A novel di-leucine motif and a tyrosine-based motif independently mediate lysosomal targeting and endocytosis of CD3 chains

doi:10.1016/0092-8674(92)90636-Q

Cell

Volume 69, Issue 7, 26 June 1992, Pages 1143-1157

https://doi.org/10.1016/0092-8674(92)90636-Q Get rights and content

Abstract

Partial complexes of the T cell antigen receptor lacking ξ chains are delivered to lysosomes. Chimeric proteins composed of the Tac antigen fused to the cytoplasmic domains of each CD3 chain has allowed the identification of lysosomal targeting sequences. Tac-γ and Tac-δ chimeras are retained in the endoplasmic reticulum because of the presence of basic residues reminiscent of sequences responsible for the localization of endoplasmic reticulum resident proteins. Truncation of these retention motifs revealed lysosomal targeting of both Tac-γ and δ chimeras. A di-leucine- and a tyrosine-based motif are individually sufficient to induce both endocytosis and delivery to lysosomes of Tac. In contrast with chimeras containing only one of these motifs, the chimera containing both was predominantly delivered directly to lysosomes without going through the cell surface. These two sequences may represent two families of targeting motifs that determine the fate of proteins within the peripheral membrane system.

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ArticleA novel di-leucine motif and a tyrosine-based motif independently mediate lysosomal targeting and endocytosis of CD3 chains

Abstract

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J. Biol. Chem.

The T cell receptor ξ chain is tyrosine phosphorylated upon activation

J. Biol. Chem.

Transfer of proteins across membranes. II. Reconstitution of functional rough microsomes from heterologous components

J. Cell. Biol.

Subunit interactions within the T cell antigen receptor: clues from the study of partial complexes

A peptide sequence confers retention and rapid degradation in the endoplasmic reticulum

Science

Role of potentially charged transmembrane residues in targeting proteins for retention and degradation within the endoplasmic reticulum

EMBO J.

Lysosomal acid phosphatase is transported to lysosomes via the cell surface

EMBO J.

Morphological localization of a major lysosomal membrane glycoprotein in the endocytic membrane system

J. Biochem.

Biochemical analysis of the movement of a major lysosomal membrane glycoprotein in the endocytic membrane system

J. Biochem.

The protein kinase family: conserved features and deduced phylogeny of the catalytic domains

Science

Article
A novel di-leucine motif and a tyrosine-based motif independently mediate lysosomal targeting and endocytosis of CD3 chains