Analysis of endocytic pathways in Drosophila cells reveals a conserved role for GBF1 in internalization via GEECs. [PDF]
PLoS ONE, 2009 In mammalian cells, endocytosis of the fluid phase and glycosylphosphatidylinositol-anchored proteins (GPI-APs) forms GEECs (GPI-AP enriched early endosomal compartments) via an Arf1- and Cdc42-mediated, dynamin independent mechanism.
Gagan D Gupta +5 more
doaj +1 more source
Dynamics of GBF1, a Brefeldin A-Sensitive Arf1 Exchange Factor at the Golgi [PDF]
Molecular Biology of the Cell, 2005 Trafficking through the Golgi apparatus requires members of the Arf family of GTPases, whose activation is regulated by guanine nucleotide exchange factors (GEFs). Once activated, Arf-GTP recruits effectors such as coat complexes and lipid-modifying enzymes to specific membrane sites, creating a domain competent for cargo concentration and transport ...
Ting-Kuang, Niu +3 more
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Hepatitis C virus replication and Golgi function in brefeldin a-resistant hepatoma-derived cells. [PDF]
PLoS ONE, 2013 Recent reports indicate that the replication of hepatitis C virus (HCV) depends on the GBF1-Arf1-COP-I pathway. We generated Huh-7-derived cell lines resistant to brefeldin A (BFA), which is an inhibitor of this pathway. The resistant cell lines could be
Rayan Farhat +7 more
doaj +1 more source
Spatial-Temporal Study of Rab1b Dynamics and Function at the ER-Golgi Interface. [PDF]
PLoS ONE, 2016 The GTPase Rab1b is involved in ER to Golgi transport, with multiple Rab1b effectors (located at ERES, VTCs and the Golgi complex) being required for its function.
Hernán Martinez +3 more
doaj +1 more source
Identification and functional characterization of the GBF1-controlled network of host proteins supporting enterovirus replication [PDF]
, 2022 The genus Enterovirus of the Picornaviridae family contains many established and emerging pathogens. However, licensed vaccines are currently available only against poliovirus and enterovirus A71.
Moghimi, Seyedehmahsa
core +1 more source
Skeletal muscle perilipin 3 and coatomer proteins are increased following exercise and are associated with fat oxidation. [PDF]
PLoS ONE, 2014 Lipid droplet-associated proteins such as perilipin 3 (PLIN3) and coatomer GTPase proteins (GBF1, ARF1, Sec23a, and ARFRP1) are expressed in skeletal muscle but little is known so far as to their regulation of lipolysis.
Jeffrey D Covington +7 more
doaj +1 more source
The AtCathB3 gene, encoding a cathepsin B-like protease, is expressed during germination of Arabidopsis thaliana and transcriptionally repressed by the basic leucine zipper protein GBF1. [PDF]
, 2013 Protein hydrolysis plays an important role during seed germination and post-germination seedling establishment. In Arabidopsis thaliana, cathepsin B-like proteases are encoded by a gene family of three members, but only the AtCathB3 gene is highly ...
Barrero-Sicilia, C. +16 more
core +1 more source
Rab1b Interacts with GBF1 and Modulates both ARF1 Dynamics and COPI Association [PDF]
Molecular Biology of the Cell, 2007 Assembly of the cytosolic coat protein I (COPI) complex at the ER–Golgi interface is directed by the ADP ribosylation factor1 (Arf1) and its guanine nucleotide exchange factor (GBF1). Rab1b GTPase modulates COPI recruitment, but the molecular mechanism underlying this action remains unclear.
Monetta, Pablo Miguel +3 more
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Hijacking of multiple phospholipid biosynthetic pathways and induction of membrane biogenesis by a picornaviral 3CD protein. [PDF]
PLoS Pathogens, 2018 RNA viruses induce specialized membranous structures for use in genome replication. These structures are often referred to as replication organelles (ROs). ROs exhibit distinct lipid composition relative to other cellular membranes.
Sravani Banerjee +10 more
doaj +1 more source
Targeting of the Arf-GEF GBF1 to lipid droplets and Golgi membranes [PDF]
Journal of Cell Science, 2013 Lipid droplet metabolism and secretory pathway trafficking both require activation of the Arf1 small G protein. The spatio-temporal regulation of Arf1 activation is mediated by guanine nucleotide exchange factors (GEFs) of the GBF and BIG families, but the mechanisms of their localization to multiple sites within cells are poorly understood.
Bouvet, S. +3 more
openaire +3 more sources