ArticlePloS one2012
Analysis of Gga null mice demonstrates a non-redundant role for mammalian GGA2 during development.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- GGAs: Regulation of Multiple Sorting Pathways and Potential Association With Human Diseases.Journal of cellular and molecular medicine · 2026Review
- Computational identification of disease models through cross-species phenotype comparison.Disease models & mechanisms · 2024Article
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- Article
- Clathrin adapters AP-1 and GGA2 support expression of epidermal growth factor receptor for cell growth.Oncogenesis · 2021Article
- Inactivation of the three GGA genes in HeLa cells partially compromises lysosomal enzyme sorting.FEBS open bio · 2021Article
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- Induction of membrane curvature by proteins involved in Golgi trafficking.Advances in biological regulation · 2020Review
- Cargo Sorting at theCells · 2019Review
- GGA2 interacts with EGFR cytoplasmic domain to stabilize the receptor expression and promote cell growth.Scientific reports · 2018Article
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- Conserved role for Gga proteins in phosphatidylinositol 4-kinase localization to theProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Genetic Deletion of the Clathrin Adaptor GGA3 Reduces Anxiety and Alters GABAergic Transmission.PloS one · 2016Article
- Impact of genetic background on neonatal lethality of Gga2 gene-trap mice.G3 (Bethesda, Md.) · 2014Article
- Clathrin terminal domain-ligand interactions regulate sorting of mannose 6-phosphate receptors mediated by AP-1 and GGA adaptors.The Journal of biological chemistry · 2014Article
- Distinct and overlapping roles for AP-1 and GGAs revealed by the "knocksideways" system.Current biology : CB · 2012Article
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Authors and funding
4 authors.
Funding
Abstract
Numerous studies using cultured mammalian cells have shown that the three GGAs (Golgi-localized, gamma-ear containing, ADP-ribosylation factor- binding proteins) function in the transport of cargo proteins between the trans- Golgi network and endosomes. However, the in vivo role(s) of these adaptor proteins and their possible functional redundancy has not been analyzed. In this study, the genes encoding GGAs1-3 were disrupted in mice by insertional mutagenesis. Loss of GGA1 or GGA3 alone was well tolerated whereas the absence of GGA2 resulted in embryonic or neonatal lethality, depending on the genetic background of the mice. Thus, GGA2 mediates a vital function that cannot be compensated for by GGA1and/or GGA3. The combined loss of GGA1 and GGA3 also resulted in a high incidence of neonatal mortality but in this case the expression level of GGA2 may be inadequate to compensate for the loss of the other two GGAs. We conclude that the three mammalian GGAs are essential proteins that are not fully redundant.
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