PubMed:1671043 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PubMed/sourceid/1671043","sourcedb":"PubMed","sourceid":"1671043","source_url":"http://www.ncbi.nlm.nih.gov/pubmed/1671043","text":"The endoplasmic reticulum retention signal of the E3/19K protein of adenovirus-2 is microtubule binding.\nThe signal for retention in the endoplasmic reticulum of the E3/19K protein of adenovirus type 2 is located within the carboxyl-terminal cytoplasmic extension. A synthetic peptide corresponding to this sequence showed affinity for beta-tubulin, could promote tubulin polymerization in vitro, and bound to taxol-polymerized microtubules. When compared with the microtubule binding sequences from two microtubule-associated proteins (MAPs; MAP2 and tau), we found similarities suggesting that the cytoplasmic tail might bind to tubulin/microtubules in a MAPs-like fashion. A synthetic peptide corresponding to the cytoplasmic tail of an E3/19K deletion mutant not retained in the endoplasmic reticulum was also tested. It had the same net charge but did not promote tubulin polymerization in vitro nor did it show measurable affinity for tubulin or microtubules. This indicates that binding to microtubules is important for retention of the E3/19K protein in the endoplasmic 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