SPRED1
(Redirected from
SPRED1 gene
)Sprouty-related, EVH1 domain-containing protein 1 (Spread-1) is a
exons.[5]
Function
SPRED-1 is a member of the Sprouty family of proteins and is phosphorylated by tyrosine kinase in response to several growth factors. The encoded protein can act as a homodimer or as a heterodimer with SPRED2 to regulate activation of the MAP kinase cascade.[5]
Clinical associations
Defects in this gene are a cause of neurofibromatosis type 1-like syndrome (NFLS).[5]
Mutations in this gene are associated with
- Legius syndrome.[6][7]
- Childhood leukemia[8]
Mutations
The following mutations have been observed:
- An exon 3 c.46C>T mutation leading to p.Arg16Stop.Ras pathwaymutations. Ras pathway mutations are also associated with monosomy 7.
- 3 Nonsense (R16X, E73X, R262X)[9]
- 2 Frameshift (c.1048_c1049 delGG, c.149_1152del 4 bp)[9]
- Missense (V44D)[9]
- p.R18X and p.Q194X with phenotype altered pigmentation without tumoriginesis.[10]
Disease Database
See also
- Neurofibromin 1
- Patients without Neurofibromin 1 or SPRED1 mutations may have SPRED2, SPRED3 or SPRY1, SPRY2, SPRY3 or SPRY4 mutations.[9]
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000166068 - Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000027351 - Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ a b c "Entrez Gene: sprouty-related".
- PMID 19920235.
- Allison Gandey (November 18, 2009). "Legius Syndrome Often Mistaken for Neurofibromatosis Type 1". Medscape.
- ^ "Legius Syndrome (SPRED1) Sequencing & (NF1) Sequencing Exon 22 (Exon 17)" (PDF). ARUP Laboratories. 2010. Archived from the original (PDF) on 2012-05-30. Retrieved 2011-06-07.
- ^ PMID 19643996.
- ^ PMID 19443465.
- PMID 20179001.
Further reading
- Batz C, Hasle H, Bergsträsser E, van den Heuvel-Eibrink MM, Zecca M, Niemeyer CM, Flotho C (March 2010). "Does SPRED1 contribute to leukemogenesis in juvenile myelomonocytic leukemia (JMML)?" (PDF). Blood. 115 (12): 2557–8. PMID 20339110.
- Lock P, I ST, Straffon AF, Schieb H, Hovens CM, Stylli SS (December 2006). "Spred-2 steady-state levels are regulated by phosphorylation and Cbl-mediated ubiquitination". Biochemical and Biophysical Research Communications. 351 (4): 1018–23. PMID 17094949.
- Pasmant E, Sabbagh A, Hanna N, Masliah-Planchon J, Jolly E, Goussard P, Ballerini P, Cartault F, Barbarot S, Landman-Parker J, Soufir N, Parfait B, Vidaud M, Wolkenstein P, Vidaud D, France RN (July 2009). "SPRED1 germline mutations caused a neurofibromatosis type 1 overlapping phenotype" (PDF). Journal of Medical Genetics. 46 (7): 425–30. S2CID 21323989.
- Nonami A, Taketomi T, Kimura A, Saeki K, Takaki H, Sanada T, Taniguchi K, Harada M, Kato R, Yoshimura A (September 2005). "The Sprouty-related protein, Spred-1, localizes in a lipid raft/caveola and inhibits ERK activation in collaboration with caveolin-1". Genes to Cells. 10 (9): 887–95. PMID 16115197.
- Szafranski K, Schindler S, Taudien S, Hiller M, Huse K, Jahn N, Schreiber S, Backofen R, Platzer M (2007). "Violating the splicing rules: TG dinucleotides function as alternative 3' splice sites in U2-dependent introns". Genome Biology. 8 (8): R154. PMID 17672918.
- Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, Yamamoto J, Sekine M, Tsuritani K, Wakaguri H, Ishii S, Sugiyama T, Saito K, Isono Y, Irie R, Kushida N, Yoneyama T, Otsuka R, Kanda K, Yokoi T, Kondo H, Wagatsuma M, Murakawa K, Ishida S, Ishibashi T, Takahashi-Fujii A, Tanase T, Nagai K, Kikuchi H, Nakai K, Isogai T, Sugano S (January 2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Research. 16 (1): 55–65. PMID 16344560.
