/JVI.68.9.5423-5432.1994. J Virol. 1994. PMID: 8057424 Free PMC article.
References
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Research Materials
Miscellaneous