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Trafficking protein, kinesin binding 2

Top mentioned proteins: Trak1, ACID, Rdl, KIF5C, Rhodopsin
Papers on GRIF-1
DISC1-dependent Regulation of Mitochondrial Dynamics Controls the Morphogenesis of Complex Neuronal Dendrites.
Kittler et al., London, United Kingdom. In J Biol Chem, Feb 2016
Here we have demonstrated that DISC1 couples to the mitochondrial transport and fusion machinery via interaction with the outer mitochondrial membrane GTPase proteins Miro1 and Miro2, the TRAK1 and TRAK2 mitochondrial trafficking adaptors, and the mitochondrial fusion proteins (mitofusins).
Localization of the kinesin adaptor proteins trafficking kinesin proteins 1 and 2 in primary cultures of hippocampal pyramidal and cortical neurons.
Stephenson et al., London, United Kingdom. In J Neurosci Res, Jul 2015
Previous work has established that trafficking kinesin proteins (TRAKs),TRAK1 and TRAK2, are kinesin adaptor proteins that link mitochondria to kinesin motor proteins via an acceptor protein in the mitochondrial outer membrane, etc. the Rho GTPase Miro.
Neuronal influences are necessary to produce mitochondrial co-localization with glutamate transporters in astrocytes.
Rattray et al., Reading, United Kingdom. In J Neurochem, 2014
We used primary cultures of mouse astrocytes to assess co-localization of GLT-1 with mitochondria, and tested whether the interaction was dependent on neurons, actin polymerization or the kinesin adaptor, TRAK2.
Revisiting the TRAK family of proteins as mediators of GABAA receptor trafficking.
Stephenson, London, United Kingdom. In Neurochem Res, 2014
Further work however, established that GRIF-1, now known as trafficking kinesin protein 2 (TRAK2), is a member of the TRAK family of kinesin adaptor proteins.
Evidence that dendritic mitochondria negatively regulate dendritic branching in pyramidal neurons in the neocortex.
Murakami et al., Suita, Japan. In J Neurosci, 2014
We altered the mitochondrial distribution in vivo by overexpressing Mfn1, a mitochondrial shaping protein, or the Miro-binding domain of TRAK2 (TRAK2-MBD), a truncated form of a motor-adaptor protein.
Transcriptome profiling and pathway analysis of genes expressed differentially in participants with or without a positive response to topiramate treatment for methamphetamine addiction.
Johnson et al., Charlottesville, United States. In Bmc Med Genomics, 2013
Many of these genes, such as GRINA, PRKACA, PRKCI, SNAP23, and TRAK2, which are involved in glutamate receptor and GABA receptor signaling, are direct targets for TPM.
Delineation of the TRAK binding regions of the kinesin-1 motor proteins.
Stephenson et al., London, United Kingdom. In Febs Lett, 2013
Three contributory regions forming the TRAK2 binding site within KIF5A and KIF5C cargo binding domains were delineated.
TRAK/Milton motor-adaptor proteins steer mitochondrial trafficking to axons and dendrites.
Hoogenraad et al., Utrecht, Netherlands. In Neuron, 2013
Here, we show that TRAK family adaptor proteins, TRAK1 and TRAK2, which link mitochondria to microtubule-based motors, are required for axonal and dendritic mitochondrial motility and utilize different transport machineries to steer mitochondria into axons and dendrites.
Genotypic variants at 2q33 and risk of esophageal squamous cell carcinoma in China: a meta-analysis of genome-wide association studies.
Wang et al., Bethesda, United States. In Hum Mol Genet, 2012
Our meta-analysis found genome-wide significant SNPs at 2q33 that map to the CASP8/ALS2CR12/TRAK2 gene region.
Amplification of thymosin beta 10 and AKAP13 genes in metastatic and aggressive papillary thyroid carcinomas.
Puskás et al., Szeged, Hungary. In Pathol Oncol Res, 2012
The CGH-array and confirmatory quantitative real-time PCR results identified the deletion of the EIF4EBP3 and TRAK2 gene loci, while amplification of thymosin beta 10 (TB10) and Tre-2 oncogene regions were observed as general markers for PTC.
Trafficking kinesin protein (TRAK)-mediated transport of mitochondria in axons of hippocampal neurons.
Stephenson et al., London, United Kingdom. In J Biol Chem, 2011
In this study, we used gene silencing by targeted shRNAi and dominant negative approaches in conjunction with live imaging to investigate the contribution of endogenous TRAKs, TRAK1 and TRAK2, to the transport of mitochondria in axons of hippocampal pyramidal neurons.
N-acetylglucosamine transferase is an integral component of a kinesin-directed mitochondrial trafficking complex.
Stephenson et al., London, United Kingdom. In Biochim Biophys Acta, 2011
TRAK2 was a substrate for N-acetylglucosamine transferase with TRAK2 (S562) identified as a site of O-N-acetylglucosamine modification.
GTPase dependent recruitment of Grif-1 by Miro1 regulates mitochondrial trafficking in hippocampal neurons.
Kittler et al., London, United Kingdom. In Mol Cell Neurosci, 2009
These data suggest that Miro1 and the kinesin adaptor Grif-1 play an important role in regulating mitochondrial transport in neurons.
GABAA receptor associated proteins: a key factor regulating GABAA receptor function.
Olsen et al., Los Angeles, United States. In J Neurochem, 2007
Recently, several labs have used the yeast two-hybrid assay to identify proteins interacting with GABA(A) receptors, for example, the interaction of GABA(A) receptor associated protein (GABARAP) and Golgi-specific DHHC zinc finger protein (GODZ) with gamma subunits, PRIP, phospholipase C-related, catalytically inactive proteins (PRIP-1) and (PRIP-2) with GABARAP and receptor gamma2 and beta subunits, Plic-1 with some alpha and beta subunits, radixin with the alpha5 subunit, HAP1 with the beta1 subunit, GABA(A) receptor interacting factor-1 (GRIF-1) with the beta2 subunit, and brefeldin A-inhibited GDP/GTP exchange factor 2 (BIG2) with the beta3 subunit.
GRIF1 binds Hrs and is a new regulator of endosomal trafficking.
Li et al., Atlanta, United States. In J Cell Sci, 2006
GRIF1 may participate in microtubule-based transport of early endosomes by acting as an adaptor linking Hrs-containing endosomes to kinesin.
Identification of gamma-aminobutyric acid receptor-interacting factor 1 (TRAK2) as a trafficking factor for the K+ channel Kir2.1.
Zaks-Makhina et al., Pittsburgh, United States. In J Biol Chem, 2006
Binds to Kir2.1 and facilitates trafficking of this channel to the cell surface.
Mapping the GRIF-1 binding domain of the kinesin, KIF5C, substantiates a role for GRIF-1 as an adaptor protein in the anterograde trafficking of cargoes.
Stephenson et al., London, United Kingdom. In J Biol Chem, 2006
analysis of the GRIF-1 binding domain of the kinesin, KIF5C, which substantiates a role for GRIF-1 as an adaptor protein in the anterograde trafficking of cargoes
GRIF-1 and OIP106, members of a novel gene family of coiled-coil domain proteins: association in vivo and in vitro with kinesin.
Stephenson et al., London, United Kingdom. In J Biol Chem, 2005
GRIF-1 and OIP106 have roles in protein and/or organelle transport in excitable cells in a manner analogous to glutamate receptor-interacting-protein 1
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