Sortilin 1
(Preusmjereno sa stranice Gp95)
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Sortilin je protein koji je kod ljudi kodiran SORT1 genom.[1] SORT1 locus pokazuje najjaču vezu sa lipoproteinima seruma.[2] U hepatocitima, sortilin učestvuje u presekretornog degradaciji formirajućih VLDL čestica.[3]
| Sortilin 1 | |||||||||||
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| Identifikatori | |||||||||||
| Simboli | SORT1; NT3; Gp95 | ||||||||||
| Vanjski ID | OMIM: 602458 MGI: 1338015 HomoloGene: 39282 GeneCards: SORT1 Gene | ||||||||||
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| Pregled RNK izražavanja | |||||||||||
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| Ortolozi | |||||||||||
| Vrsta | Čovek | Miš | |||||||||
| Entrez | 6272 | 20661 | |||||||||
| Ensembl | ENSG00000134243 | ENSMUSG00000068747 | |||||||||
| UniProt | Q99523 | Q6PHU5 | |||||||||
| RefSeq (mRNA) | NM_002959 | NM_019972 | |||||||||
| RefSeq (protein) | NP_002950 | NP_064356 | |||||||||
| Lokacija (UCSC) | Chr 1: 109.65 - 109.74 Mb | Chr 3: 108.41 - 108.49 Mb | |||||||||
| PubMed pretraga | [1] | [2] | |||||||||
Ovaj protein je multi-ligandni tip-1 receptora, koji je sličan karboksipeptidaznom Y sortirajućim receptoru kvasca (Vps10 proteinu). To je transmembranski protein trans-Goldžijeve mreže (TGN), koji vezuje brojne nevezane ligande koji učestvuju u širokom nizu ćelijskih procesa; međutim, njemu nedostaju tipične osobine signalnog receptora. U TGN furin posreduje aktivaciju formirane vezujuće forme proteina. Protein se sastoji od velikog luminalnog domena, transmembranskog segmenta i kratkog C-terminalnog citoplazmatičnog repa. Luminalni domen se sastoji od cisteinom-bogatog regiona sličnog sa dva corespondirajuća segmenta u kvaščevom Vps10p. Citoplazmatični rep je sličan sa odgovarajućim segmentom katjon-nezavisnog manoza 6-fosfatnog receptora, i rep takođe interaguje sa VHS domenima GGA (Goldži-vezanim, gama-adaptin homolognim, ARF-interagujućim) proteinima.[1]
U melanocitnim ćelijama izražavanje SORT1 gena može da bude regulisano putem MITF.[4]
Interakcije uredi
Za sortilin 1 je bilo pokazano da interaguje sa GGA1[5] i GGA2.[5][6]
Vidi još uredi
Reference uredi
- ↑ 1,0 1,1 „Entrez Gene: SORT1 sortilin 1”.
- ↑ Teslovich TM, Musunuru K, Smith AV, et al. (August 2010). „Biological, clinical and population relevance of 95 loci for blood lipids”. Nature 466 (7307): 707–13. DOI:10.1038/nature09270. PMID 20686565.
- ↑ Musunuru K, Strong A, Frank-Kamenetsky M, et al. (August 2010). „From noncoding variant to phenotype via SORT1 at the 1p13 cholesterol locus”. Nature 466 (7307): 714–9. DOI:10.1038/nature09266. PMID 20686566.
- ↑ Hoek KS, Schlegel NC, Eichhoff OM, et al. (2008). „Novel MITF targets identified using a two-step DNA microarray strategy”. Pigment Cell Melanoma Res. 21 (6): 665–76. DOI:10.1111/j.1755-148X.2008.00505.x. PMID 19067971.
- ↑ 5,0 5,1 Jacobsen, Linda; Madsen Peder, Nielsen Morten S, Geraerts Wijnand P M, Gliemann Jørgen, Smit August B, Petersen Claus M (January 2002). „The sorLA cytoplasmic domain interacts with GGA1 and -2 and defines minimum requirements for GGA binding”. FEBS Lett. (Netherlands) 511 (1-3): 155–8. DOI:10.1016/S0014-5793(01)03299-9. ISSN 0014-5793. PMID 11821067.
- ↑ Nielsen, M S; Madsen P, Christensen E I, Nykjaer A, Gliemann J, Kasper D, Pohlmann R, Petersen C M (May 2001). „The sortilin cytoplasmic tail conveys Golgi-endosome transport and binds the VHS domain of the GGA2 sorting protein”. EMBO J. (England) 20 (9): 2180–90. DOI:10.1093/emboj/20.9.2180. ISSN 0261-4189. PMC 125444. PMID 11331584.
Literatura uredi
- Vincent JP, Mazella J, Kitabgi P (1999). „Neurotensin and neurotensin receptors.”. Trends Pharmacol. Sci. 20 (7): 302–9. DOI:10.1016/S0165-6147(99)01357-7. PMID 10390649.
