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Science 1 June 2001:
Vol. 292. no. 5522, pp. 1663 - 1665
DOI: 10.1126/science.1062239
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Perspectives

CELL BIOLOGY:
GGAs Tie Up the Loose Ends

Sharon A. Tooze

Cargo receptors, which recruit cargo proteins into transport vesicles, must themselves be sorted into appropriate vesicles budding from the correct cellular compartment. The job of sorting CI-MPR and CD-MPR cargo receptors into newly forming vesicles at the trans-Golgi network (TGN) has been widely attributed to the adaptor protein AP-1. Now, as Tooze explains in her Perspective, the job of sorting MPRs into TGN vesicles appears to be carried out instead by members of the GGA protein family (Zhu et al., Puertollano et al.).

The author is in the Secretory Pathways Laboratory, Imperial Cancer Research Fund, London WC2A 3PX, UK. E-mail: tooze{at}icrf.icnet.uk

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Binding Partners for the COOH-Terminal Appendage Domains of the GGAs and {gamma}-Adaptin.
W. W.Y. Lui, B. M. Collins, J. Hirst, A. Motley, C. Millar, P. Schu, D. J. Owen, and M. S. Robinson (2003)
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Assembly of Cell Regulatory Systems Through Protein Interaction Domains.
T. Pawson and P. Nash (2003)
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When cell biology meets development: endocytic regulation of signaling pathways.
E. S. Seto, H. J. Bellen, and T. E. Lloyd (2002)
Genes & Dev. 16, 1314-1336
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Access of a Membrane Protein to Secretory Granules Is Facilitated by Phosphorylation.
T. C. Steveson, G. C. Zhao, H. T. Keutmann, R. E. Mains, and B. A. Eipper (2001)
J. Biol. Chem. 276, 40326-40337
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