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SORT1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3F6K, 3G2U, 3G2V, 4MSL, 4N7E, 4PO7
Identifiers
Aliases	SORT1, Gp95, LDLCQ6, NT3, NTR3, Sortilin 1
External IDs	OMIM: 602458; MGI: 1338015; HomoloGene: 136097; GeneCards: SORT1; OMA:SORT1 - orthologs
Gene location (Human) Chr. Chromosome 1 (human) Band 1p13.3|1p21.3-p13.1 Start 109,309,568 bp End 109,397,918 bp
Gene location (Mouse) Chr. Chromosome 3 (mouse) Band 3|3 F3 Start 108,191,398 bp End 108,268,827 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in inferior ganglion of vagus nerve corpus epididymis subthalamic nucleus postcentral gyrus globus pallidus external globus pallidus internal globus pallidus pars reticulata corpus callosum superior vestibular nucleus Top expressed in dentate gyrus of hippocampal formation granule cell superior frontal gyrus primary visual cortex ascending aorta granulocyte muscle of thigh lumbar subsegment of spinal cord aortic valve spermatid neural layer of retina More reference expression data BioGPS More reference expression data
Gene ontology Molecular function nerve growth factor receptor activity neurotensin receptor activity, non-G protein-coupled nerve growth factor binding protein binding enzyme binding Cellular component integral component of membrane endosome Golgi apparatus nuclear membrane endoplasmic reticulum membrane membrane intracellular membrane-bounded organelle plasma membrane Golgi cisterna membrane cell surface lysosomal membrane soma dendrite early endosome endoplasmic reticulum perinuclear region of cytoplasm clathrin-coated pit trans-Golgi network transport vesicle lysosome endosome membrane clathrin-coated vesicle nucleus cytosol cytoplasmic vesicle membrane cytoplasmic vesicle Biological process G protein-coupled receptor signaling pathway cell differentiation myotube differentiation negative regulation of fat cell differentiation endocytosis neurotrophin TRK receptor signaling pathway ossification endosome transport via multivesicular body sorting pathway vesicle organization endosome to lysosome transport Golgi to endosome transport positive regulation of epithelial cell apoptotic process multicellular organism development response to insulin plasma membrane to endosome transport regulation of gene expression negative regulation of lipoprotein lipase activity glucose import neuropeptide signaling pathway extrinsic apoptotic signaling pathway via death domain receptors nerve growth factor signaling pathway post-Golgi vesicle-mediated transport Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 6272 20661 Ensembl ENSG00000134243 ENSMUSG00000068747 UniProt Q99523 Q6PHU5 RefSeq (mRNA) NM_001205228 NM_002959 NM_001271599 NM_019972 RefSeq (protein) NP_001192157 NP_002950 NP_001258528 NP_064356 Location (UCSC) Chr 1: 109.31 – 109.4 Mb Chr 3: 108.19 – 108.27 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Sortilin (SORT1) is a protein that in humans is encoded by the SORT1 gene on chromosome 1. This protein is a type I membrane glycoprotein in the vacuolar protein sorting 10 protein (Vps10p) family of sorting receptors. While it is ubiquitously expressed in many tissues, sortilin is most abundant in the central nervous system. At the cellular level, sortilin functions in protein transport between the Golgi apparatus, endosome, lysosome, and plasma membrane, leading to its involvement in multiple biological processes such as glucose and lipid metabolism as well as neural development and cell death. Moreover, the function and role of sortilin is now emerging in several major human diseases such as hypertension, atherosclerosis, coronary artery disease, Alzheimer’s disease, and cancer. The SORT1 gene also contains one of 27 loci associated with increased risk of coronary artery disease.

Structure

Gene

The SORT1 gene resides on chromosome 1 at the band 1p13.3 and includes 23 exons. This gene encodes 2 isoforms through alternative splicing.