- Mazella J (2001). „Sortilin/neurotensin receptor-3: a new tool to investigate neurotensin signaling and cellular trafficking?”. Cell. Signal. 13 (1): 1–6. DOI:10.1016/S0898-6568(00)00130-3. PMID 11257441.
- Petersen CM, Nielsen MS, Nykjaer A, et al. (1997). „Molecular identification of a novel candidate sorting receptor purified from human brain by receptor-associated protein affinity chromatography.”. J. Biol. Chem. 272 (6): 3599–605. DOI:10.1074/jbc.272.6.3599. PMID 9013611.
- Lin BZ, Pilch PF, Kandror KV (1997). „Sortilin is a major protein component of Glut4-containing vesicles.”. J. Biol. Chem. 272 (39): 24145–7. DOI:10.1074/jbc.272.39.24145. PMID 9305862.
- Tauris J, Ellgaard L, Jacobsen C, et al. (1998). „The carboxy-terminal domain of the receptor-associated protein binds to the Vps10p domain of sortilin.”. FEBS Lett. 429 (1): 27–30. DOI:10.1016/S0014-5793(98)00559-6. PMID 9657377.
- Mazella J, Zsürger N, Navarro V, et al. (1998). „The 100-kDa neurotensin receptor is gp95/sortilin, a non-G-protein-coupled receptor.”. J. Biol. Chem. 273 (41): 26273–6. DOI:10.1074/jbc.273.41.26273. PMID 9756851.
- Munck Petersen C, Nielsen MS, Jacobsen C, et al. (1999). „Propeptide cleavage conditions sortilin/neurotensin receptor-3 for ligand binding.”. EMBO J. 18 (3): 595–604. DOI:10.1093/emboj/18.3.595. PMC 1171152. PMID 9927419.
- Nielsen MS, Jacobsen C, Olivecrona G, et al. (1999). „Sortilin/neurotensin receptor-3 binds and mediates degradation of lipoprotein lipase.”. J. Biol. Chem. 274 (13): 8832–6. DOI:10.1074/jbc.274.13.8832. PMID 10085125.
- Nielsen MS, Madsen P, Christensen EI, et al. (2001). „The sortilin cytoplasmic tail conveys Golgi-endosome transport and binds the VHS domain of the GGA2 sorting protein.”. EMBO J. 20 (9): 2180–90. DOI:10.1093/emboj/20.9.2180. PMC 125444. PMID 11331584.
- Takatsu H, Katoh Y, Shiba Y, Nakayama K (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.”. J. Biol. Chem. 276 (30): 28541–5. DOI:10.1074/jbc.C100218200. PMID 11390366.
- Hampe W, Rezgaoui M, Hermans-Borgmeyer I, Schaller HC (2001). „The genes for the human VPS10 domain-containing receptors are large and contain many small exons.”. Hum. Genet. 108 (6): 529–36. DOI:10.1007/s004390100504. PMID 11499680.
- Shiba T, Takatsu H, Nogi T, et al. (2002). „Structural basis for recognition of acidic-cluster dileucine sequence by GGA1.”. Nature 415 (6874): 937–41. DOI:10.1038/415937a. PMID 11859376.
- Maeda S, Nobukuni T, Shimo-Onoda K, et al. (2002). „Sortilin is upregulated during osteoblastic differentiation of mesenchymal stem cells and promotes extracellular matrix mineralization.”. J. Cell. Physiol. 193 (1): 73–9. DOI:10.1002/jcp.10151. PMID 12209882.
- Martin S, Navarro V, Vincent JP, Mazella J (2002). „Neurotensin receptor-1 and -3 complex modulates the cellular signaling of neurotensin in the HT29 cell line.”. Gastroenterology 123 (4): 1135–43. DOI:10.1053/gast.2002.36000. PMID 12360476.
- Navarro V, Vincent JP, Mazella J (2003). „Shedding of the luminal domain of the neurotensin receptor-3/sortilin in the HT29 cell line.”. Biochem. Biophys. Res. Commun. 298 (5): 760–4. DOI:10.1016/S0006-291X(02)02564-0. PMID 12419319.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). „Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.”. Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. DOI:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Martin S, Vincent JP, Mazella J (2003). „Involvement of the neurotensin receptor-3 in the neurotensin-induced migration of human microglia.”. J. Neurosci. 23 (4): 1198–205. PMID 12598608.
- Lefrancois S, Zeng J, Hassan AJ, et al. (2004). „The lysosomal trafficking of sphingolipid activator proteins (SAPs) is mediated by sortilin.”. EMBO J. 22 (24): 6430–7. DOI:10.1093/emboj/cdg629. PMC 291824. PMID 14657016.