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Mol Biol Cell. 2017 Jun 15;28(12):1676-1687. doi: 10.1091/mbc.E16-12-0863. Epub 2017 Apr 20.

A novel physiological role for ARF1 in the formation of bidirectional tubules from the Golgi.

Author information

1
Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06520.
2
Department of Biomedical Engineering, Yale University, New Haven, CT 06520.
3
Department of Chemistry, Yale University, New Haven, CT 06520.
4
Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06520.
5
Nanobiology Institute, Yale University, West Haven, CT 06516.
6
Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06520 james.rothman@yale.edu.

Abstract

Capitalizing on CRISPR/Cas9 gene-editing techniques and super-resolution nanoscopy, we explore the role of the small GTPase ARF1 in mediating transport steps at the Golgi. Besides its well-established role in generating COPI vesicles, we find that ARF1 is also involved in the formation of long (∼3 µm), thin (∼110 nm diameter) tubular carriers. The anterograde and retrograde tubular carriers are both largely free of the classical Golgi coat proteins coatomer (COPI) and clathrin. Instead, they contain ARF1 along their entire length at a density estimated to be in the range of close packing. Experiments using a mutant form of ARF1 affecting GTP hydrolysis suggest that ARF1[GTP] is functionally required for the tubules to form. Dynamic confocal and stimulated emission depletion imaging shows that ARF1-rich tubular compartments fall into two distinct classes containing 1) anterograde cargoes and clathrin clusters or 2) retrograde cargoes and coatomer clusters.

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