Functional characterization of novel human ARFGAP3

Autor: Fuchu He, Guichun Xing, Chenggang Zhang, Xiaoqin Liu, Qingtang Chen
Rok vydání: 2001
Předmět:
Male
Phosphatidylinositol 4
5-Diphosphate
Time Factors
GTPase-activating protein
ADP ribosylation factor
Biochemistry
Mice
chemistry.chemical_compound
Cytosol
Thioredoxins
Structural Biology
Testis
Cells
Cultured
Vesicular transport
ADP-Ribosylation Factors
GTPase-Activating Proteins
Vesicular transport protein
Protein Transport
COS Cells
Phosphatidylcholines
Guanosine Triphosphate
Intracellular
Recombinant Fusion Proteins
Blotting
Western
Green Fluorescent Proteins
Immunoblotting
Secreted alkaline phosphatase
Biophysics
Biology
Transfection
Endocrine Glands
Escherichia coli
Genetics
Animals
Humans
Phosphatidylinositol
Molecular Biology
Secretory pathway
Cell Nucleus
Dose-Response Relationship
Drug
Cell Biology
Alkaline Phosphatase
In vitro
Luminescent Proteins
Microscopy
Fluorescence
chemistry
Zdroj: FEBS Letters. 490:79-83
ISSN: 0014-5793
Popis: ADP ribosylation factors (ARFs) are critical in the vesicular trafficking pathway. ARF activity is controlled by GTPase-activating proteins (GAPs). We have identified recently a novel tentative ARF GAP derived from human fetal liver, ARFGAP3 (originally named as ARFGAP1). In the present study, we demonstrated that ARFGAP3 had GAP activity in vitro and remarked that the GAP activity of ARFGAP3 was regulated by phospholipids, i.e. phosphatidylinositol 4,5-diphosphate as agonist and phosphatidylcholine as antagonist. ARFGAP3 is a predominantly cytosolic protein, and concentrated in the perinuclear region. Its transient ectopic overexpression in cultured mammalian cells reduced the constitutive secretion of secreted alkaline phosphatase, indicating that ectopic overexpression of ARFGAP3 inhibits the early secretory pathway of proteins in vivo. These results demonstrated that ARFGAP3 is a novel GAP for ARF1 and might be involved in intracellular traffic of proteins and vesicular transport as predicted.
Databáze: OpenAIRE
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