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{{Infobox_gene}}
{{PBB_Controls
'''''FBXL3''''' is a [[gene]] in humans and mice that encodes the F-box/LRR-repeat protein 3 (FBXL3).<ref name="pmid10531035">{{cite journal | vauthors = Cenciarelli C, Chiaur DS, Guardavaccaro D, Parks W, Vidal M, Pagano M | title = Identification of a family of human F-box proteins | journal = Current Biology | volume = 9 | issue = 20 | pages = 1177–9 | date = October 1999 | pmid = 10531035 | doi = 10.1016/S0960-9822(00)80020-2 }}</ref><ref name="pmid10828603">{{cite journal | vauthors = Chiaur DS, Murthy S, Cenciarelli C, Parks W, Loda M, Inghirami G, Demetrick D, Pagano M | title = Five human genes encoding F-box proteins: chromosome mapping and analysis in human tumors | journal = Cytogenetics and Cell Genetics | volume = 88 | issue = 3–4 | pages = 255–8 | date = Jun 2000 | pmid = 10828603 | doi = 10.1159/000015532 }}</ref>
| update_page = yes
FBXL3 is a member of the [[F-box protein]] family, which constitutes one of the four subunits in the [[SCF complex|SCF]] [[ubiquitin ligase]] complex.<ref name="Entrez_Gene_FBXL3">{{cite web |url=https://www.ncbi.nlm.nih.gov/gene?cmd=Retrieve&dopt=full_report&list_uids=26224 | title = FBXL3 F-box and leucine rich repeat protein 3 [ Homo sapiens (human) |work = Entrez Gene | access-date = 27 April 2017 }}</ref>
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
The FBXL3 protein participates in the [[negative feedback]] loop responsible for generating molecular [[circadian rhythms]] in mammals by binding to the [[CRY1]] and [[CRY2]] proteins to facilitate their [[polyubiquitination]] by the SCF complex and their subsequent degradation by the [[proteasome]].<ref name="VirshupForger2007">{{cite journal | vauthors = Virshup DM, Forger DB | title = After hours keeps clock researchers CRYing Overtime | journal = Cell | volume = 129 | issue = 5 | pages = 857–9 | date = June 2007 | pmid = 17540165 | doi = 10.1016/j.cell.2007.05.015 }}</ref> FBXL3 also plays a role in the related loop that regulates the transcription of the [[BMAL1]] gene.<ref name="Ko2006">{{cite journal | vauthors = Ko CH, Takahashi JS | title = Molecular components of the mammalian circadian clock | journal = Human Molecular Genetics | volume = 15 Spec No 2 | issue = Review Issue 2 | pages = R271–7 | date = October 2006 | pmid = 16987893 | doi = 10.1093/hmg/ddl207 }}</ref>
{{GNF_Protein_box
| image =
| image_source = 
| PDB =  
| Name = F-box and leucine-rich repeat protein 3
| HGNCid = 13599
| Symbol = FBXL3
| AltSymbols =; FBL3; FBL3A; FBXL3A
| OMIM = 605653
| ECnumber =
| Homologene = 8127
| MGIid = 1354702
| GeneAtlas_image1 = 225132_at
| GeneAtlas_image2 = 54900_at
| GeneAtlas_image3 = 62716_at
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = 03:19, 2 October 2007 (UTC)
| Function = {{GNF_GO|id=GO:0004842 |text = ubiquitin-protein ligase activity}}
| Component = {{GNF_GO|id=GO:0000151 |text = ubiquitin ligase complex}} {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0016567 |text = protein ubiquitination}}  
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 26224
    | Hs_Ensembl = ENSG00000005812
    | Hs_RefseqProtein = NP_036290
    | Hs_RefseqmRNA = NM_012158
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 13
    | Hs_GenLoc_start = 76477388
    | Hs_GenLoc_end = 76499295
    | Hs_Uniprot = Q9UKT7
    | Mm_EntrezGene = 50789
    | Mm_Ensembl = ENSMUSG00000022124
    | Mm_RefseqmRNA = XM_975284
    | Mm_RefseqProtein = XP_980378
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 14
    | Mm_GenLoc_start = 101967535
    | Mm_GenLoc_end = 101986017
    | Mm_Uniprot = Q3TJJ7
  }}
}}
'''F-box and leucine-rich repeat protein 3''', also known as '''FBXL3''', is a human [[gene]].