- Chandramouli S, Yu CY, Yusoff P, Lao DH, Leong HF, Mizuno K, Guy GR (January 2008). "Tesk1 interacts with Spry2 to abrogate its inhibition of ERK phosphorylation downstream of receptor tyrosine kinase signaling". The Journal of Biological Chemistry. 283 (3): 1679–91. PMID 17974561.
- Johne C, Matenia D, Li XY, Timm T, Balusamy K, Mandelkow EM (April 2008). "Spred1 and TESK1--two new interaction partners of the kinase MARKK/TAO1 that link the microtubule and actin cytoskeleton". Molecular Biology of the Cell. 19 (4): 1391–403. PMID 18216281.
- Nonami A, Kato R, Taniguchi K, Yoshiga D, Taketomi T, Fukuyama S, Harada M, Sasaki A, Yoshimura A (December 2004). "Spred-1 negatively regulates interleukin-3-mediated ERK/mitogen-activated protein (MAP) kinase activation in hematopoietic cells". The Journal of Biological Chemistry. 279 (50): 52543–51. PMID 15465815.
- Talmud PJ, Drenos F, Shah S, Shah T, Palmen J, Verzilli C, Gaunt TR, Pallas J, Lovering R, Li K, Casas JP, Sofat R, Kumari M, Rodriguez S, Johnson T, Newhouse SJ, Dominiczak A, Samani NJ, Caulfield M, Sever P, Stanton A, Shields DC, Padmanabhan S, Melander O, Hastie C, Delles C, Ebrahim S, Marmot MG, Smith GD, Lawlor DA, Munroe PB, Day IN, Kivimaki M, Whittaker J, Humphries SE, Hingorani AD (November 2009). "Gene-centric association signals for lipids and apolipoproteins identified via the HumanCVD BeadChip". American Journal of Human Genetics. 85 (5): 628–42. PMID 19913121.
- Colland F, Jacq X, Trouplin V, Mougin C, Groizeleau C, Hamburger A, Meil A, Wojcik J, Legrain P, Gauthier JM (July 2004). "Functional proteomics mapping of a human signaling pathway". Genome Research. 14 (7): 1324–32. PMID 15231748.
- Brems H, Chmara M, Sahbatou M, Denayer E, Taniguchi K, Kato R, Somers R, Messiaen L, De Schepper S, Fryns JP, Cools J, Marynen P, Thomas G, Yoshimura A, Legius E (September 2007). "Germline loss-of-function mutations in SPRED1 cause a neurofibromatosis 1-like phenotype". Nature Genetics. 39 (9): 1120–6. S2CID 35709088.
- Yoshida T, Hisamoto T, Akiba J, Koga H, Nakamura K, Tokunaga Y, Hanada S, Kumemura H, Maeyama M, Harada M, Ogata H, Yano H, Kojiro M, Ueno T, Yoshimura A, Sata M (October 2006). "Spreds, inhibitors of the Ras/ERK signal transduction, are dysregulated in human hepatocellular carcinoma and linked to the malignant phenotype of tumors". Oncogene. 25 (45): 6056–66. S2CID 22188239.
- King JA, Straffon AF, D'Abaco GM, Poon CL, I ST, Smith CM, Buchert M, Corcoran NM, Hall NE, Callus BA, Sarcevic B, Martin D, Lock P, Hovens CM (June 2005). "Distinct requirements for the Sprouty domain for functional activity of Spred proteins". The Biochemical Journal. 388 (Pt 2): 445–54. PMID 15683364.
- Bailey SD, Xie C, Do R, Montpetit A, Diaz R, Mohan V, Keavney B, Yusuf S, Gerstein HC, Engert JC, Anand S (October 2010). "Variation at the NFATC2 locus increases the risk of thiazolidinedione-induced edema in the Diabetes REduction Assessment with ramipril and rosiglitazone Medication (DREAM) study". Diabetes Care. 33 (10): 2250–3. PMID 20628086.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.