Tethering of vesicles to the Golgi by GMAP210 controls LAT delivery to the immune synapse

Nat Commun. 2019 Jun 28;10(1):2864. doi: 10.1038/s41467-019-10891-w.

Abstract

The T cell immune synapse is a site of intense vesicular trafficking. Here we show that the golgin GMAP210, known to capture vesicles and organize membrane traffic at the Golgi, is involved in the vesicular transport of LAT to the immune synapse. Upon activation, more GMAP210 interact with LAT-containing vesicles and go together with LAT to the immune synapse. Regulating LAT recruitment and LAT-dependent signaling, GMAP210 controls T cell activation. Using a rerouting and capture assay, we show that GMAP210 captures VAMP7-decorated vesicles. Overexpressing different domains of GMAP210, we also show that GMAP210 allows their specific delivery to the immune synapse by tethering LAT-vesicles to the Golgi. Finally, in a model of ectopic expression of LAT in ciliated cells, we show that GMAP210 tethering activity controls the delivery of LAT to the cilium. Hence, our results reveal a function for the golgin GMAP210 conveying specific vesicles to the immune synapse.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptor Proteins, Signal Transducing / metabolism*
  • Cell Line
  • Cytoskeletal Proteins
  • Female
  • Gene Expression Regulation
  • Golgi Apparatus / physiology*
  • Humans
  • Leukocytes, Mononuclear / physiology*
  • Male
  • Membrane Proteins / metabolism*
  • Nuclear Proteins / genetics
  • Nuclear Proteins / metabolism*
  • R-SNARE Proteins / genetics
  • R-SNARE Proteins / metabolism
  • SNARE Proteins / genetics
  • SNARE Proteins / metabolism
  • Signal Transduction
  • T-Lymphocytes / physiology
  • Transport Vesicles / physiology*

Substances

  • Adaptor Proteins, Signal Transducing
  • Cytoskeletal Proteins
  • LAT protein, human
  • Membrane Proteins
  • Nuclear Proteins
  • R-SNARE Proteins
  • SNARE Proteins
  • TRIP11 protein, human
  • VAMP7 protein, human