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A lysosomal protein negatively regulates surface T cell antigen receptor expression by promoting CD3zeta-chain degradation.

Abstract：

:Modulation of surface T cell antigen receptor (TCR) expression is an important mechanism for the regulation of immune responses and the prevention of T cell hyperactivation and autoimmunity. The TCR is rapidly internalized after antigen stimulation and then degraded in lysosomes. However, few of the molecules involved in this process have been identified. We demonstrate that the lysosomal protein LAPTM5 negatively regulated surface TCR expression by specifically interacting with the invariant signal-transducing CD3zeta chain and promoting its degradation without affecting other CD3 proteins, CD3epsilon, CD3delta, or CD3gamma. TCR downmodulation required the polyproline-tyrosine motifs and the ubiquitin-interacting motif of LAPTM5. LAPTM5 deficiency resulted in elevated TCR expression on both CD4(+)CD8(+) thymocytes and spleen T cells after CD3 stimulation, as well as enhanced T cell responses in vitro and in vivo. These results identify a lysosomal protein important for CD3zeta degradation and illustrate a unique mechanism for the control of surface TCR expression and T cell activation.

journal_name

Immunity

journal_title

Immunity

authors

Ouchida R,Yamasaki S,Hikida M,Masuda K,Kawamura K,Wada A,Mochizuki S,Tagawa M,Sakamoto A,Hatano M,Tokuhisa T,Koseki H,Saito T,Kurosaki T,Wang JY

doi

10.1016/j.immuni.2008.04.024

subject

Has Abstract

pub_date

2008-07-18 00:00:00

pages

33-43

issue

1

eissn

1074-7613

issn

1097-4180

pii

S1074-7613(08)00281-1

journal_volume

29

pub_type

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