Protein

Sortilin is a member of the Vps10p sorting receptor family. Crystallization studies of the protein reveal that, when complexed with the ligand neurotensin, the Vps10 ectodomain of sortilin forms a ten-bladed beta-propeller structure with an inner tunnel that contains multiple ligand binding sites. To prevent premature ligand binding during its synthesis, the precursor protein of sortilin contains a 44-amino acid pro-peptide that serves as a chaperone for the Vps10p domain. In addition, two hydrophobic loops have been detected in this domain and act to anchor the protein in the cell membrane. Sortilin has also been shown to undergo a conformational change and form a protein dimer in acidic conditions similar to ones found in the endosome, indicating a double mechanism for low pH-induced ligand release and possibly signaling towards recycling of the receptor.

Function

In humans, sortilin is expressed over a wide range of cell types and tissues such as the brain, spinal cord, adrenal gland, thyroid, B-lymphocytes, adipocytes, skeletal muscle, and heart. As a sorting receptor on the cell surface and on the endoplasmic reticulum-Golgi apparatus within the cell, sortilin is involved in the transport of a wide variety of intracellular proteins between the trans-Golgi network, endosome, lysosome, and secretory granules, as well as the plasma membrane. This molecular function enables sortilin to participate in various biological processes, including the transport of GLUT4 to the plasma membrane of fat and skeletal muscle cells in response to insulin. It also mediates the interaction between proNGF and the p75NTR:sortilin complex by acting as a co-receptor to signal cell death. The fine regulation of the brain-derived neurotrophic factor (BDNF) by sortilin is required for both neuronal and tumor cell survival. Moreover, sortilin has been implicated in LDL-cholesterol metabolism, VLDL secretion, and PCSK9 secretion, and thus plays a role in the development of atherosclerotic lesions. It modulates lipid metabolism in adipocytes, hepatocytes, and macrophages. Other processes involving sortilin include endocytosis, negative regulation of lipoprotein lipase activity, myotube differentiation, ossification, and regulation of gene expression.

Clinical significance

Given its function in facilitating lysosomal degradation or recycling of ligands in lipid metabolism and the neural system, sortilin likely plays an important role in the underlying mechanisms and pathophysiology of atherogenesis and coronary artery disease, as well as in neurological disorders. For example, sortilin has been identified as an important receptor for brain apolipoprotein E (APOE) metabolism, which is implicated in the underlying mechanisms of Alzheimer’s disease. A significant role for sortilin has recently also been reported in the field of oncology, as it has been detected in several cancer cell lines. Notably, human cancerous epithelial cells exhibited increased levels of sortilin as compared to normal epithelial tissues. Furthermore, it appears that sortilin participates in the progression of breast cancer and contributes to tumor cell adhesion and invasion.

Clinical marker

In 2007, chromosome 1p13.3 was identified as a promising locus through a genome-wide approach in patients with coronary artery disease. Subsequently, accumulating evidence suggests that the SORT1 gene at the 1p13 locus is an important risk factor for coronary artery disease, which is attributed to lipid metabolism disorders. Several single nucleotide polymorphisms of the SORT1 gene have a genetic association between serum blood lipid levels and the pathogenesis of cardiometabolic syndrome, including obesity, hypertension, and coronary artery disease. As the role of sortilin in lipid metabolism and the development of atherosclerosis has been established, a recent study further reported that increased release of soluble sortilin from platelets, measured as circulating sortilin, may be associated with in vivo platelet activation. This observation also indicates that sortilin has a potential application as a clinical biomarker for diagnosis and prognosis. Additionally, a multi-locus genetic risk score study, based on a combination of 27 loci including the SORT1 gene, identified individuals at increased risk for both incident and recurrent coronary artery disease events, as well as an enhanced clinical benefit from statin therapy. The study was based on a community cohort study (the Malmo Diet and Cancer study) and four additional randomized controlled trials of primary prevention cohorts (JUPITER and ASCOT) and secondary prevention cohorts (CARE and PROVE IT-TIMI 22).

Interactions

Sortilin has been shown to interact with GGA1 and GGA2.

Interactive Pathway Map

Sortilin participates in interactions within the trans-Golgi network vesicle budding and BDNF signaling pathways.

