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TNF receptor-associated factor 3 interacting protein 1

MIP-T3, microtubule interacting protein that associates with TRAF3
Top mentioned proteins: MIP, DISC1, Actin, SET, ACID
Papers on MIP-T3
MIP-T3 is a negative regulator of innate type I IFN response.
Jin et al., Hong Kong, Hong Kong. In J Immunol, 2012
MIP-T3 functions as a negative regulator of the innate type I interferon response by preventing TRAF3 from forming protein complexes with critical downstream transducers and effectors of antiviral response.
Mutations in Traf3ip1 reveal defects in ciliogenesis, embryonic development, and altered cell size regulation.
Yoder et al., Birmingham, United States. In Dev Biol, 2012
Tumor necrosis factor alpha receptor 3 interacting protein 1 (Traf3ip1), also known as MIPT3, was initially characterized through its interactions with tubulin, actin, TNFR-associated factor-3 (Traf3), IL-13R1, and DISC1.
The C-terminus of MIP-T3 protein is required for ubiquitin-proteasome-mediated degradation in human cells.
Kitazato et al., Nagasaki, Japan. In Febs Lett, 2011
Data show that MIP-T3 protein level is highly regulated; mainly mediated by the ubiquitin-proteasome system.
Proteomic analysis reveals novel binding partners of MIP-T3 in human cells.
Kitazato et al., Nagasaki, Japan. In Proteomics, 2010
The interaction of MIP-T3 with both actin filaments and microtubule suggested that MIP-T3 may play an important role in regulation of cytoskeleton dynamics in cells.
Functional genomics of intraflagellar transport-associated proteins in C. elegans.
Leroux et al., Canada. In Methods Cell Biol, 2008
Many proteins were first described as participating in IFT in this organism, including IFTA-1 (IFT121), DYF-1 (fleer/IFT70), DYF-2 (IFT144), DYF-3 (Qilin), DYF-11 (MIP-T3/IFT54), DYF-13, XBX-1 (dynein light intermediate chain), XBX-2 (dynein light chain), CHE-13 (IFT57/HIPPI), orthologs of Bardet-Biedl syndrome proteins, and potential regulatory protein, IFTA-2 (RABL5/IFT22).
An essential role for DYF-11/MIP-T3 in assembling functional intraflagellar transport complexes.
Leroux et al., Canada. In Plos Genet, 2008
Analyses in different mutant backgrounds further suggest that DYF-11 functions as a novel component of IFT subcomplex B. Consistent with an evolutionarily conserved cilia-associated role, mammalian MIP-T3 localizes to basal bodies and cilia, and zebrafish mipt3 functions synergistically with the Bardet-Biedl syndrome protein Bbs4 to ensure proper gastrulation, a key cilium- and basal body-dependent developmental process.
Caenorhabditis elegans DYF-11, an orthologue of mammalian Traf3ip1/MIP-T3, is required for sensory cilia formation.
Iino et al., Tokyo, Japan. In Genes Cells, 2008
We further show that Traf3ip1/MIP-T3, the mammalian orthologue of DYF-11, localizes to cilia in the MDCK renal epithelial cells.
Association analysis of ATF4 and ATF5, genes for interacting-proteins of DISC1, in bipolar disorder.
Kato et al., Wako, Japan. In Neurosci Lett, 2007
As interacting-proteins with DISC1, Nudel, ATF4, ATF5, LIS1, alpha-tubulin, PDE4B, eIF3, FEZ1, Kendrin, MAP1A and MIPT3 were identified.
Piecing together a ciliome.
Leroux et al., Canada. In Trends Genet, 2006
We have compiled a cilia protein database that includes known cilia-associated proteins and numerous putative ciliary proteins including RAB-like small GTPases, which might be implicated in vesicular trafficking, and the microtubule-binding protein MIP-T3, some of which might be associated with ciliopathies.
Riboproteomics of the hepatitis C virus internal ribosomal entry site.
Anderson et al., San Francisco, United States. In J Proteome Res, 2004
These included five ribosomal subunits, nine eukaryotic initiation factor 3 subunits, and novel interacting proteins such as the cytoskeletal-related proteins actin, FHOS (formin homologue overexpressed in spleen) and MIP-T3 (microtubule interacting protein that associates with TRAF3).
MIP-T3 associates with IL-13Ralpha1 and suppresses STAT6 activation in response to IL-13 stimulation.
Kobayashi et al., Nagasaki, Japan. In Febs Lett, 2003
These results suggest that MIP-T3 is a novel inhibitor of IL-13 signaling and may be a useful molecule in ameliorating various conditions in which IL-13 plays a central role.
DISC1 (Disrupted-In-Schizophrenia 1) is a centrosome-associated protein that interacts with MAP1A, MIPT3, ATF4/5 and NUDEL: regulation and loss of interaction with mutation.
Austin et al., United States. In Hum Mol Genet, 2003
DISC1 interacts by yeast two-hybrid, mammalian two-hybrid, and co-immunoprecipitation assays with multiple proteins of the centrosome and cytoskeletal system, including MIPT3, MAP1A and NUDEL; proteins which localize receptors to membranes, including alpha-actinin2 and beta4-spectrin; and proteins which transduce signals from membrane receptors, including ATF4 and ATF5.
MIP-T3, a novel protein linking tumor necrosis factor receptor-associated factor 3 to the microtubule network.
Goeddel et al., San Francisco, United States. In J Biol Chem, 2000
In this study, we report the identification of a novel tumor necrosis factor receptor-associated factor 3 (TRAF3)-interacting protein designated MIP-T3.
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