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
==Discovery==
{{PBB_Summary
The ''Fbxl3'' gene function was independently identified in 2007 by three groups, lead by [[Joseph S. Takahashi]], Dr. Patrick Nolan and [[Michael Hastings (geneticist)|Michael Hastings]], and [http://cbio.med.upenn.edu/bioTemplate.asp?pageID=3 Lucio Busino] respectively. Takahashi used [[forward genetics]] [[N-ethyl-N-nitrosourea]] (ENU) [[mutagenesis]] to screen for mice with varied circadian activity which led to the discovery of the ''Overtime'' (''Ovtm'') mutant of the ''Fbxl3'' gene.  Nolan discovered the ''Fbxl3'' mutation ''After hours'' (''Afh'') by a forward screen assessing wheel activity behavior of mutagenized mice.<ref name="VirshupForger2007" /> Busino discovered that the FBXL3 protein is necessary for the reactivation of the [[CLOCK]] and BMAL1 protein [[heterodimer]] by inducing the degradation of CRY proteins.<ref name="pmid17463251">{{cite journal | vauthors = Busino L, Bassermann F, Maiolica A, Lee C, Nolan PM, Godinho SI, Draetta GF, Pagano M | title = SCFFbxl3 controls the oscillation of the circadian clock by directing the degradation of cryptochrome proteins | journal = Science | volume = 316 | issue = 5826 | pages = 900–4 | date = May 2007 | pmid = 17463251 | doi = 10.1126/science.1141194 }} </ref>
| section_title =
| summary_text = This gene encodes a member of the F-box protein family which is characterized by an approximately 40 amino acid motif, the F-box. The F-box proteins constitute one of the four subunits of ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box), which function in phosphorylation-dependent ubiquitination. The F-box proteins are divided into 3 classes: Fbws containing WD-40 domains, Fbls containing leucine-rich repeats, and Fbxs containing either different protein-protein interaction modules or no recognizable motifs. The protein encoded by this gene belongs to the Fbls class and, in addition to an F-box, contains several tandem leucine-rich repeats and is localized in the nucleus.<ref>{{cite web | title = Entrez Gene: FBXL3 F-box and leucine-rich repeat protein 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=26224| accessdate = }}</ref>
}}


==References==
===''Overtime''===
{{reflist|2}}
Mice with the homozygous mutation of ''Ovtm'', free run with an intrinsic period of 26 hours. ''Overtime'' is a loss of function mutation caused by a substitution of [[isoleucine]] to [[threonine]] in the region of FBXL3 that binds to CRY. In mice with this mutation, levels of the proteins [[PER1]] and [[PER2]] are decreased, while levels of CRY proteins do not differ from those of wild type mice. The stabilization of CRY protein levels leads to continued repression of ''Per1'' and ''Per2'' transcription and translation. <ref name="VirshupForger2007" /><ref name="SiepkaYoo2007">{{cite journal | vauthors = Siepka SM, Yoo SH, Park J, Lee C, Takahashi JS | title = Genetics and neurobiology of circadian clocks in mammals | journal = Cold Spring Harbor Symposia on Quantitative Biology | volume = 72 | issue = 1 | pages = 251–9 | year = 2007 | pmid = 18419282 | doi = 10.1101/sqb.2007.72.052 }}</ref>
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =  
}}
{{refend}}


