2017/10/06 by Beata Kaczmarek, Jean‐Marc Verbavatz, Catherine L. Jackson +1 · 65 citations
Biochemistry, Genetics and Molecular Biology · #Biochemistry #Biology #COPI #Cell biology #Cellular transport and secretion #Endocytosis #Endoplasmic reticulum #Function (biology) #Golgi apparatus #Guanine nucleotide exchange factor #Integral membrane protein #Lipid Membrane Structure and Behavior #Membrane #Membrane contact site #Membrane protein #Microtubule #Microtubule and mitosis dynamics #Organelle #Receptor #Secretory pathway #Signal transduction #Vesicle #Vesicular transport protein
paper · doi:10.1111/boc.201700042
published in Biology of the Cell 109(12), 391-399 (Wiley)
openalex publication_date 2017/10/06 · crossref created 2017/10/06 · crossref issued 2017/11/06 · crossref published 2017/11/06 · crossref published-online 2017/11/06 · crossref published-print 2017/12/01 · crossref deposited 2023/10/01 · openalex created_date 2025/10/10 · crossref indexed 2026/08/04 · openalex updated_date 2026/08/06
The ADP-ribosylation factor (Arf) small G proteins act as molecular switches to coordinate multiple downstream pathways that regulate membrane dynamics. Their activation is spatially and temporally controlled by the guanine nucleotide exchange factors (GEFs). Members of the evolutionarily conserved GBF/Gea family of Arf GEFs are well known for their roles in formation of coat protein complex I (COPI) vesicles, essential for maintaining the structure and function of the Golgi apparatus. However, studies over the past 10 years have found new functions for these GEFs, along with their substrate Arf1, in lipid droplet metabolism, clathrin-independent endocytosis, signalling at the plasma membrane, mitochondrial dynamics and transport along microtubules. Here, we describe these different functions, focussing in particular on the emerging theme of GFB1 and Arf1 regulation of organelle movement on microtubules.