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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Golgin A3

golgin-160, MEA-2, Golga3, GCP170
The Golgi apparatus, which participates in glycosylation and transport of proteins and lipids in the secretory pathway, consists of a series of stacked cisternae (flattened membrane sacs). Interactions between the Golgi and microtubules are thought to be important for the reorganization of the Golgi after it fragments during mitosis. This gene encodes a member of the golgin family of proteins which are localized to the Golgi. Its encoded protein has been postulated to play a role in nuclear transport and Golgi apparatus localization. Several alternatively spliced transcript variants that encode different protein isoforms have been described for this gene. [provided by RefSeq, Feb 2010] (from NCBI)
Top mentioned proteins: PrP, ACID, fibrillin-1, GM130, caspase-2
Papers on golgin-160
Interactome analysis reveals that FAM161A, deficient in recessive retinitis pigmentosa, is a component of the Golgi-centrosomal network.
Rivolta et al., Lausanne, Switzerland. In Hum Mol Genet, Jul 2015
Notable FAM161A interactors included AKAP9, FIP3, GOLGA3, KIFC3, KLC2, PDE4DIP, NIN and TRIP11.
Draft genomes of two sordariomycete fungi that produce novel secondary metabolites.
Stevenson et al., Norman, United States. In Genome Announc, 2014
The genomes of two fungi isolated from soil (MEA-2) and sediment (SUP5-1) were sequenced.
Three basic residues of intracellular loop 3 of the beta-1 adrenergic receptor are required for golgin-160-dependent trafficking.
Machamer et al., Baltimore, United States. In Int J Mol Sci, 2013
Golgin-160 is a member of the golgin family of proteins, which have been implicated in the maintenance of Golgi structure and in vesicle tethering.
New point mutation in Golga3 causes multiple defects in spermatogenesis.
Linder et al., United States. In Andrology, 2013
Mice with repro27 exhibit fully penetrant male-specific infertility associated with a nonsense mutation in the golgin subfamily A member 3 gene (Golga3).
Caspase-2 is involved in cell death induction by taxanes in breast cancer cells.
Kovář et al., In Cancer Cell Int, 2012
Caspase-2 activation was confirmed by decreasing levels of procaspase-2, increasing levels of cleaved caspase-2 and the cleavage of caspase-2 substrate golgin-160.
Golgin160 recruits the dynein motor to position the Golgi apparatus.
Linstedt et al., Pittsburgh, United States. In Dev Cell, 2012
Golgi protein golgin160 recruits dynein to Golgi membranes.
Genome-wide association study of antibody response to smallpox vaccine.
Poland et al., Rochester, United States. In Vaccine, 2012
Additional SNP associations in Hispanics (p≤3.40×10(-7)) were mapped to the KIF6/LOC100131899, CYP2C9, and ANKLE2/GOLGA3 genes.
Identification of a common autoantigenic epitope of protein disulfide isomerase, golgin-160 and voltage-gated potassium channel in type 1 diabetes.
Saura et al., Roma, Italy. In Diabetes Res Clin Pract, 2010
A common epitope of proteins golgin-160, voltage-gated potassium channel and disulfide isomerase was identified by screening with autoantibodies of a type 1 diabetic patient
Modulation of amyloid-β peptide-induced toxicity through inhibition of JNK nuclear localization and caspase-2 activation.
Rodrigues et al., Lisbon, Portugal. In J Alzheimers Dis, 2009
Furthermore, active caspase-2 cleaved golgin-160 and was localized to the Golgi complex.
Listeria monocytogenes ActA-mediated escape from autophagic recognition.
Sasakawa et al., Tokyo, Japan. In Nat Cell Biol, 2009
The ability of ActA to mediate protection from ubiquitylation was further demonstrated by generating aggregate-prone GFP-ActA-Q79C and GFP-ActA-170(*) chimaeras, consisting of GFP (green fluorescent protein), the ActA protein and segments of polyQ or Golgi membrane protein GCP170 (ref.
A primary role for Golgi positioning in directed secretion, cell polarity, and wound healing.
Linstedt et al., Pittsburgh, United States. In Mol Biol Cell, 2009
Here, we identify golgin-160 and GMAP210 as proteins required for centripetal motility of Golgi membranes.
D-amino acids in the brain: the biochemistry of brain serine racemase.
Rodríguez-Crespo et al., Madrid, Spain. In Febs J, 2008
Several yeast two-hybrid screens for interaction partners identified the proteins glutamate receptor interacting protein, protein interacting with C kinase 1 and Golga3 to bind to serine racemase, having different effects on its catalytic activity or stability.
A novel 165-kDa Golgin protein induced by brain ischemia and phosphorylated by Akt protects against apoptosis.
Sharp et al., Sacramento, United States. In Mol Cell Neurosci, 2007
A cDNA encoding a novel protein was cloned from ischemic rat brain and found to be homologous to testis Mea-2 Golgi-associated protein (Golga3).
Identification of a redox-sensitive cysteine in GCP60 that regulates its interaction with golgin-160.
Machamer et al., Baltimore, United States. In J Biol Chem, 2007
nuclear translocation of golgin-160-(140-311) is a highly coordinated event regulated not only by cleavage of the golgin-160 head but also by the oxidation state of GCP60
Fragmentation of the Golgi apparatus: an early apoptotic event independent of the cytoskeleton.
Shields et al., United States. In Traffic, 2007
Finally, in response to Fas receptor activation or staurosporine treatment the levels of beta-actin or alpha-tubulin remained unaltered, whereas several Golgi proteins, p115 and golgin-160, underwent caspase-mediated cleavage.
Golgin-160 is required for the Golgi membrane sorting of the insulin-responsive glucose transporter GLUT4 in adipocytes.
Pessin et al., Stony Brook, United States. In Mol Biol Cell, 2006
These data demonstrate that golgin-160 plays an important role in directing insulin-regulated trafficking proteins toward the insulin-responsive compartment in adipocytes.
Golgin-160 promotes cell surface expression of the beta-1 adrenergic receptor.
Machamer et al., Baltimore, United States. In Traffic, 2006
golgin-160 may promote efficient surface delivery of a subset of cargo molecules
Emergence of complex rearrangements at translocation breakpoints in a transgenic mouse; implications for mechanisms involved in the formation of chromosome rearrangements.
Ferguson-Smith et al., Yokohama, Japan. In Cytogenet Genome Res, 2006
Analysis of the breakpoint junctions in our previous studies showed that the ada transgene was integrated at the breakpoint forming a fusion gene with Golga3 (Mea2).
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