{{protein-stub}}
===''After-hours''===
The ''After-hours'' mutation is a substitution of [[cysteine]] to [[serine]] at position 358. Similar to ''Overtime'', the mutation occurs in the region where FBXL3 binds to CRY. Mice homozygous for the ''Afh'' mutation have a free running period of about 27 hours. The ''Afh'' mutation delays the rate of CRY protein degradation, therefore affecting the transcription of PER2 protein. <ref name="VirshupForger2007" /><ref name="GodinhoMaywood2007">{{cite journal | vauthors = Godinho SI, Maywood ES, Shaw L, Tucci V, Barnard AR, Busino L, Pagano M, Kendall R, Quwailid MM, Romero MR, O'neill J, Chesham JE, Brooker D, Lalanne Z, Hastings MH, Nolan PM | title = The after-hours mutant reveals a role for Fbxl3 in determining mammalian circadian period | journal = Science | volume = 316 | issue = 5826 | pages = 897–900 | date = May 2007 | pmid = 17463252 | doi = 10.1126/science.1141138 }}</ref>


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===''Fbxl21''===
The closest homologue to ''Fbxl3'' is ''Fbxl21'' as it also binds to the CRY1 and CRY2 proteins. Predominantly localized to the cytosol, ''Fbxl21'' antagonizes the action of ''Fbxl3'' through [[ubiquitination]] and stabilization of CRY proteins instead of leading it to degradation.<ref name="HiranoYumimoto2013">{{cite journal | vauthors = Hirano A, Yumimoto K, Tsunematsu R, Matsumoto M, Oyama M, Kozuka-Hata H, Nakagawa T, Lanjakornsiripan D, Nakayama KI, Fukada Y | title = FBXL21 regulates oscillation of the circadian clock through ubiquitination and stabilization of cryptochromes | journal = Cell | volume = 152 | issue = 5 | pages = 1106–18 | date = February 2013 | pmid = 23452856 | doi = 10.1016/j.cell.2013.01.054 }}</ref>


{{WikiDoc Sources}}
== Characteristics ==
The human ''FBXL3'' gene is located on the long arm of [[chromosome 13]] at position 22.3.<ref name="pmid18797559">{{cite journal | vauthors = Toh KL | title = Basic science review on circadian rhythm biology and circadian sleep disorders | journal = Annals of the Academy of Medicine, Singapore | volume = 37 | issue = 8 | pages = 662–8 | date = August 2008 | pmid = 18797559 | url =  http://www.annals.edu.sg/pdf/37VolNo8Aug2008/V37N8p662.pdf | doi =  }} </ref> The protein is composed of 428 amino acids and has a mass of 48,707 Daltons.<ref name="pmid20878054">{{cite journal | vauthors = Sato K, Yoshida K | title = Augmentation of the ubiquitin-mediated proteolytic system by F-box and additional motif-containing proteins (Review) | journal = International Journal of Oncology | volume = 37 | issue = 5 | pages = 1071–6 | date = November 2010 | pmid = 20878054 | doi = 10.3892/ijo_00000758 }} </ref> The FBXL3 protein contains an F-box domain, characterized by a 40 amino acid motif that mediates protein-protein interactions, and several tandem [[leucine-rich repeats]] used for substrate recognition. It has eight [[post-translational modification]] sites involving ubiquitination and four sites involving [[phosphorylation]]. The FBXL3 protein is predominantly localized to the nucleus. It is one of four subunits of a ubiquitin ligase complex called SKP1-CUL1-F-box-protein, which includes the proteins CUL1, SKP1, and RBX1. <ref name="SiepkaYoo2007" /><ref name="Entrez_Gene_FBXL3" />
 
