The DOI matches its Crossref record.
A Family of Proteins with γ-Adaptin and Vhs Domains That Facilitate Trafficking between the Trans-Golgi Network and the Vacuole/Lysosome
Abstract
We have cloned and characterized members of a novel family of proteins, the GGAs. These proteins contain an NH2-terminal VHS domain, one or two coiled-coil domains, and a COOH-terminal domain homologous to the COOH-terminal “ear” domain of γ-adaptin. However, unlike γ-adaptin, the GGAs are not associated with clathrin-coated vesicles or with any of the components of the AP-1 complex. GGA1 and GGA2 are also not associated with each other, although they colocalize on perinuclear membranes. Immunogold EM shows that these membranes correspond to trans elements of the Golgi stack and the TGN. GST pulldown experiments indicate that the GGA COOH-terminal domains bind to a subset of the proteins that bind to the γ-adaptin COOH-terminal domain. In yeast there are two GGA genes. Deleting both of these genes results in missorting of the vacuolar enzyme carboxypeptidase Y, and the cells also have a defective vacuolar morphology phenotype. These results indicate that the function of the GGAs is to facilitate the trafficking of proteins between the TGN and the vacuole, or its mammalian equivalent, the lysosome.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
GGA proteins are monomeric adaptor proteins that mediate transport of cargo proteins between the TGN and endosomes.
“GGA proteins are monomeric adaptor proteins that mediate transport of cargo proteins between the TGN and endosomes”
From GGA1 Is Expressed in the Human Brain and Affects the Generation of Amyloid β-Peptide (2006) · cites this paper as Hirst et al., 2000
The Abstract and Discussion support a role for GGAs in trafficking proteins from the TGN toward the vacuole or lysosome, and report that GGA1 and GGA2 are not associated with each other or AP-1. The Discussion does not establish monomeric adaptor status and explicitly leaves open whether the trafficking step runs from the late Golgi to a prevacuolar endosomal compartment. (LLM, conf=0.86)
Experimental — accuracy not yet measuredGGA2 belongs to a recently described family of monomeric cytosolic proteins that includes three mammalian and two yeast members.
“GGA2 belongs to a recently described family of monomeric cytosolic proteins that includes three mammalian and two (gga) yeast members (Boman et al., 2000;Dell'Angelica et al., 2000;Hirst et al., 2000;Poussu et al., 2000;Takatsu et al., 2000).”
From The sortilin cytoplasmic tail conveys Golgi–endosome transport and binds the VHS domain of the GGA2 sorting protein (2001) · cites this paper as Hirst et al., 2000
Vps10p-mediated sorting of CPY is impaired in gga null cells.
“Thus, Vps10p-mediated sorting of CPY is impaired in gga null cells (Hirst et al., 2000)”
From The sortilin cytoplasmic tail conveys Golgi–endosome transport and binds the VHS domain of the GGA2 sorting protein (2001) · cites this paper as Hirst et al., 2000
Important findings in yeast convincingly implicate the GGA family in Golgi-endosome/lysosome transport.
“Information concerning their physiological function is still limited, but important ®ndings in yeast convincingly implicate the family in Golgi±endosome/lysosome transport.”
From The sortilin cytoplasmic tail conveys Golgi–endosome transport and binds the VHS domain of the GGA2 sorting protein (2001) · cites this paper as Hirst et al., 2000
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
No references could be resolved yet.
