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Sorting nexin 15

SNX15, sorting nexin 15
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. Overexpression of this gene results in a decrease in the processing of insulin and hepatocyte growth factor receptors to their mature subunits. This decrease is caused by the mislocalization of furin, the endoprotease responsible for cleavage of insulin and hepatocyte growth factor receptors. This protein is involved in endosomal trafficking from the plasma membrane to recycling endosomes or the trans-Golgi network. Alternative splicing results in multiple transcript variants. Read-through transcription also exists between this gene and the upstream ADP-ribosylation factor-like 2 (ARL2) gene. [provided by RefSeq, Dec 2010] (from NCBI)
Top mentioned proteins: spastin, CAN, Vps4, ACID, SNX3
Papers on SNX15
SNX15 Regulates Cell Surface Recycling of APP and Aβ Generation.
Zhang et al., Xiamen, China. In Mol Neurobiol, Jul 2015
Sorting nexin 15 (SNX15) is known to regulate protein trafficking.
ESCRT-0 marks an APPL1-independent transit route for EGFR between the cell surface and the EEA1-positive early endosome.
Woodman et al., Westmead, Australia. In J Cell Sci, Mar 2015
The peripheral Hrs-labelled endosomes are distinct from APPL1-containing endosomes, but co-label with the novel endocytic adaptor SNX15.
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.
MIT domain of Vps4 is a Ca2+-dependent phosphoinositide-binding domain.
Hiroaki et al., Nagoya, Japan. In J Biochem, 2013
The microtubule interacting and trafficking (MIT) domain is a small protein module that is conserved in proteins of diverged function, such as Vps4, spastin and sorting nexin 15 (SNX15).
Transcriptomic signature of cell lines isolated from canine mammary adenocarcinoma metastases to lungs.
Motyl et al., Warsaw, Poland. In J Appl Genet, 2009
These differently expressed genes are involved mainly in signal transduction, cell structure and motility, nucleic acid metabolism, developmental processing, and apoptosis (GHSR, RASSF1, ARF1GAP, WDR74, SMOC2, SFRP4, DIAPH1, FSCN1, ALX4, SNX15, PLD2, WNT7B, POU6F2, NKG7, and POLR2F).
Structural characterization of the MIT domain from human Vps4b.
Hiroaki et al., Yokohama, Japan. In Biochem Biophys Res Commun, 2005
The microtubule interacting and trafficking (MIT) domain is a small protein module of unknown function that is conserved in proteins of diverse function, such as Vps4, sorting nexin 15 (SNX15), and spastin.
A clinical, genetic and candidate gene study of Silver syndrome, a complicated form of hereditary spastic paraplegia.
Crosby et al., London, United Kingdom. In J Neurol, 2004
Mutation analysis of genes encoding calpain 1 ( CAPN1), copper chaperone for superoxide dismutase ( CCS), ADP ribosylation factor-like 2 ( ARL2), LOC120664, a putative homologue of atlastin ( ATLSTL-1) and sorting nexin 15 ( SNX15) failed to identify any disease-specific mutations.
The identification of a conserved domain in both spartin and spastin, mutated in hereditary spastic paraplegia.
Crosby et al., Heidelberg, Germany. In Genomics, 2003
The domain, which corresponds to a slightly extended version of the recently described ESP domain of unknown function, was also identified in VPS4, SKD1, RPK118, and SNX15, all of which have a well established and consistent role in endosomal trafficking.
Identification and characterization of SNX15, a novel sorting nexin involved in protein trafficking.
Haft et al., Bethesda, United States. In J Biol Chem, 2001
We have identified a novel 342-amino acid residue sorting nexin, SNX15, and a 252-amino acid splice variant, SNX15A.
Overexpression of a novel sorting nexin, SNX15, affects endosome morphology and protein trafficking.
Haft et al., Bethesda, United States. In Traffic, 2000
Overexpression of myc-tagged SNX15 in COS-7 cells altered the morphology of several endosomal compartments.
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