== Function ==
 
The FBXL3 protein plays a role in the negative feedback loop of the mammalian molecular circadian rhythm. The PER and CRY proteins inhibit the transcription factors CLOCK and BMAL1. The degradation of PER and CRY prevent the inhibition of the CLOCK and BMAL1 protein heterodimer. In the nucleus, the FBXL3 protein targets CRY1 and CRY2 for polyubiquitination, which triggers the degradation of the proteins by the [[proteasome]].<ref name="VirshupForger2007">{{cite journal | vauthors = Virshup DM, Forger DB | title = After hours keeps clock researchers CRYing Overtime | journal = Cell | volume = 129 | issue = 5 | pages = 857–9 | date = June 2007 | pmid = 17540165 | doi = 10.1016/j.cell.2007.05.015 }}</ref> FBXL3 binds to CRY2 by occupying its [[flavin adenine dinucleotide]] (FAD) cofactor pocket with a [[C-terminal]] tail and buries the PER-binding interface on the CRY2 protein.<ref name="XingBusino2013">{{cite journal | vauthors = Xing W, Busino L, Hinds TR, Marionni ST, Saifee NH, Bush MF, Pagano M, Zheng N | title = SCF(FBXL3) ubiquitin ligase targets cryptochromes at their cofactor pocket | journal = Nature | volume = 496 | issue = 7443 | pages = 64–8 | date = April 2013 | pmid = 23503662 | doi = 10.1038/nature11964 }}</ref>
 
The FBXL3 protein is also involved in a related feedback loop that regulates the transcription of the ''Bmal1'' gene. ''Bmal1'' expression is regulated by the binding of [[Rev-ErbA alpha|REV-ERBα]] and [[RAR-related orphan receptor alpha|RORα]] proteins to retinoic acid-related orphan receptor response elements (ROREs) in the ''Bmal1'' [[promoter (genetics)|promoter]] region. The binding of the REV-ERBα protein to the promoter represses expression, while RORα binding activates expression.<ref name="Ko2006" />  FBXL3 decreases the repression of ''Bmal1'' transcription by inactivating the REV-ERBα and [[HDAC3]] repressor complex.<ref name="ShiXing2013">{{cite journal | vauthors = Shi G, Xing L, Liu Z, Qu Z, Wu X, Dong Z, Wang X, Gao X, Huang M, Yan J, Yang L, Liu Y, Ptácek LJ, Xu Y | title = Dual roles of FBXL3 in the mammalian circadian feedback loops are important for period determination and robustness of the clock | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 110 | issue = 12 | pages = 4750–5 | date = March 2013 | pmid = 23471982 | doi = 10.1073/pnas.1302560110 }}</ref>
 
The FBXL3 protein has also been found to cooperatively degrade [[c-MYC]] when bound to CRY2. The c-MYC protein is a [[transcription factor]] important in regulating [[cell proliferation]]. The CRY2 protein can function as a co-factor for the FBXL3 ligase complex and interacts with [[phosphorylated]] c-MYC. This interaction promotes the ubiquitination and degradation of the c-MYC protein. <ref name="HuberPapp2016">{{cite journal | vauthors = Huber AL, Papp SJ, Chan AB, Henriksson E, Jordan SD, Kriebs A, Nguyen M, Wallace M, Li Z, Metallo CM, Lamia KA | title = CRY2 and FBXL3 Cooperatively Degrade c-MYC | journal = Molecular Cell | volume = 64 | issue = 4 | pages = 774–789 | date = November 2016 | pmid = 27840026 | doi = 10.1016/j.molcel.2016.10.012 }}</ref>
 
== Interactions ==
 
FBXL3 has been shown to [[Protein-protein interaction|interact]] with:
* [[SKP1A]]<ref name=autogenerated1>{{cite journal | vauthors = Cenciarelli C, Chiaur DS, Guardavaccaro D, Parks W, Vidal M, Pagano M | title = Identification of a family of human F-box proteins | journal = Current Biology | volume = 9 | issue = 20 | pages = 1177–9 | date = October 1999 | pmid = 10531035 | doi = 10.1016/S0960-9822(00)80020-2 }}</ref>
* [[CRY1]] <ref name="VirshupForger2007" />
* [[CRY2]] <ref name="VirshupForger2007" /><ref name="XingBusino2013" /><ref name="HuberPapp2016" />
* [[Rev-ErbA alpha|REV-ERBα]] <ref name="ShiXing2013" />
* [[HDAC3]] <ref name="ShiXing2013" />
* [[c-MYC]] <ref name="HuberPapp2016" />
 