Research works printed but not linked: 37
- Asao, 1997, Hrs is associated with STAM, a signal-transducing adaptor molecule. Its suppressive effect on cytokine-induced cell growth, J. Biol. Chem., 272, 32785, 10.1074/jbc.272.52.32785 · DOI
- Boman, 2000, A family of Arf effectors that can alter membrane transport through the trans-Golgi, Mol. Biol. Cell., In press
- Cereghino, 1995, The cytoplasmic tail domain of the vacuolar protein sorting receptor Vps10p and a subset of VPS gene products regulate receptor stability, function and localisation, Mol. Biol. Cell, 6, 1089, 10.1091/mbc.6.9.1089 · DOI
- Cowles, 1997, The AP-3 adaptor complex is essential for cargo-selective transport to the yeast vacuole, Cell, 91, 109, 10.1016/S0092-8674(01)80013-1 · DOI
- Dell'Angelica, 1997, An adaptor-like protein complex with ubiquitous expression, EMBO (Eur. Mol. Biol. Organ.) J., 16, 917, 10.1093/emboj/16.5.917 · DOI
- Dell'Angelica, 1999, AP-4, a novel protein complex related to clathrin adaptors, J. Biol. Chem., 274, 7278, 10.1074/jbc.274.11.7278 · DOI
- Dell'Angelica, 2000, GGAsa family of ADP ribosylation factor-binding proteins related to adaptors and associated with the Golgi complex, J. Cell Biol., 149, 81, 10.1083/jcb.149.1.81 · DOI · Paper page
- Futter, 1998, In polarized MDBK cells basolateral vesicles arise from clathrin-gamma-adaptin-coated domains on endosomal tubules, J. Cell Biol., 141, 611, 10.1083/jcb.141.3.611 · DOI
- Hirst, 1998, Clathrin and adaptors, Biochim. Biophys. Acta, 1401, 173, 10.1016/S0167-4889(98)00056-1 · DOI
- Hirst, 1999, Characterization of a fourth adaptor-related protein complex, Mol. Biol. Cell, 10, 2787, 10.1091/mbc.10.8.2787 · DOI
- Huang, 1999, Clathrin functions in the absence of heterotetrameric adaptors and AP180-related proteins in yeast, EMBO (Eur. Mol. Biol. Organ.) J., 18, 3897, 10.1093/emboj/18.14.3897 · DOI
- Komada, 1997, Hrs, a tyrosine kinase substrate with a conserved double zinc finger domain, is localized to the cytoplasmic surface of early endosomes, J. Biol. Chem., 272, 20538, 10.1074/jbc.272.33.20538 · DOI
- Lohi, 1998, VHS domain marks a group of proteins involved in endocytosis and vesicular trafficking, FEBS Lett., 440, 255, 10.1016/S0014-5793(98)01401-X · DOI
- Lohi, 1998, EAST, an epidermal growth factor receptor- and Eps15-associated protein with Src homology 3 and tyrosine-based activation motif domains, J. Biol. Chem., 273, 21408, 10.1074/jbc.273.33.21408 · DOI
- Manfredi, 1987, Purification and characterisation of two distinct complexes of assembly polypeptides from calf brain coated vesicles that differ in their polypeptide composition and kinase activities, J. Biol. Chem., 262, 12182, 10.1016/S0021-9258(18)45334-3 · DOI
- Marsh, 1999, The structural era of endocytosis, Science, 285, 215, 10.1126/science.285.5425.215 · DOI
- Nagase, 1995, Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121–KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1, DNA Res., 2, 167, 10.1093/dnares/2.4.167 · DOI
- Owen, 1999, A structural explanation for the binding of multiple ligands by the alpha-adaptin appendage domain, Cell, 97, 805, 10.1016/S0092-8674(00)80791-6 · DOI
- Page, 1995, Targeting signals and subunit interactions in coated vesicle adaptor complexes, J. Cell Biol., 131, 619, 10.1083/jcb.131.3.619 · DOI
- Page, 1999, γ-Synerginan EH domain-containing protein that interacts with γ-adaptin, J. Cell Biol., 146, 993, 10.1083/jcb.146.5.993 · DOI
- Payne, 1988, Protein transport to the vacuole and receptor-mediated endocytosis in clathrin heavy chain-deficient yeast, J. Cell Biol., 106, 1453, 10.1083/jcb.106.5.1453 · DOI
- Peyroche, 1996, Nucleotide exchange on ARF mediated by yeast Gea1 protein, Nature, 384, 479, 10.1038/384479a0 · DOI
