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Sorting nexin 5

SNX5, sorting nexin 5
This gene encodes a member of the sorting nexin family. Members of this family contain a phox (PX) domain, which is a phosphoinositide binding domain, and are involved in intracellular trafficking. This protein binds to fanconi anemia complementation group A protein, but its function is unknown. This gene results in two transcript variants encoding the same protein. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: SNX1, SNX6, Epidermal Growth Factor, beta 2-adrenoceptor, SNX2
Papers using SNX5 antibodies
Cellular senescence in human myoblasts is overcome by human telomerase reverse transcriptase and cyclin-dependent kinase 4: consequences in aging muscle and therapeutic strategies for muscular dystrophies
Brodsky Frances M. et al., In The Journal of Cell Biology, 2006
... Signaling Technology); GM130 (rabbit polyclonal, Sigma-Aldrich); CI-MPR (mouse monoclonal, EMD); Cathepsin D (rabbit polyclonal; EMD); and SNX5 (goat polyclonal; Abcam).
Papers on SNX5
Sorting nexin 5 selectively regulates dorsal-ruffle-mediated macropinocytosis in primary macrophages.
Gleeson et al., Melbourne, Australia. In J Cell Sci, Jan 2016
We previously identified sorting nexin 5 (SNX5) as a regulator of macropinocytosis in macrophages.
Retromer: Structure, function, and roles in mammalian disease.
Kim et al., Springfield, United States. In Eur J Cell Biol, Nov 2015
These five proteins (Vps5, Vps17, Vps26, Vps29, and Vps35 in yeast and SNX1/2, SNX5/6, Vps26, Vps29, and Vps35 in mammalian cells) act as a coat for vesicles budding off of the endosome, as well as perform cargo sorting at the endosome.
Global Mapping of the Inc-Human Interactome Reveals that Retromer Restricts Chlamydia Infection.
Engel et al., San Francisco, United States. In Cell Host Microbe, Aug 2015
IncE binds to sorting nexins (SNXs) 5/6, components of the retromer, which relocalizes SNX5/6 to the inclusion membrane and augments inclusion membrane tubulation.
The Proteome of the Isolated Chlamydia trachomatis Containing Vacuole Reveals a Complex Trafficking Platform Enriched for Retromer Components.
Heuer et al., Berlin, Germany. In Plos Pathog, Jun 2015
Functional studies showed that in particular, SNX5 controls the C. trachomatis infection and that retrograde trafficking is essential for infectious progeny formation.
Sorting nexin 5 and dopamine d1 receptor regulate the expression of the insulin receptor in human renal proximal tubule cells.
Jose et al., Chongqing, China. In Endocrinology, Jun 2015
Sorting nexin 5 (SNX5) belongs to the SNX family, which is composed of a diverse group of proteins that mediate trafficking of plasma membrane proteins, receptors, and transporters.
miR-216a regulates snx5, a novel notch signaling pathway component, during zebrafish retinal development.
Patton et al., United States. In Dev Biol, May 2015
Sorting Nexin 5 (SNX5) co-localizes with Mib and Delta complexes and has been shown to directly bind to Mib.
LAPTM4B is a PtdIns(4,5)P2 effector that regulates EGFR signaling, lysosomal sorting, and degradation.
Anderson et al., Madison, United States. In Embo J, Mar 2015
This is counteracted by the endosomal PIP kinase, PIPKIγi5, which directly binds LAPTM4B and neutralizes the inhibitory function of LAPTM4B in EGFR sorting by generating PtdIns(4,5)P2 and recruiting SNX5.
Rapid mapping of interactions between Human SNX-BAR proteins measured in vitro by AlphaScreen and single-molecule spectroscopy.
Gambin et al., Australia. In Mol Cell Proteomics, 2014
We find that while nine SNX-BAR proteins are able to form homo-dimers, several including the retromer-associated SNX1, SNX2, and SNX5 require heteromeric interactions for dimerization.
Isoform 5 of PIPKIγ regulates the endosomal trafficking and degradation of E-cadherin.
