ARL3 Antibody

1. By molecular functional analysis, we observed that ARL3 promotes the aggregation of GFP-LC3, up-regulation of LC3-II/LC3-I and down-regulation of SQSMT1/BECN1, and knocking down of ARL3 inbibits autophagy, which suggested that ARL3 is necessary for autophagy. PMID: 30227171
2. this study identifies ARL3 as a key player in prenylated protein trafficking in rod photoreceptor cells and establishes the potential role for ARL3 dysregulation in the pathogenesis of RP2-related forms of XLRP PMID: 26936825
3. Studies indicate that the binding of UNC119 and PDE6D, to the lipid-modified ciliary cargo and the specific release of the cargo in the cilia by the ciliary small G-protein Arl3 in a GTP-dependent manner. PMID: 27911709
4. Biochemical characterization of purified mammalian ARL13B protein indicates that it is an atypical GTPase and ARL3 guanine nucleotide exchange factor (GEF).( PMID: 28487361
5. These results indicate that ARL3 interacts with STAT3 and regulates the transcriptional activation of STAT3 by influencing its nuclear accumulation of STAT3. PMID: 27048653
6. De Novo Occurrence of a Variant in ARL3 and Apparent Autosomal Dominant Transmission of Retinitis Pigmentosa. PMID: 26964041
7. Arl3 acts negatively in ciliogenesis but positively in cilia signaling (Review). PMID: 23548655
8. When Arl3 binds UNC119, it allosterically displaces cargo by accelerating its release by 3 orders of magnitude. The N-terminal amphipathic helix of Arl3.GppNHp is not displaced by the interswitch toggle but remains bound on the surface of the protein. PMID: 22960633
9. The G proteins Arl3 acts in a GTP-dependent manner as allosteric release factors for farnesylated cargo. PMID: 22002721
10. We propose that RP2 regulation of Arl3 is important for maintaining Golgi cohesion, facilitating the transport and docking of vesicles and thereby carrying proteins to the base of the photoreceptor connecting cilium for transport to the outer segment. PMID: 20106869
11. Knockdown of Arl3 by siRNA resulted in changes in cell morphology, increased acetylation of alpha-tubulin, failure of cytokinesis, and increased number of binucleated cells. PMID: 16525022

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HGNC: 694

OMIM: 604695

KEGG: hsa:403

STRING: 9606.ENSP00000260746

UniGene: Hs.182215