ArticleProceedings of the National Academy of Sciences of the United States of America2007
BIG1, a brefeldin A-inhibited guanine nucleotide-exchange protein, is required for correct glycosylation and function of integrin beta1.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
28 citing papers in PubMed, 47 citations in OpenAlex.
- Comparative proteomic analysis indicates differential responses to fumonisin BMycotoxin research · 2025Article
- The lipid flippase ATP8A1 regulates the recruitment of ARF effectors to the trans-Golgi Network.Archives of biochemistry and biophysics · 2024Article
- Expanding the Phenotypic and Genotypic Spectrum ofFrontiers in molecular neuroscience · 2022Article
- ARL15 modulates magnesium homeostasis through N-glycosylation of CNNMs.Cellular and molecular life sciences : CMLS · 2021Article
- The NLRP3-inflammasome as a sensor of organelle dysfunction.The Journal of cell biology · 2020Review
- Article
- BIG1 controls macrophage pro-inflammatory responses through ARF3-mediated PI(4,5)P2 synthesis.Cell death & disease · 2020Article
- Podocyte-Specific Sialylation-Deficient Mice Serve as a Model for Human FSGS.Journal of the American Society of Nephrology : JASN · 2019Article
- Promiscuity of the catalytic Sec7 domain within the guanine nucleotide exchange factor GBF1 in ARF activation, Golgi homeostasis, and effector recruitment.Molecular biology of the cell · 2019Article
- Cell-matrix adhesion controls Golgi organization and function through Arf1 activation in anchorage-dependent cells.Journal of cell science · 2018Article
- Brefeldin A-Inhibited Guanine Nucleotide-Exchange Factor 1 (BIG1) Governs the Recruitment of Tumor Necrosis Factor Receptor-Associated Factor 2 (TRAF2) to Tumor Necrosis Factor Receptor 1 (TNFR1) Signaling Complexes.International journal of molecular sciences · 2016Article
- Arf proteins in cancer cell migration.Small GTPases · 2016Review
- Enhancement of β-catenin activity by BIG1 plus BIG2 via Arf activation and cAMP signals.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Oligomerization of the Sec7 domain Arf guanine nucleotide exchange factor GBF1 is dispensable for Golgi localization and function but regulates degradation.American journal of physiology. Cell physiology · 2016Article
- Regulating the large Sec7 ARF guanine nucleotide exchange factors: the when, where and how of activation.Cellular and molecular life sciences : CMLS · 2014Review
- BIG1, a brefeldin A-inhibited guanine nucleotide-exchange factor, is required for GABA-gated Cl⁻ influx through regulation of GABAA receptor trafficking.Molecular neurobiology · 2014Article
- N-ethylmaleimide-sensitive factor attachment protein α (αSNAP) regulates matrix adhesion and integrin processing in human epithelial cells.The Journal of biological chemistry · 2014Article
- Arf guanine nucleotide-exchange factors BIG1 and BIG2 regulate nonmuscle myosin IIA activity by anchoring myosin phosphatase complex.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- BIG1, a brefeldin A-inhibited guanine nucleotide-exchange protein modulates ATP-binding cassette transporter A-1 trafficking and function.Arteriosclerosis, thrombosis, and vascular biology · 2013Article
- Brefeldin A-inhibited ADP-ribosylation factor activator BIG2 regulates cell migration via integrin β1 cycling and actin remodeling.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Glycosylation of beta1 integrin (beta1) in the Golgi complex has been related to its function in multiple cell processes, e.g., invasiveness, matrix adhesion, and migration. Brefeldin A-inhibited guanine nucleotide-exchange proteins (BIG) 1 and BIG2 activate human ADP-ribosylation factors (ARF) 1 and ARF3 by catalyzing the replacement of ARF-bound GDP with GTP to regulate Golgi vesicular transport. We show here a requirement for BIG1 (but not BIG2) in glycosylation and function of beta1. In HepG2 cells treated for 48 or 72 h with BIG1, but not BIG2, siRNA, both the amount and electrophoretic mobility of the initially 130-kDa beta1 were increased. BIG1 content had risen by 48 h after removal of BIG1 siRNA, and the faster-migrating, aberrant 130-kDa beta1 was not seen. Peptide N-glycosidase F, but not endoglycosidase H, digestion converted all beta1 to an approximately 85-kDa (core protein) form. By electron microscopy, Golgi membranes in BIG1-depleted cells were less sharply defined than those in mock or BIG2 siRNA-treated cells, with more vesicle-like structures at the transface. Amounts of active RhoA-GTP also were decreased in such cells and restored by overexpression of HA-BIG1. Aberrant beta1 was present on the cell surface, but its function in cell spreading, adhesion, and migration was impaired. By immunofluorescence microscopy, BIG1 siRNA-treated cells showed less spreading and concentration of beta1 at the cell surface. These results indicate a previously unrecognized role for BIG1 in the glycosylation of beta1 by Golgi enzymes, which is critical for its function in developmental and other vital cell processes.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.