ADP-ribosylation factors (ARFs), small guanine nucleotide-binding proteins that enhance the enzymatic activities of cholera toxin, constitute 1 family of the RAS superfamily. Monomeric guanine nucleotide-binding proteins of the RAS superfamily function in a variety of cellular processes including signaling, growth, immunity, and protein transport. ARFs are essential and ubiquitous in eukaryotes, being involved in vesicular transport and functioning as activators of phospholipase D. The functions of ARF proteins in membrane traffic and organelle integrity are intimately tied to their reversible association with membranes and specific interactions with membrane phospholipids. A common feature of these functions is their regulation by the binding and hydrolysis of GTP. Bobak et al. (1989) cloned 2 ARF cDNAs, ARF1 and ARF3 from a human cerebellum library.
This gene is FSH induced. Identification of differential gene expression in in vitro FSH treated pig granulosa cells using suppression subtractive hybridization. Bonnet A et al. ABSTRACT: FSH, which binds to specific receptors on granulosa cells in mammals, plays a key role in folliculogenesis. Its biological activity involves stimulation of intercellular communication and upregulation of steroidogenesis, but the entire spectrum of the genes regulated by FSH has yet to be fully characterized. In order to find new regulated transcripts, however rare, we have used a Suppression Subtractive Hybridization approach (SSH) on pig granulosa cells in primary culture treated or not with FSH. Two SSH libraries were generated and 76 clones were sequenced after selection by differential screening. Sixty four different sequences were identified, including 3 novel sequences. Experiments demonstrated the presence of 25 regulated transcripts. A gene ontology analysis of these 25 genes revealed (1) catalytic; (2) transport; (3) signal transducer; (4) binding; (5) anti-oxidant and (6) structural activities. These findings may deepen our understanding of FSH's effects. Particularly, they suggest that FSH is involved in the modulation of peroxidase activity and remodelling of chromatin.
NCBI Summary:
ADP-ribosylation factor 1 (ARF1) is a member of the human ARF gene family. These genes encode small guanine nucleotide-binding proteins that stimulate the ADP-ribosyltransferase activity of cholera toxin and play a role in vesicular trafficking and as activators of phospholipase D. The gene products include 6 ARF proteins and 11 ARF-like proteins and constitute 1 family of the RAS superfamily. The ARF proteins are categorized as class I (ARF1, ARF2,and ARF3), class II (ARF4 and ARF5) and class III (ARF6) and members of each class share a common gene organization. The ARF1 gene spans approximately 16.5 kb and contains five exons and four introns. The ARF1 protein is localized to the Golgi apparatus and has a central role in intra-Golgi transport.
General function
Intracellular signaling cascade
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Cellular localization
Cytoplasmic, Plasma membrane
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Ovarian function
Oogenesis, Oocyte maturation
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Schumann et al reported that ARP is a plasma membrane-associated Ras-related GTPase with remote similarity to the family of ADP-ribosylation factors.
ARP lacks the myristoylation site at position 2 and comprises an insertion of 8 amino acids in the region between PM1 and PM2. mRNA was found in most rat tissues examined (skeletal muscle, fat, liver, kidney, spleen, testis, adrenals, ovary, thymus, intestine, and lung). Zhang et al 2000 reported the characterization, Chromosomal Assignment, and Tissue Expression of a Novel Human Gene Belonging to the ARF GAP Family.
Gene whose expression is detected by cDNA array hybridization: transporters, signal transduction Rozenn Dalbi?Tran and Pascal Mermilloda
Expression regulated by
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Ovarian localization
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This gene was found in a rat ovarian cDNA library (Unigene)
Follicle stages
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Phenotypes
Mutations
1 mutations
Species: mouse
Mutation name: None
type: null mutation fertility: infertile - ovarian defect Comment: ADP-Ribosylation Factor 1 Regulates Asymmetric Cell Division in Female Meiosis in the Mouse. Wang S et al. Mouse oocytes undergo two successive meiotic divisions to generate one large egg with two small polar bodies, which is essential for preserving the maternal resources to support embryonic development. Although previous studies have shown that some small GTPases, such as RAC, RAN and CDC42, play important roles in cortical polarization and spindle pole anchoring, no oocytes undergo cytokinesis when the mutant forms of these genes are expressed in mouse oocytes. Here we show that the ADP-ribosylation factor 1 (ARF1) plays an important role in regulating asymmetric cell division in mouse oocyte meiosis. Microinjection of mRNA of a dominant negative mutant form of Arf1 (Arf1(T31N)) into fully grown germinal vesicle oocytes led to symmetric cell division in meiosis I, generating two metaphase II (MII) oocytes of equal size. Subsequently, the two MII oocytes of equal size underwent the second round of symmetric cell division to generate a 4-cell embryo (zygote) when activated parthenogenetically or via sperm injection. Furthermore, inactivation of MAPK, but not MDK (also known as MEK), has been discovered in the ARF1 mutant oocytes, and further demonstrated that ARF1, MAPK pathway plays an important role in regulating asymmetric cell division in meiosis I. Similarly, ARF1(T31N)-expressing superovulated MII oocytes underwent symmetric cell division in meiosis II when activation was performed. Rotation of MII spindle for 90 degree was prohibited in ARF1(T31N) expressing MII oocytes. Taken together, our results suggest that ARF1 plays an essential role in regulating asymmetric cell division in female meiosis.Microinjection of mRNA of a dominant negative mutant form of ARF1 (ARF1(T31N)) into fully grown germinal vesicle oocytes led to symmetric cell division in meiosis I, generating two metaphase II (MII) oocytes of equal size. Subsequently, the two MII oocytes of equal size underwent the second round of symmetric cell division to generate a 4-cell embryo (zygote) when activated parthenogenetically or via sperm injection. Furthermore, inactivation of MAP kinase, but not MEK, has been discovered in the ARF1 mutant oocytes, and further demonstrated that ARF1, MAPK pathway plays an important role in regulating asymmetric cell division in meiosis I. Similarly, ARF1(T31N)-expressing superovulated MII oocytes underwent symmetric cell division in meiosis II when activation was performed. Rotation of MII spindle for 90 degree was prohibited in ARF1(T31N) expressing MII oocytes. Taken together, our results suggest that ARF1 plays an essential role in regulating asymmetric cell division in female meiosis.