See also

• Neurotensin receptor

References

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20. ^ Nykjaer A, Willnow TE (April 2012). "Sortilin: a receptor to regulate neuronal viability and function". Trends in Neurosciences. 35 (4): 261–270. doi:10.1016/j.tins.2012.01.003. PMID 22341525. S2CID 28152980.
21. Quistgaard EM, Grøftehauge MK, Madsen P, Pallesen LT, Christensen B, Sørensen ES, et al. (September 2014). "Revisiting the structure of the Vps10 domain of human sortilin and its interaction with neurotensin". Protein Science. 23 (9): 1291–1300. doi:10.1002/pro.2512. PMC 4243999. PMID 24985322.
22. Leloup N, Lössl P, Meijer DH, Brennich M, Heck AJ, Thies-Weesie DM, Janssen BJ (November 2017). "Low pH-induced conformational change and dimerization of sortilin triggers endocytosed ligand release". Nature Communications. 8 (1): 1708. Bibcode:2017NatCo...8.1708L. doi:10.1038/s41467-017-01485-5. PMC 5700061. PMID 29167428.
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26. Nielsen MS, Jacobsen C, Olivecrona G, Gliemann J, Petersen CM (March 1999). "Sortilin/neurotensin receptor-3 binds and mediates degradation of lipoprotein lipase". The Journal of Biological Chemistry. 274 (13): 8832–8836. doi:10.1074/jbc.274.13.8832. PMID 10085125.
27. ^ Ariga M, Nedachi T, Katagiri H, Kanzaki M (April 2008). "Functional role of sortilin in myogenesis and development of insulin-responsive glucose transport system in C2C12 myocytes". The Journal of Biological Chemistry. 283 (15): 10208–10220. doi:10.1074/jbc.M710604200. PMID 18258592.
28. Maeda S, Nobukuni T, Shimo-Onoda K, Hayashi K, Yone K, Komiya S, Inoue I (October 2002). "Sortilin is upregulated during osteoblastic differentiation of mesenchymal stem cells and promotes extracellular matrix mineralization". Journal of Cellular Physiology. 193 (1): 73–79. doi:10.1002/jcp.10151. PMID 12209882. S2CID 32754981.
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Further reading

