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Golgin A5

golgin-84, ret-II, GOLGA5, RFG5
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 protein is a coiled-coil membrane protein that has been postulated to play a role in vesicle tethering and docking. Translocations involving this gene and the ret proto-oncogene have been found in tumor tissues; the chimeric sequences have been designated RET-II and PTC5. [provided by RefSeq, Feb 2010] (from NCBI)
Top mentioned proteins: RET, V1a, Rab5, Rab6, ACID
Papers on golgin-84
Identification of PLP2 and RAB5C as novel TPD52 binding partners through yeast two-hybrid screening.
Byrne et al., Westmead, Australia. In Mol Biol Rep, 2014
A large, low-stringency yeast two-hybrid screen using full-length TPD52 bait identified known partners (TPD52, TPD52L1, TPD52L2, MAL2) and four other preys that reproducibly bound TPD52 and TPD52L1 baits (PLP2, RAB5C, GOLGA5, YIF1A).
Golgin-84-associated Golgi fragmentation triggers tau hyperphosphorylation by activation of cyclin-dependent kinase-5 and extracellular signal-regulated kinase.
Tian et al., Wuhan, China. In Neurobiol Aging, 2014
Simultaneously, golgin-84 and Golgi reassembly stacking protein 65, 2 important Golgi matrix proteins, were decreased in the brains of elder mice.
Chlamydia trachomatis infection prevents front-rear polarity of migrating HeLa cells.
Heuer et al., Berlin, Germany. In Cell Microbiol, 2013
Silencing of golgin-84 phenocopied this defect in the absence of the infection.
Transcriptional Changes of Blood Eosinophils After Methacholine Inhalation Challenge in Asthmatics.
Carlsten et al., Vancouver, Canada. In Genomics Insights, 2011
Notable changes included the GOLGA5 and METTL2B genes and the protein ubiquitination and CCR3 pathways.
Targeting of a chlamydial protease impedes intracellular bacterial growth.
Heuer et al., München, Germany. In Plos Pathog, 2011
GA fragmentation results from infection-associated cleavage of the integral GA protein, golgin-84.
Interaction of Golgin-84 with the COG complex mediates the intra-Golgi retrograde transport.
Oda et al., Niigata, Japan. In Traffic, 2010
Golgin-84 on coat protein I vesicles interacts with the conserved oligomeric Golgi complex before SNARE assembly.
PRMT5 regulates Golgi apparatus structure through methylation of the golgin GM130.
Bao et al., Beijing, China. In Cell Res, 2010
Some Golgi proteins including golgin-84 are also known to be methylated, but the function of golgin methylation remains unclear.
Rab6 and Rab11 regulate Chlamydia trachomatis development and golgin-84-dependent Golgi fragmentation.
Heuer et al., Berlin, Germany. In Plos Pathog, 2009
We further examined the interplay between these Rab proteins and the Golgi matrix components golgin-84 and p115 with regard to Chlamydia-induced Golgi fragmentation.
The COG complex, Rab6 and COPI define a novel Golgi retrograde trafficking pathway that is exploited by SubAB toxin.
Lupashin et al., Little Rock, United States. In Traffic, 2009
Surprisingly, depletion of Golgi tethers p115 and golgin-84 that regulates two previously described coat protein I (COPI) vesicle-mediated pathways did not interfere with SubAB trafficking, indicating that SubAB is exploiting a novel COG/Rab6/COPI-dependent retrograde trafficking pathway.
Identification of internal control genes for quantitative polymerase chain reaction in mammary tissue of lactating cows receiving lipid supplements.
Loor et al., College Park, United States. In J Dairy Sci, 2009
Among those COPS7A, CORO1B, DNAJC19, EIF3K, EMD, GOLGA5, MTG1, UXT, MRPL39, GPR175, and MARVELD1 (sample/reference expression ratio = 1 +/- 0.1) were selected for PCR analysis upon verification of goodness of BLAT/BLAST sequence and primer design.
Chlamydia causes fragmentation of the Golgi compartment to ensure reproduction.
Meyer et al., Berlin, Germany. In Nature, 2009
Ministack formation is triggered by the proteolytic cleavage of the Golgi matrix protein golgin-84.
Localization and domain characterization of Arabidopsis golgin candidates.
Carvalho et al., Dundee, United Kingdom. In J Exp Bot, 2006
Two of these golgin candidates (GC1 and GC2) possess C-terminal transmembrane (TM) domains with similarity to the TM domain of human golgin-84.
Golgin tethers define subpopulations of COPI vesicles.
Warren et al., New Haven, United States. In Science, 2005
characterization of the golgin-84-CASP tether binding to coat protein complex I (COPI) vesicles
Membrane traffic: a glitch in the Golgi matrix.
Barr et al., Martinsried, Germany. In Curr Biol, 2003
This model is brought into question by new evidence that two golgins, GM130 and golgin-84, contribute to but are not essential for protein transport and Golgi structure.
Golgin-84 is a rab1 binding partner involved in Golgi structure.
Warren et al., New Haven, United States. In Traffic, 2003
Golgin-84 (Golga5) involved in generating and maintaining the architecture of the Golgi apparatus.
Molecular genetics of childhood papillary thyroid carcinomas after irradiation: high prevalence of RET rearrangement.
Klugbauer et al., München, Germany. In Recent Results Cancer Res, 1997
Less frequently, RET/PTC1 (i.e., H4/RET rearrangements), and a novel type (RET/PTC5, i.e., RFG5/RET) were observed.
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