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

Golgin A1

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 one of the golgins, a family of proteins localized to the Golgi. This encoded protein is associated with Sjogren's syndrome. [provided by RefSeq, Feb 2010] (from NCBI)
Top mentioned proteins: ARF3, HAD, GM130, TGN38, GCC185
Papers on golgin-97
Arfaptin-1 negatively regulates Arl1-mediated retrograde transport.
Yu et al., Taiwan. In Plos One, 2014
Exogenous arfaptin-1 expression did not interfere with the localization of the Arl1-interacting proteins golgin-97 and golgin-245 to the TGN and vice versa.
Enhanced myometrial autophagy in postpartum uterine involution.
Huang et al., Tainan City, Taiwan. In Taiwan J Obstet Gynecol, 2014
For cell hypertrophy analysis, organelle proteins, β-actin, prohibin, calnexin, and golgin-97 were analyzed by Western blotting.
Intracellular distribution of the ΔNp73 protein isoform in medulloblastoma cells: a study with newly generated rabbit polyclonal antibodies.
Zitterbart et al., Brno, Czech Republic. In Histol Histopathol, 2013
By double-labeling with ΔNp73 and golgin-97, we showed the co-localization of the ΔNp73 isoform with the Golgi apparatus.
Trafficking of the Menkes copper transporter ATP7A is regulated by clathrin-, AP-2-, AP-1-, and Rab22-dependent steps.
Monaco et al., Oxford, United Kingdom. In Mol Biol Cell, 2013
These appear to be a subdomain of the mammalian TGN, showing only partial overlap with the TGN marker golgin-97.
Molecular basis of insulin-responsive GLUT4 trafficking systems revealed by single molecule imaging.
Kanzaki et al., Sendai, Japan. In Traffic, 2011
Specifically, (i) the endosomes-to-trans-Golgi network (TGN) retrieval system specialized for GLUT4 develops in response to sortilin expression, which requires an intricately balanced interplay among retromers, golgin-97 and syntaxin-6, the housekeeping vesicle trafficking machinery.
SFTA2--a novel secretory peptide highly expressed in the lung--is modulated by lipopolysaccharide but not hyperoxia.
Holzinger et al., München, Germany. In Plos One, 2011
In accordance with other hydrophilic surfactant proteins, SFTA2 did not colocalize with lamellar bodies but colocalized with golgin97 and clathrin-labelled vesicles, suggesting a classical secretory pathway for its expression and secretion.
Arfaptins are localized to the trans-Golgi by interaction with Arl1, but not Arfs.
Shin et al., Kyoto, Japan. In J Biol Chem, 2011
We also demonstrate that arfaptins interact with Arl1 through their BAR domain-containing region and compete for Arl1 binding with golgin-97 and golgin-245/p230, both of which also bind to Arl1 through their GRIP (golgin-97/RanBP2/Imh1p/p230) domains.
FIP1/RCP binding to Golgin-97 regulates retrograde transport from recycling endosomes to the trans-Golgi network.
Prekeris et al., Aurora, United States. In Mol Biol Cell, 2010
FIP1/RCP binding to Golgin-97 is required for tethering and fusion of recycling endosome-derived retrograde transport vesicles to the trans-Golgi network.
The localization of the Golgin GCC185 is independent of Rab6A/A' and Arl1.
Gleeson et al., Melbourne, Australia. In Cell, 2009
The localization of two TGN golgins, p230/golgin-245 and golgin-97, is mediated by the small GTPase Arl1, whereas recruitment of the TGN golgin GCC185 is controversial.
The golgin GCC88 is required for efficient retrograde transport of cargo from the early endosomes to the trans-Golgi network.
Gleeson et al., Melbourne, Australia. In Mol Biol Cell, 2007
Of the four TGN golgins, p230/golgin-245, golgin-97, GCC185, and GCC88, we show that GCC88 defines a retrograde transport pathway from early endosomes to the TGN.
A specific inhibitor of cholesterol biosynthesis, BM15.766, reduces the expression of beta-secretase and the production of amyloid-beta in vitro.
Austen et al., London, United Kingdom. In J Neurochem, 2007
Similar changes were observed in the expression of the Golgi marker golgin-97, suggesting that reduced BACE expression may arise from a decrease in protein trafficking and an increase in degradation.
A host cell membrane protein, golgin-97, is essential for poxvirus morphogenesis.
Hruby et al., Corvallis, United States. In Virology, 2007
Using RNA interference approach, it was demonstrated that a cellular trans-Golgi network membrane protein, golgin-97, is essential for Vaccinia virus replication.
The trans-Golgi network golgin, GCC185, is required for endosome-to-Golgi transport and maintenance of Golgi structure.
Gleeson et al., Melbourne, Australia. In Traffic, 2007
The TGN golgins, p230/golgin-245 and golgin-97, are recruited via the GTPase Arl1, whereas the TGN golgin GCC185 is recruited independently of Arl1.
A trans-Golgi network resident protein, golgin-97, accumulates in viral factories and incorporates into virions during poxvirus infection.
Hruby et al., Corvallis, United States. In J Virol, 2006
In the work described here, we demonstrate that a host cell protein residing in the trans-Golgi network membrane, golgin-97, is transported to the sites of virus replication and assembly and becomes incorporated into the virions during poxvirus infection.
Multilayer interactions determine the Golgi localization of GRIP golgins.
Hong et al., Singapore, Singapore. In Traffic, 2006
Golgin-97, RanBP2alpha, Imh1p and p230/golgin-245 (GRIP) domain golgins are targeted to the Golgi membrane through their GRIP domains.
E-cadherin transport from the trans-Golgi network in tubulovesicular carriers is selectively regulated by golgin-97.
Stow et al., Brisbane, Australia. In Traffic, 2005
Selective and essential component of the tubulovesicular carriers transporting E-cadherin out of the trans-Golgi network.
The trans-Golgi network GRIP-domain proteins form alpha-helical homodimers.
Gleeson et al., Melbourne, Australia. In Biochem J, 2005
The ability of the four mammalian GRIP domain proteins, p230, golgin-97, GCC88, and GCC185 to interact is reported.
Autoantigen Golgin-97, an effector of Arl1 GTPase, participates in traffic from the endosome to the trans-golgi network.
Hong et al., Singapore, Singapore. In Mol Biol Cell, 2004
Data show that Arl1 regulates the membrane recruitment of Golgin-97, which plays a role in transport from the endosome to the trans-Golgi network.
Autoantibodies to protein transport and messenger RNA processing pathways: endosomes, lysosomes, Golgi complex, proteasomes, assemblyosomes, exosomes, and GW bodies.
Fritzler et al., Calgary, Canada. In Clin Immunol, 2004
Autoantigens in the Golgi complex include giantin/macrogolgin, golgin-245, golgin 160, golgin-97, golgin 95/gm130, and golgin-67.
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