SUFU
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesSUFU, PRO1280, SUFUH, SUFUXL, SUFU negative regulator of hedgehog signaling, JBTS32
External IDsOMIM: 607035 MGI: 1345643 HomoloGene: 9262 GeneCards: SUFU
Orthologs
SpeciesHumanMouse
Entrez

51684

24069

Ensembl

ENSG00000107882

ENSMUSG00000025231

UniProt

Q9UMX1

Q9Z0P7

RefSeq (mRNA)

NM_001178133
NM_016169

NM_001025391
NM_015752

RefSeq (protein)

NP_001171604
NP_057253

NP_001020562
NP_056567

Location (UCSC)Chr 10: 102.5 – 102.63 MbChr 19: 46.39 – 46.48 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Suppressor of fused homolog is a protein that in humans is encoded by the SUFU gene.[5][6] In molecular biology, the protein domain suppressor of fused protein (Sufu) has an important role in the cell. The Sufu is important in negatively regulating an important signalling pathway in the cell, the Hedgehog signalling pathway (HH). This particular pathway is crucial in embryonic development. There are several homologues of Sufu, found in a wide variety of organisms.

Function

SUFU encodes a component of the sonic hedgehog (SHH) / patched (PTCH) signaling pathway. Mutations in genes encoding components of this pathway are deleterious for normal development and are associated with cancer-predisposing syndromes (e.g., holoprosencephaly, HPE3, basal cell nevus syndrome, BCNS, and Greig cephalopolysyndactyly syndrome, GCPS).[6]Sufu has also been found to have a crucial role in tumour suppression. To be more specific, it has a tumour-suppressor gene that predisposes, or in other words makes individuals more susceptible to medulloblastoma, because it modulates the SHH signalling pathway.[7] The N-terminal domain, which this entry refers to contains Gli transcription factors.[8]

Interactions

SUFU has been shown to interact with GLI1,[9][10][11] GLI3[12] and PEX26.[13]

Conservation

The human ortholog of Drosophila suppressor of fused, has a conserved sequence, this means that particular amino acids have remained the same throughout evolution. Consequently, they have very similar roles in repressing Hedgehog signalling. It represses the Gli and Ci transcription factors of the Hedgehog pathway,[14] and functions by binding to these proteins and preventing their translocation to the nucleus. Homologues of Sufu have been found in bacteria. However their function remains to be elucidated.

Structure

Sufu is actually protein that contains two domains.[8] In eukaryotic Sufu, an additional domain is found at the C terminus of the protein. This protein domain also binds to the C-terminal domain of the Gli/Ci transcription factors, inhibiting their activity.[5]

Genes

Human gene that encodes SUFU, also named SUFU, is found to be localized on chromosome 10q24–25, and contains 12 exons.[14]

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000107882 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000025231 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. 1 2 Merchant M, Vajdos FF, Ultsch M, Maun HR, Wendt U, Cannon J, Desmarais W, Lazarus RA, de Vos AM, de Sauvage FJ (Sep 2004). "Suppressor of fused regulates Gli activity through a dual binding mechanism". Mol Cell Biol. 24 (19): 8627–41. doi:10.1128/MCB.24.19.8627-8641.2004. PMC 516763. PMID 15367681.
  6. 1 2 "Entrez Gene: SUFU suppressor of fused homolog (Drosophila)".
  7. Taylor MD, Liu L, Raffel C, Hui CC, Mainprize TG, Zhang X, Agatep R, Chiappa S, Gao L, Lowrance A, Hao A, Goldstein AM, Stavrou T, Scherer SW, Dura WT, Wainwright B, Squire JA, Rutka JT, Hogg D (July 2002). "Mutations in SUFU predispose to medulloblastoma". Nat. Genet. 31 (3): 306–10. doi:10.1038/ng916. PMID 12068298. S2CID 6882566.
  8. 1 2 Das D, Finn RD, Abdubek P, Astakhova T, Axelrod HL, Bakolitsa C, et al. (2010). "The crystal structure of a bacterial Sufu-like protein defines a novel group of bacterial proteins that are similar to the N-terminal domain of human Sufu". Protein Sci. 19 (11): 2131–40. doi:10.1002/pro.497. PMC 3005784. PMID 20836087.
  9. Stone DM, Murone M, Luoh S, Ye W, Armanini MP, Gurney A, Phillips H, Brush J, Goddard A, de Sauvage FJ, Rosenthal A (December 1999). "Characterization of the human suppressor of fused, a negative regulator of the zinc-finger transcription factor Gli". J. Cell Sci. 112 (23): 4437–48. doi:10.1242/jcs.112.23.4437. PMID 10564661.
  10. Kogerman P, Grimm T, Kogerman L, Krause D, Undén AB, Sandstedt B, Toftgård R, Zaphiropoulos PG (September 1999). "Mammalian suppressor-of-fused modulates nuclear-cytoplasmic shuttling of Gli-1". Nat. Cell Biol. 1 (5): 312–9. doi:10.1038/13031. PMID 10559945. S2CID 6907964.
  11. Dunaeva M, Michelson P, Kogerman P, Toftgard R (February 2003). "Characterization of the physical interaction of Gli proteins with SUFU proteins". J. Biol. Chem. 278 (7): 5116–22. doi:10.1074/jbc.M209492200. PMID 12426310.
  12. Humke EW, Dorn KV, Milenkovic L, Scott MP, Rohatgi R (April 2010). "The output of Hedgehog signaling is controlled by the dynamic association between Suppressor of Fused and the Gli proteins". Genes Dev. 24 (7): 670–82. doi:10.1101/gad.1902910. PMC 2849124. PMID 20360384.
  13. Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
  14. 1 2 Rubin JB, Rowitch DH (July 2002). "Medulloblastoma: a problem of developmental biology". Cancer Cell. 2 (1): 7–8. doi:10.1016/S1535-6108(02)00090-9. PMID 12150819.

Further reading


This article incorporates text from the public domain Pfam and InterPro: IPR020941
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