Neuropilin 1

From Wikipedia, the free encyclopedia

Neuropilin 1

PDB rendering based on 1kex.

Available structures: 1kex, 2orx, 2orz

Identifiers

Symbol(s)

NRP1; NRP; CD304; DKFZp686A03134; DKFZp781F1414; VEGF165R

External IDs

OMIM: 602069 MGI: 106206 HomoloGene: 2876

Gene ontology
Molecular Function:	• receptor activity • vascular endothelial growth factor receptor activity • protein binding • semaphorin receptor activity
Cellular Component:	• membrane fraction • endoplasmic reticulum • membrane • integral to membrane
Biological Process:	• angiogenesis • cell adhesion • signal transduction • cell-cell signaling • multicellular organismal development • nervous system development • axon guidance • heart development • positive regulation of cell proliferation • organ morphogenesis • dendrite development • cell differentiation • negative regulation of axon extension • vascular endothelial growth factor receptor signaling pathway

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001024628 (mRNA)
NP_001019799 (protein)

NM_008737 (mRNA)
NP_032763 (protein)

Location

Chr 10: 33.51 - 33.67 Mb

Chr 8: 131.25 - 131.39 Mb

Pubmed search

[1]

[2]

Neuropilin 1, also known as NRP1, is a human gene.^[1]. This is one of two human neuropilins.

NRP1 is a membrane-bound coreceptor to a tyrosine kinase receptor for both vascular endothelial growth factor (VEGF; MIM 192240) and semaphorin (see SEMA3A; MIM 603961) family members. NRP1 plays versatile roles in angiogenesis, axon guidance, cell survival, migration, and invasion.[supplied by OMIM]^[1]

[edit] References

^ ^a ^b Entrez Gene: NRP1 neuropilin 1.

[edit] Further reading

Zachary I, Gliki G (2001). "Signaling transduction mechanisms mediating biological actions of the vascular endothelial growth factor family.". Cardiovasc. Res. 49 (3): 568–81. PMID 11166270.
He Z, Tessier-Lavigne M (1997). "Neuropilin is a receptor for the axonal chemorepellent Semaphorin III.". Cell 90 (4): 739–51. PMID 9288753.
Chen H, Chédotal A, He Z, et al. (1997). "Neuropilin-2, a novel member of the neuropilin family, is a high affinity receptor for the semaphorins Sema E and Sema IV but not Sema III.". Neuron 19 (3): 547–59. PMID 9331348.
Soker S, Takashima S, Miao HQ, et al. (1998). "Neuropilin-1 is expressed by endothelial and tumor cells as an isoform-specific receptor for vascular endothelial growth factor.". Cell 92 (6): 735–45. PMID 9529250.
Giger RJ, Urquhart ER, Gillespie SK, et al. (1999). "Neuropilin-2 is a receptor for semaphorin IV: insight into the structural basis of receptor function and specificity.". Neuron 21 (5): 1079–92. PMID 9856463.
Chen H, He Z, Bagri A, Tessier-Lavigne M (1999). "Semaphorin-neuropilin interactions underlying sympathetic axon responses to class III semaphorins.". Neuron 21 (6): 1283–90. PMID 9883722.
Takahashi T, Nakamura F, Jin Z, et al. (1999). "Semaphorins A and E act as antagonists of neuropilin-1 and agonists of neuropilin-2 receptors.". Nat. Neurosci. 1 (6): 487–93. doi:10.1038/2203. PMID 10196546.
Rossignol M, Beggs AH, Pierce EA, Klagsbrun M (1999). "Human neuropilin-1 and neuropilin-2 map to 10p12 and 2q34, respectively.". Genomics 57 (3): 459–60. doi:10.1006/geno.1999.5790. PMID 10329017.
Makinen T, Olofsson B, Karpanen T, et al. (1999). "Differential binding of vascular endothelial growth factor B splice and proteolytic isoforms to neuropilin-1.". J. Biol. Chem. 274 (30): 21217–22. PMID 10409677.
Cai H, Reed RR (1999). "Cloning and characterization of neuropilin-1-interacting protein: a PSD-95/Dlg/ZO-1 domain-containing protein that interacts with the cytoplasmic domain of neuropilin-1.". J. Neurosci. 19 (15): 6519–27. PMID 10414980.
Takahashi T, Fournier A, Nakamura F, et al. (1999). "Plexin-neuropilin-1 complexes form functional semaphorin-3A receptors.". Cell 99 (1): 59–69. PMID 10520994.
Tamagnone L, Artigiani S, Chen H, et al. (1999). "Plexins are a large family of receptors for transmembrane, secreted, and GPI-anchored semaphorins in vertebrates.". Cell 99 (1): 71–80. PMID 10520995.
Gagnon ML, Bielenberg DR, Gechtman Z, et al. (2000). "Identification of a natural soluble neuropilin-1 that binds vascular endothelial growth factor: In vivo expression and antitumor activity.". Proc. Natl. Acad. Sci. U.S.A. 97 (6): 2573–8. doi:10.1073/pnas.040337597. PMID 10688880.
Gluzman-Poltorak Z, Cohen T, Herzog Y, Neufeld G (2000). "Neuropilin-2 is a receptor for the vascular endothelial growth factor (VEGF) forms VEGF-145 and VEGF-165 [corrected].". J. Biol. Chem. 275 (24): 18040–5. doi:10.1074/jbc.M909259199. PMID 10748121.
Fuh G, Garcia KC, de Vos AM (2000). "The interaction of neuropilin-1 with vascular endothelial growth factor and its receptor flt-1.". J. Biol. Chem. 275 (35): 26690–5. doi:10.1074/jbc.M003955200. PMID 10842181.
Rossignol M, Gagnon ML, Klagsbrun M (2001). "Genomic organization of human neuropilin-1 and neuropilin-2 genes: identification and distribution of splice variants and soluble isoforms.". Genomics 70 (2): 211–22. doi:10.1006/geno.2000.6381. PMID 11112349.
Simpson JC, Wellenreuther R, Poustka A, et al. (2001). "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing.". EMBO Rep. 1 (3): 287–92. doi:10.1093/embo-reports/kvd058. PMID 11256614.
Whitaker GB, Limberg BJ, Rosenbaum JS (2001). "Vascular endothelial growth factor receptor-2 and neuropilin-1 form a receptor complex that is responsible for the differential signaling potency of VEGF(165) and VEGF(121).". J. Biol. Chem. 276 (27): 25520–31. doi:10.1074/jbc.M102315200. PMID 11333271.
Walter JW, North PE, Waner M, et al. (2002). "Somatic mutation of vascular endothelial growth factor receptors in juvenile hemangioma.". Genes Chromosomes Cancer 33 (3): 295–303. PMID 11807987.