Anderson et al., Madison, United States. In J Cell Sci, 2014
Additionally, we show that the endosomal trafficking proteins SNX5 and SNX6 associate with PIPKIγi5 and inhibit PIPKIγi5-mediated E-cadherin degradation.
Tick-borne encephalitis virus replication, intracellular trafficking, and pathogenicity in human intestinal Caco-2 cell monolayers.
Bücker et al., Berlin, Germany. In Plos One, 2013
Immunofluorescence microscopy revealed co-localization of TBEV with early endosome antigen-1 (EEA1) as well as with sorting nexin-5 (SNX5), pointing to macropinocytosis as trafficking mechanism.
SNX15 links clathrin endocytosis to the PtdIns3P early endosome independently of the APPL1 endosome.
Cullen et al., Bristol, United Kingdom. In J Cell Sci, 2013
In designing an RNAi-mediated loss-of-function screen, we establish that of 30 human SNXs only SNX3, SNX5, SNX9, SNX15 and SNX21 appear to regulate EGF receptor degradative sorting.
Endosomal type Iγ PIP 5-kinase controls EGF receptor lysosomal sorting.
Anderson et al., Madison, United States. In Dev Cell, 2013
In this pathway, PIPKIγi5 interacts with sorting nexin 5 (SNX5), a protein that binds PtdIns4,5P(2) and other phosphoinositides.
Disruption of sorting nexin 5 causes respiratory failure associated with undifferentiated alveolar epithelial type I cells in mice.
Kong et al., Seoul, South Korea. In Plos One, 2012
Sorting nexin 5 (Snx5) has been posited to regulate the degradation of epidermal growth factor receptor and the retrograde trafficking of cation-independent mannose 6-phosphate receptor/insulin-like growth factor II receptor.
A SNX3-dependent retromer pathway mediates retrograde transport of the Wnt sorting receptor Wntless and is required for Wnt secretion.
Korswagen et al., Utrecht, Netherlands. In Nat Cell Biol, 2011
Here, we report that Wls recycling is mediated through a retromer pathway that is independent of the retromer sorting nexins SNX1-SNX2 and SNX5-SNX6.
The DHR1 domain of DOCK180 binds to SNX5 and regulates cation-independent mannose 6-phosphate receptor transport.
Matsuda et al., Kyoto, Japan. In Mol Biol Cell, 2008
DOCK180 regulates CI-MPR trafficking via SNX5 and this function is independent of its guanine nucleotide exchange factor activity toward Rac1
Hurley et al., Bethesda, United States. In Curr Opin Cell Biol, 2008
The mammalian retromer complex comprises a sorting nexin dimer composed of a still undefined combination of SNX1, SNX2, SNX5 and SNX6, and a cargo-recognition trimer composed of Vps26, Vps29 and Vps35.
A role for SNX5 in the regulation of macropinocytosis.
Gleeson et al., Melbourne, Australia. In Bmc Cell Biol, 2007
SNX5 requires the generation of phosphoinositides for recruitment to the plasma membrane and, moreover, influences the level of macropinocytic activity
A loss-of-function screen reveals SNX5 and SNX6 as potential components of the mammalian retromer.
Cullen et al., Bristol, United Kingdom. In J Cell Sci, 2007
SNX5 and SNX6 may constitute functional equivalents of Vps17p in mammalian retromer
Snx5, as a Mind bomb-binding protein, is expressed in hematopoietic and endothelial precursor cells in zebrafish.
Kim et al., Taejŏn, South Korea. In Febs Lett, 2006
Snx5, a novel interacting partner of Mind bomb, may have an essential role for cell fate determination in early development.
Sorting nexin 5 is localized to a subdomain of the early endosomes and is recruited to the plasma membrane following EGF stimulation.
Gleeson et al., Melbourne, Australia. In J Cell Sci, 2005
SNX5 is localized to a subdomain of the early endosomes and is recruited to the cell membrane following EGF stimulation.
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