Characterization, Chromosomal Localization, and Expression during Hematopoietic Differentiation of the Gene Encoding Arl6ip, ADP-Ribosylation-like Factor-6 Interacting Protein (ARL6)

Pettersson, M; Bessonova, Marina; Gu, Harvest F.; Groop, Leif; Jönsson, Jan‐Ingvar

doi:10.1006/geno.2000.6278

Cited by 30 publications

(27 citation statements)

References 10 publications

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“…3B), suggesting a link to membrane trafficking. This link is further strengthened by the microarray data revealing genes affected by C5orf30 depletion in RASFs such as ARL6IP1, a transmembrane protein involved in membrane protein transport in hematopoietic cells (33); and ERC1, a Rab6 endosomes-interacting protein essential for cell migration and adhesion turnover (34). C5orf30 proteins do not show any similarity to any characterized protein sequence, making impossible the inference of its cellular function from homology; nonetheless, their amino acid composition makes them positively charged at physiological conditions, suggesting that natural interacting partners are negatively charged molecules, such as lipids or phosphorylated cargo.…”

Section: Discussionmentioning

confidence: 94%

C5orf30 is a negative regulator of tissue damage in rheumatoid arthritis

Muthana

Hawtree

Wilshaw

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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The variant rs26232, in the first intron of the chromosome 5 open reading frame 30 (C5orf30) locus, has recently been associated with both risk of developing rheumatoid arthritis (RA) and severity of tissue damage. The biological activities of human C5orf30 are unknown, and neither the gene nor protein show significant homology to any other characterized human sequences. The C5orf30 gene is present only in vertebrate genomes with a high degree of conservation, implying a central function in these organisms. Here, we report that C5orf30 is highly expressed in the synovium of RA patients compared with control synovial tissue, and that it is predominately expressed by synovial fibroblast (RASF) and macrophages in the lining and sublining layer of the tissue. These cells play a central role in the initiation and perpetuation of RA and are implicated in cartilage destruction. RASFs lacking C5orf30 exhibit increased cell migration and invasion in vitro, and gene profiling following C5orf30 inhibition confirmed up-regulation of genes involved in cell migration, adhesion, angiogenesis, and immune and inflammatory pathways. Importantly, loss of C5orf30 contributes to the pathology of inflammatory arthritis in vivo, because inhibition of C5orf30 in the collagen-induced arthritis model markedly accentuated joint inflammation and tissue damage. Our study reveal C5orf30 to be a previously unidentified negative regulator of tissue damage in RA, and this protein may act by modulating the autoaggressive phenotype that is characteristic of RASFs.

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Section: Discussionmentioning

confidence: 94%

C5orf30 is a negative regulator of tissue damage in rheumatoid arthritis

Muthana

Hawtree

Wilshaw

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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“…The Arl6ip1 protein was first identified by yeast two-hybrid screening using mouse ARL6 as bait (Ingley et al, 1999) and as a negative regulatory factor during myeloid differentiation by differential display (Pettersson et al, 2000). Moreover, a novel protein, designated ARMER, initially discovered as a false-positive clone by yeast two-hybrid screening using Bcl-xL as bait, is also Arl6ip1 (Lui et al, 2003).…”

Section: Arl6ip1mentioning

confidence: 99%

“…In addition, Arl6ip1 has more than 96% homology with the human protein KIAA0069, the product of a cDNA isolated from the human myeloblast cell line KG-1 during a systematic effort to characterize complete cDNAs (Nomura et al, 1994). Amino acid analysis of Arl6ip1 demonstrates that it is composed of 203 amino acids and encodes a 23-kDa protein with four putative transmembrane segments (Pettersson et al, 2000). Several studies indicate that Arl6ip1 is an integral membrane protein localized to the ER (Lui et al, 2003;Pettersson et al, 2000).…”

Section: Arl6ip1mentioning

confidence: 99%

“…Amino acid analysis of Arl6ip1 demonstrates that it is composed of 203 amino acids and encodes a 23-kDa protein with four putative transmembrane segments (Pettersson et al, 2000). Several studies indicate that Arl6ip1 is an integral membrane protein localized to the ER (Lui et al, 2003;Pettersson et al, 2000). Furthermore, computational analysis of the topology of Arl6ip1 demonstrates that the N-and C-terminal ends are both exposed to the cytoplasm (Lui et al, 2003).…”

Section: Arl6ip1mentioning

confidence: 99%

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Modulation of EAAC1-Mediated Glutamate Uptake by Addicsin

Ikemoto¹,

Arano²

2012

Biochemistry

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“…Previous studies have shown that ARL6IP1 protects HT1080 fibrosarcoma cells by inhibiting caspase-9 activity and reveal a possible role for ARL6IP1 in cell survival (18). ARL6IP1 was also isolated as a down-regulatory factor during myeloid differentiation by differential display and ARL6IP1 gene is suggested to be involved in protein transport, membrane trafficking, or cell signaling during hematopoietic maturation (19).…”

Section: Introductionmentioning

confidence: 99%

ARL6IP1 mediates cisplatin-induced apoptosis in CaSki cervical cancer cells

Li¹,

Liu²,

Wang³

et al. 2010

Oncol Rep

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Abstract. Cisplatin has been shown to induce apoptosis in various types of cancer cells. Despite the great efficacy at treating certain kinds of cancers, cisplatin introduced into clinical use shows side effects and the acquisition or presence of resistance to the drug. Thus, it is important that we further understand the anti-cancer mechanism of cisplatin with the goal of enhancing its efficacy. ADP-ribosylation factor-like 6 interacting protein 1 (ARL6IP1) is an apoptotic regulator. We studied cisplatin-induced apoptosis with suppression of ARL6IP1 expression in CaSki cervical cancer cells. Exogenous expression of ARL6IP1 suppressed cisplatin-induced apoptosis in CaSki cells, and siRNAinduced silencing of ARL6IP1 triggered apoptosis in CaSki cells even in the absence of other apoptotic stimuli. Cisplatin treatment induced caspase-3, -9, p53, Bax, NF-κB and MAPK expression, and suppressed Bcl-2 and Bcl-xl expression, whereas cells transfected with pcDNA3.1-ARL6IP1 showed lower levels of cisplatin-induced caspase-3, -9, p53, Bax, NF-κB and MAPK up-regulation and higher levels of cisplatin-suppressed Bcl-2 and Bcl-xl downregulation. These novel findings collectively suggest that ARL6IP1 may play a key role in cisplatin-induced apoptosis in CaSki cervical cancer cells by regulating the expression of apoptosis-associated proteins such as caspase-3, -9, p53, NF-κB, MAPK, Bcl-2, Bcl-xl, and Bax.

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Characterization, Chromosomal Localization, and Expression during Hematopoietic Differentiation of the Gene Encoding Arl6ip, ADP-Ribosylation-like Factor-6 Interacting Protein (ARL6)

Cited by 30 publications

References 10 publications

C5orf30 is a negative regulator of tissue damage in rheumatoid arthritis

C5orf30 is a negative regulator of tissue damage in rheumatoid arthritis

Modulation of EAAC1-Mediated Glutamate Uptake by Addicsin

ARL6IP1 mediates cisplatin-induced apoptosis in CaSki cervical cancer cells

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