Results 191 to 200 of about 3,458 (213)

Screening of gene function in cell intoxication by CNF1 links Sec61 translocon to Rac1 GTPase activity. [PDF]

mBio
Paillares E, Deboosere N, Descorps-Declere S, Marechal M, Gillet D, Demangel C, Mettouchi A, Brodin P, Lemichez E.   +8 more
europepmc   +1 more source

Hijacking host cell vesicular transport: New insights into the nutrient acquisition mechanism of Chlamydia. [PDF]

Virulence
Wenbo L, Yewei Y, Hui Z, Zhongyu L.
europepmc   +1 more source

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Rab18 regulates lipolysis via Arf/GBF1 and adipose triglyceride lipase.

Biochemical and Biophysical Research Communications, 2019
Rab18 is a small GTPase associated with lipid droplets and other membranes. While it likely has multiple functions on lipid droplets, one proposed function is regulation of lipolysis. Previous work has concentrated on regulation of autophagy; however, in
S. Dejgaard, J. Presley
semanticscholar   +3 more sources

GBF1 deficiency causes cataracts in human and mouse

Human Genetics
Any opacification of the lens can be defined as cataracts, and lens epithelium cells play a crucial role in guaranteeing lens transparency by maintaining its homeostasis. Although several causative genes of congenital cataracts have been reported, the mechanisms underlying lens opacity remain unclear.
Weimin Jia, Chenming Zhang, Yalin Luo, Jing Gao, Chao Yuan, Dazhi Zhang, Xiaopei Zhou, Yongyao Tan, Shuang Wang, Zhuo Chen, Guigang Li, Xianqin Zhang   +11 more
semanticscholar   +3 more sources

Loss of Arf Guanine Nucleotide Exchange Factor GBF1 Activity Disturbs Organelle Dynamics in Mouse Oocytes

Microscopy and Microanalysis, 2021
GBF1 [Golgi brefeldin A (BFA) resistance factor 1] is a member of the guanine nucleotide exchange factors Arf family. GBF1 localizes at the cis-Golgi and endoplasmic reticulum (ER)-Golgi intermediate compartment where it participates in ER-Golgi traffic ...
Yuan-Jing Zou, Meng-Meng Shan, Zhen‐Nan Pan, Meng-Hao Pan, Xiao-Han Li, Shao‐Chen Sun   +5 more
semanticscholar   +1 more source

GBF1 recruitment to membranes: domains and interacting proteins

, 2020
The Golgi complex resides at the center of the cellular trafficking pathway, where it functions in the modification, sorting, and trafficking of over one third of human proteins to their correct cellular destination. Initiation of vesicle formation at the Golgi requires activation of small GTPases of the ADP-ribosylation factor (Arf) family.
Calvin J Chan
semanticscholar   +2 more sources

GBF1 and Arf1 function in vesicular trafficking, lipid homoeostasis and organelle dynamics

Biology of the Cell, 2017
AbstractThe 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).
Beata Kaczmarek, J. Verbavatz, C. L. Jackson   +2 more
semanticscholar   +3 more sources

Dissection of Membrane Dynamics of the ARF-Guanine Nucleotide Exchange Factor GBF1

Traffic, 2005
ADP‐ribosylation factor (ARF)‐facilitated recruitment of COP I to membranes is required for secretory traffic. The guanine nucleotide exchange factor GBF1 activates ARF and regulates ARF/COP I dynamics at the endoplasmic reticulum (ER)–Golgi interface. Like ARF and coatomer, GBF1 peripherally associates with membranes.
Rafael Garcia-Mata, Cecilia Alvarez, Elizabeth Sztul   +2 more
exaly   +3 more sources

Rab1b-GBF1-ARFs mediated intracellular trafficking is required for classical swine fever virus replication in swine umbilical vein endothelial cells.

Veterinary Microbiology, 2020
Classical swine fever virus (CSFV), a plus-sense RNA virus, utilizes host intracellular membrane organelles for its replication. Our previous studies have shown that disruption of the intracellular membrane-trafficking events can inhibit CSFV replication.
Liang Zhang, Tao Wang, Mengzhao Song, Mingxing Jin, Shanchuan Liu, K. Guo, Yanming Zhang   +6 more
semanticscholar   +1 more source

The Arf GEF GBF1 Is Required for GGA Recruitment to Golgi Membranes

Traffic, 2007
The lysosomal trafficking of the mannose 6‐phosphate receptor and sortilin require that the Golgi‐localized, γ‐ear‐containing, ADP ribosylation factor (Arf)‐binding proteins (GGAs) be recruited to Golgi membranes where they bind a signal in the cytosolic tail of the receptors and recruit clathrin to form trafficking vesicles.
Lefrançois, Stephane, McCormick, Peter J.   +1 more
openaire   +3 more sources