Sortilin 1
| Sortilin 1 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| 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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| podaci | |||||||||||
| 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] | |||||||||
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]
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[уреди | уреди извор]
Za sortilin 1 je bilo pokazano da interaguje sa GGA1[5] i GGA2.[5][6]
Vidi još[уреди | уреди извор]
Reference[уреди | уреди извор]
- ^ а б „Entrez Gene: SORT1 sortilin 1”.
- ^ TM, Teslovich; Musunuru K; AV, Smith; et al. (avgust 2010). „Biological, clinical and population relevance of 95 loci for blood lipids”. Nature. 466 (7307): 707—13. PMID 20686565. doi:10.1038/nature09270.
- ^ K, Musunuru; Strong A; Frank-Kamenetsky M; et al. (avgust 2010). „From noncoding variant to phenotype via SORT1 at the 1p13 cholesterol locus”. Nature. 466 (7307): 714—9. PMID 20686566. doi:10.1038/nature09266.
- ^ KS, Hoek; Schlegel NC; OM, Eichhoff; et al. (2008). „Novel MITF targets identified using a two-step DNA microarray strategy”. Pigment Cell Melanoma Res. 21 (6): 665—76. PMID 19067971. doi:10.1111/j.1755-148X.2008.00505.x.
- ^ а б Jacobsen, Linda; Peder, Madsen; et al. (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. ISSN 0014-5793. PMID 11821067. doi:10.1016/S0014-5793(01)03299-9.
- ^ Nielsen, M S; P, Madsen; et al. (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. ISSN 0261-4189. PMC 125444
. PMID 11331584. doi:10.1093/emboj/20.9.2180.
Literatura[уреди | уреди извор]
- Vincent JP, Mazella J, Kitabgi P (1999). „Neurotensin and neurotensin receptors.”. Trends Pharmacol. Sci. 20 (7): 302—9. PMID 10390649. doi:10.1016/S0165-6147(99)01357-7.
- J, Mazella (2001). „Sortilin/neurotensin receptor-3: a new tool to investigate neurotensin signaling and cellular trafficking?”. Cell. Signal. 13 (1): 1—6. PMID 11257441. doi:10.1016/S0898-6568(00)00130-3.
- CM, Petersen; Nielsen MS; A, Nykjaer; 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. PMID 9013611. doi:10.1074/jbc.272.6.3599.
- Lin BZ, Pilch PF, Kandror KV (1997). „Sortilin is a major protein component of Glut4-containing vesicles.”. J. Biol. Chem. 272 (39): 24145—7. PMID 9305862. doi:10.1074/jbc.272.39.24145.
- J, Tauris; Ellgaard L; C, Jacobsen; 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. PMID 9657377. doi:10.1016/S0014-5793(98)00559-6.
- J, Mazella; Zsürger N; V, Navarro; et al. (1998). „The 100-kDa neurotensin receptor is gp95/sortilin, a non-G-protein-coupled receptor.”. J. Biol. Chem. 273 (41): 26273—6. PMID 9756851. doi:10.1074/jbc.273.41.26273.
- Munck Petersen C; MS, Nielsen; Jacobsen C; et al. (1999). „Propeptide cleavage conditions sortilin/neurotensin receptor-3 for ligand binding.”. EMBO J. 18 (3): 595—604. PMC 1171152 . PMID 9927419. doi:10.1093/emboj/18.3.595.
- MS, Nielsen; Jacobsen C; G, Olivecrona; et al. (1999). „Sortilin/neurotensin receptor-3 binds and mediates degradation of lipoprotein lipase.”. J. Biol. Chem. 274 (13): 8832—6. PMID 10085125. doi:10.1074/jbc.274.13.8832.
- MS, Nielsen; Madsen P; EI, Christensen; 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. PMC 125444 . PMID 11331584. doi:10.1093/emboj/20.9.2180.
- 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. PMID 11390366. doi:10.1074/jbc.C100218200.
- 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. PMID 11499680. doi:10.1007/s004390100504.
- T, Shiba; Takatsu H; T, Nogi; et al. (2002). „Structural basis for recognition of acidic-cluster dileucine sequence by GGA1.”. Nature. 415 (6874): 937—41. PMID 11859376. doi:10.1038/415937a.
- S, Maeda; 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. PMID 12209882. doi:10.1002/jcp.10151.
- 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. PMID 12360476. doi:10.1053/gast.2002.36000.
- 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. PMID 12419319. doi:10.1016/S0006-291X(02)02564-0.
- RL, Strausberg; Feingold EA; LH, Grouse; 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. PMC 139241 . PMID 12477932. doi:10.1073/pnas.242603899.
- 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.
- S, Lefrancois; Zeng J; AJ, Hassan; et al. (2004). „The lysosomal trafficking of sphingolipid activator proteins (SAPs) is mediated by sortilin.”. EMBO J. 22 (24): 6430—7. PMC 291824 . PMID 14657016. doi:10.1093/emboj/cdg629.