Multiple activities of Arl1 GTPase in the trans-Golgi network

• Published in: Journal of cell science Vol. 130; no. 10; pp. 1691 - 1699
• Main Authors: Yu, Chia-Jung, Lee, Fang-Jen S.
• Format: Journal Article
• Language: English
• Published: England The Company of Biologists Ltd 15.05.2017
• Subjects: Adenosine diphosphate; ADP-ribosylation factor; ADP-Ribosylation Factors - metabolism; Animals; Cell Membrane - metabolism; Cytoskeleton; Effectors; Golgi apparatus; GTP Phosphohydrolases - metabolism; Guanosine triphosphatases; Guanosine triphosphate; Humans; Immunity; Innate immunity; Membrane Proteins - metabolism; Protein folding; Protein Transport; Proteins; Regulators; Structure-function relationships; trans-Golgi Network - metabolism; Transport Vesicles - metabolism; Yeast; Arf; Golgi complex; GAP; GEF; Membrane trafficking; Endosome; GTPase; Golgin
• ISSN: 0021-9533; 1477-9137; 1477-9137
• DOI: 10.1242/jcs.201319

ADP-ribosylation factors (Arfs) and ADP-ribosylation factor-like proteins (Arls) are highly conserved small GTPases that function as main regulators of vesicular trafficking and cytoskeletal reorganization. Arl1, the first identified member of the large Arl family, is an important regulator of Golgi complex structure and function in organisms ranging from yeast to mammals. Together with its effectors, Arl1 has been shown to be involved in several cellular processes, including endosomal trans-Golgi network and secretory trafficking, lipid droplet and salivary granule formation, innate immunity and neuronal development, stress tolerance, as well as the response of the unfolded protein. In this Commentary, we provide a comprehensive summary of the Arl1-dependent cellular functions and a detailed characterization of several Arl1 effectors. We propose that involvement of Arl1 in these diverse cellular functions reflects the fact that Arl1 is activated at several late-Golgi sites, corresponding to specific molecular complexes that respond to and integrate multiple signals. We also provide insight into how the GTP-GDP cycle of Arl1 is regulated, and highlight a newly discovered mechanism that controls the sophisticated regulation of Arl1 activity at the Golgi complex.