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GGA proteins bind ubiquitin to facilitate sorting at the trans-Golgi network

Scott, Patricia M., Bilodeau, Patricia S., Zhdankina, Olga, Winistorfer, Stanley C., Hauglund, Melissa J., Allaman, Margaret M., Kearney, William R., Robertson, Andrew D., Boman, Annette L., Piper, Robert C.·2004·Nature Cell Biology
DOI 10.1038/ncb1107
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Abstract

Ubiquitination functions as a sorting signal for lysosomal degradation of cell-surface proteins by facilitating their internalization from the plasma membrane and incorporation into lumenal vesicles of multivesicular bodies (MVBs). Ubiquitin may also mediate sorting of proteins from the trans-Golgi network (TGN) to the endosome, thereby preventing their appearance on the cell surface and hastening their degradation in the lysosome-vacuole. Substantiation of a direct ubiquitin-dependent TGN sorting pathway relies in part on identifying candidate machinery that may function as a ubiquitin-sorting 'receptor'at the TGN. Members of the GGA family of coat proteins localize to the TGN and promote the incorporation of proteins into clathrin-coated vesicles destined for transport to endosomes. We show that the GGA coat proteins bind directly to ubiquitin through their GAT domain and demonstrate that this interaction is required for the ubiquitin-dependent sorting of the Gap1 amino acid transporter from the TGN to endosomes. Thus, GGA proteins fulfill the role of ubiquitin sorting receptors at the TGN.

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Crossref · 10.1038/ncb1107

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  • A hypothesis-driven study by Uemura and colleagues provides additional evidence that GGA2 interacts with the cytoplasmic domain of EGFR, stabilizing receptor expression and promoting growth of colorectal carcinoma cells.

    “In the process of assembling this manuscript, a hypothesis driven study by Uemura and colleagues was published that provide additional evidence that GGA2 interacts with the cytoplasmic domain of EGFR, stabilizing receptor expression and promoting growth of colorectal carcinoma cells37.”

    From Integrative Genomic Analyses Identifies GGA2 as a Cooperative Driver of EGFR-Mediated Lung Tumorigenesis (2019) · cites this paper as [37]

  • Uemura and colleagues showed that GGA2 is overexpressed in 23-30% of human hepatocellular carcinoma and colorectal cancers.

    “Further, they showed that GGA2 is overexpressed in 23-30% of human hepatocellular carcinoma and colorectal cancers37.”

    From Integrative Genomic Analyses Identifies GGA2 as a Cooperative Driver of EGFR-Mediated Lung Tumorigenesis (2019) · cites this paper as [37]

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Research works printed but not linked: 28

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Metadata

Authors
Scott, P. M., Bilodeau, P. S., Zhdankina, O., Winistorfer, S. C., Hauglund, M. J., Allaman, M. M., Kearney, W. R., Robertson, A. D., Boman, A. L., & Piper, R. C.
Venue
Nature Cell Biology
Publisher
Springer Science and Business Media LLC
Published
2004-02-22
Volume
6
Issue
3
Pages
252-259
ISSN
  • 1465-7392
  • 1476-4679
DOI
10.1038/ncb1107
Cited by
144
References
0
Language
en
Licence
www.springer.com/tdm (tdm)

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