- Piper, 1995, VPS27 controls vacuolar and endocytic traffic through a prevacuolar compartment in Saccharomyces cerevisiae, J. Cell Biol., 131, 603, 10.1083/jcb.131.3.603 · DOI
- Raymond, 1992, Morphological classification of the yeast vacuolar protein sorting mutantsevidence for a prevacuolar compartment in class E vps mutants, Mol. Biol. Cell, 3, 1389, 10.1091/mbc.3.12.1389 · DOI
- Robinson, 1992, Recruitment of coat proteins onto Golgi membranes in intact and permeabilized cellseffects of brefeldin A and G protein activators, Cell, 69, 129, 10.1016/0092-8674(92)90124-U · DOI
- Salcini, 1997, Binding specificity and in vitro targets of the EH domain, a novel protein–protein interaction module, Genes Dev., 11, 2239, 10.1101/gad.11.17.2239 · DOI · Paper page
- Sambrook, 1989, Molecular Cloning, A Laboratory Manual
- Seaman, 1993, Targeting and mistargeting of plasma membrane adaptors in vitro, J. Cell Biol., 123, 1093, 10.1083/jcb.123.5.1093 · DOI
- Seaman, 1997, Endosome to Golgi retrieval of the vacuolar protein sorting receptor, Vps10p, requires the function of the VPS29, VPS30, and VPS35 gene products, J. Cell Biol., 137, 79, 10.1083/jcb.137.1.79 · DOI · Paper page
- Seaman, 1996, Cytosolic and membrane-associated proteins involved in the recruitment of AP-1 adaptors onto the trans-Golgi network, J. Biol. Chem., 271, 25446, 10.1074/jbc.271.41.25446 · DOI
- Seeger, 1992, A role for clathrin in the sorting of vacuolar proteins in the Golgi complex of yeast, EMBO (Eur. Mol. Biol. Organ.) J., 11, 2811, 10.1002/j.1460-2075.1992.tb05348.x · DOI · Paper page
- Sikorski, 1989, A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae, Genetics, 122, 19, 10.1093/genetics/122.1.19 · DOI
- Simpson, 1996, A novel adaptor-related protein complex, J. Cell Biol., 133, 749, 10.1083/jcb.133.4.749 · DOI
- Simpson, 1999, SH3-domain-containing proteins function at distinct steps in clathrin-coated vesicle formation, Nat. Cell Biol., 1, 119, 10.1038/10091 · DOI
- Stamnes, 1993, The binding of AP-1 clathrin adaptor particles to Golgi membranes requires ADP-ribosylation factor, a small GTP-binding protein, Cell, 73, 999, 10.1016/0092-8674(93)90277-W · DOI · Paper page
- Vida, 1995, A new vital stain for visualizing vacuolar membrane dynamics and endocytosis in yeast, J. Cell Biol., 128, 779, 10.1083/jcb.128.5.779 · DOI
- Yeung, 1999, Adaptor complex-independent clathrin function in yeast, Mol. Biol. Cell, 10, 3643, 10.1091/mbc.10.11.3643 · DOI
Cited by
Sorted by citations
Nielsen, M. S., Madsen, P., Christensen, E. I., Nykjær, A., Gliemann, J., Kasper, D., Pohlmann, R., & Petersen, C. M. (2001) · The EMBO Journal · doi:10.1093/emboj/20.9.2180 · Cited by 457
GGA1 Is Expressed in the Human Brain and Affects the Generation of Amyloid β-Peptide
Wahle, T., Thal, D. R., Sastre, M., Rentmeister, A., Bogdanovic, N., Famulok, M., Heneka, M. T., & Walter, J. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.1982-06.2006 · Cited by 88
GGA function is required for maturation of neuroendocrine secretory granules
Kakhlon, O., Sakya, P., Larijani, B., Watson, R., & Tooze, S. A. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601067 · Cited by 45
Is It the Twilight of BACE1 Inhibitors?
Hrabinova, M., Pejchal, J., Kucera, T., Jun, D., Schmidt, M., & Soukup, O. (2020) · Current Neuropharmacology · doi:10.2174/1570159x18666200503023323 · Cited by 28
Metadata
- Authors
- Hirst, J., Lui, W. W. Y., Bright, N. A., Totty, N., Seaman, M. N. J., & Robinson, M. S.
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2000-04-03
- Volume
- 149
- Issue
- 1
- Pages
- 67-80
- ISSN
- 0021-9525
- 1540-8140
- PMC
- PMC2175106
- Cited by
- 291
- References
- 0
- Language
- en
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
