The T cell receptor (TCR) beta-chain is produced in the endoplasmic reticulum where it associates with the TCR alpha-chain and the members of the CD3 complex to form the complete receptor. When the other chains of the complex are not available, the beta-chain is rapidly degraded within the endoplasmic reticulum. When incomplete TCR.CD3 complexes are formed, they are transported through the Golgi apparatus and degraded in lysosomes. In this study, a truncated form of the TCR beta-chain has been made by removal of the transmembrane and cytoplasmic segments. Unlike the normal beta-chain, the truncated molecule is stable and is transported through the Golgi apparatus and secreted. This process occurs at a similar rate in both T and B cells, indicating that it is not affected by the presence or absence of CD3 components. These data suggest that an element in the transmembrane or cytoplasmic region of the beta-chain confers sensitivity to the degradative control mechanisms that regulate TCR expression.