• Vincent JP, Mazella J, Kitabgi P (July 1999). "Neurotensin and neurotensin receptors". Trends in Pharmacological Sciences. 20 (7): 302–309. doi:10.1016/S0165-6147(99)01357-7. PMID 10390649.
• Mazella J (January 2001). "Sortilin/neurotensin receptor-3: a new tool to investigate neurotensin signaling and cellular trafficking?". Cellular Signalling. 13 (1): 1–6. doi:10.1016/S0898-6568(00)00130-3. PMID 11257441.
• Petersen CM, Nielsen MS, Nykjaer A, Jacobsen L, Tommerup N, Rasmussen HH, et al. (February 1997). "Molecular identification of a novel candidate sorting receptor purified from human brain by receptor-associated protein affinity chromatography". The Journal of Biological Chemistry. 272 (6): 3599–3605. doi:10.1074/jbc.272.6.3599. PMID 9013611.
• Lin BZ, Pilch PF, Kandror KV (September 1997). "Sortilin is a major protein component of Glut4-containing vesicles". The Journal of Biological Chemistry. 272 (39): 24145–24147. doi:10.1074/jbc.272.39.24145. PMID 9305862.
• Tauris J, Ellgaard L, Jacobsen C, Nielsen MS, Madsen P, Thøgersen HC, et al. (June 1998). "The carboxy-terminal domain of the receptor-associated protein binds to the Vps10p domain of sortilin". FEBS Letters. 429 (1): 27–30. doi:10.1016/S0014-5793(98)00559-6. PMID 9657377.
• Mazella J, Zsürger N, Navarro V, Chabry J, Kaghad M, Caput D, et al. (October 1998). "The 100-kDa neurotensin receptor is gp95/sortilin, a non-G-protein-coupled receptor". The Journal of Biological Chemistry. 273 (41): 26273–26276. doi:10.1074/jbc.273.41.26273. PMID 9756851.
• Munck Petersen C, Nielsen MS, Jacobsen C, Tauris J, Jacobsen L, Gliemann J, et al. (February 1999). "Propeptide cleavage conditions sortilin/neurotensin receptor-3 for ligand binding". The EMBO Journal. 18 (3): 595–604. doi:10.1093/emboj/18.3.595. PMC 1171152. PMID 9927419.
• Nielsen MS, Jacobsen C, Olivecrona G, Gliemann J, Petersen CM (March 1999). "Sortilin/neurotensin receptor-3 binds and mediates degradation of lipoprotein lipase". The Journal of Biological Chemistry. 274 (13): 8832–8836. doi:10.1074/jbc.274.13.8832. PMID 10085125.
• Nielsen MS, Madsen P, Christensen EI, Nykjaer A, Gliemann J, Kasper D, et al. (May 2001). "The sortilin cytoplasmic tail conveys Golgi-endosome transport and binds the VHS domain of the GGA2 sorting protein". The EMBO Journal. 20 (9): 2180–2190. doi:10.1093/emboj/20.9.2180. PMC 125444. PMID 11331584.
• Takatsu H, Katoh Y, Shiba Y, Nakayama K (July 2001). "Golgi-localizing, gamma-adaptin ear homology domain, ADP-ribosylation factor-binding (GGA) proteins interact with acidic dileucine sequences within the cytoplasmic domains of sorting receptors through their Vps27p/Hrs/STAM (VHS) domains". The Journal of Biological Chemistry. 276 (30): 28541–28545. doi:10.1074/jbc.C100218200. PMID 11390366.
• Hampe W, Rezgaoui M, Hermans-Borgmeyer I, Schaller HC (June 2001). "The genes for the human VPS10 domain-containing receptors are large and contain many small exons". Human Genetics. 108 (6): 529–536. doi:10.1007/s004390100504. PMID 11499680. S2CID 23375354.
• Shiba T, Takatsu H, Nogi T, Matsugaki N, Kawasaki M, Igarashi N, et al. (February 2002). "Structural basis for recognition of acidic-cluster dileucine sequence by GGA1". Nature. 415 (6874): 937–941. Bibcode:2002Natur.415..937S. doi:10.1038/415937a. PMID 11859376. S2CID 4395774.
• Maeda S, Nobukuni T, Shimo-Onoda K, Hayashi K, Yone K, Komiya S, Inoue I (October 2002). "Sortilin is upregulated during osteoblastic differentiation of mesenchymal stem cells and promotes extracellular matrix mineralization". Journal of Cellular Physiology. 193 (1): 73–79. doi:10.1002/jcp.10151. PMID 12209882. S2CID 32754981.
• Martin S, Navarro V, Vincent JP, Mazella J (October 2002). "Neurotensin receptor-1 and -3 complex modulates the cellular signaling of neurotensin in the HT29 cell line". Gastroenterology. 123 (4): 1135–1143. doi:10.1053/gast.2002.36000. PMID 12360476.
• Navarro V, Vincent JP, Mazella J (November 2002). "Shedding of the luminal domain of the neurotensin receptor-3/sortilin in the HT29 cell line". Biochemical and Biophysical Research Communications. 298 (5): 760–764. doi:10.1016/S0006-291X(02)02564-0. PMID 12419319.
• Martin S, Vincent JP, Mazella J (February 2003). "Involvement of the neurotensin receptor-3 in the neurotensin-induced migration of human microglia". The Journal of Neuroscience. 23 (4): 1198–1205. doi:10.1523/JNEUROSCI.23-04-01198.2003. PMC 6742286. PMID 12598608.
• Lefrancois S, Zeng J, Hassan AJ, Canuel M, Morales CR (December 2003). "The lysosomal trafficking of sphingolipid activator proteins (SAPs) is mediated by sortilin". The EMBO Journal. 22 (24): 6430–6437. doi:10.1093/emboj/cdg629. PMC 291824. PMID 14657016.

External links

• Overview of all the structural information available in the PDB for UniProt: Q99523 (Sortilin) at the PDBe-KB.

• Genes on human chromosome 1