== References ==
{{reflist|33em}}

Revision as of 16:28, 21 August 2017

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External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
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RefSeq (mRNA)

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FBXL3 is a gene in humans and mice that encodes the F-box/LRR-repeat protein 3 (FBXL3).[1][2] FBXL3 is a member of the F-box protein family, which constitutes one of the four subunits in the SCF ubiquitin ligase complex.[3]

The FBXL3 protein participates in the negative feedback loop responsible for generating molecular circadian rhythms in mammals by binding to the CRY1 and CRY2 proteins to facilitate their polyubiquitination by the SCF complex and their subsequent degradation by the proteasome.[4] FBXL3 also plays a role in the related loop that regulates the transcription of the BMAL1 gene.[5]

Discovery

The Fbxl3 gene function was independently identified in 2007 by three groups, lead by Joseph S. Takahashi, Dr. Patrick Nolan and Michael Hastings, and Lucio Busino respectively. Takahashi used forward genetics N-ethyl-N-nitrosourea (ENU) mutagenesis to screen for mice with varied circadian activity which led to the discovery of the Overtime (Ovtm) mutant of the Fbxl3 gene. Nolan discovered the Fbxl3 mutation After hours (Afh) by a forward screen assessing wheel activity behavior of mutagenized mice.[4] Busino discovered that the FBXL3 protein is necessary for the reactivation of the CLOCK and BMAL1 protein heterodimer by inducing the degradation of CRY proteins.[6]

Overtime

Mice with the homozygous mutation of Ovtm, free run with an intrinsic period of 26 hours. Overtime is a loss of function mutation caused by a substitution of isoleucine to threonine in the region of FBXL3 that binds to CRY. In mice with this mutation, levels of the proteins PER1 and PER2 are decreased, while levels of CRY proteins do not differ from those of wild type mice. The stabilization of CRY protein levels leads to continued repression of Per1 and Per2 transcription and translation. [4][7]

After-hours

The After-hours mutation is a substitution of cysteine to serine at position 358. Similar to Overtime, the mutation occurs in the region where FBXL3 binds to CRY. Mice homozygous for the Afh mutation have a free running period of about 27 hours. The Afh mutation delays the rate of CRY protein degradation, therefore affecting the transcription of PER2 protein. [4][8]

Fbxl21

The closest homologue to Fbxl3 is Fbxl21 as it also binds to the CRY1 and CRY2 proteins. Predominantly localized to the cytosol, Fbxl21 antagonizes the action of Fbxl3 through ubiquitination and stabilization of CRY proteins instead of leading it to degradation.[9]

Characteristics

The human FBXL3 gene is located on the long arm of chromosome 13 at position 22.3.[10] The protein is composed of 428 amino acids and has a mass of 48,707 Daltons.[11] The FBXL3 protein contains an F-box domain, characterized by a 40 amino acid motif that mediates protein-protein interactions, and several tandem leucine-rich repeats used for substrate recognition. It has eight post-translational modification sites involving ubiquitination and four sites involving phosphorylation. The FBXL3 protein is predominantly localized to the nucleus. It is one of four subunits of a ubiquitin ligase complex called SKP1-CUL1-F-box-protein, which includes the proteins CUL1, SKP1, and RBX1. [7][3]

Function

The FBXL3 protein plays a role in the negative feedback loop of the mammalian molecular circadian rhythm. The PER and CRY proteins inhibit the transcription factors CLOCK and BMAL1. The degradation of PER and CRY prevent the inhibition of the CLOCK and BMAL1 protein heterodimer. In the nucleus, the FBXL3 protein targets CRY1 and CRY2 for polyubiquitination, which triggers the degradation of the proteins by the proteasome.[4] FBXL3 binds to CRY2 by occupying its flavin adenine dinucleotide (FAD) cofactor pocket with a C-terminal tail and buries the PER-binding interface on the CRY2 protein.[12]

The FBXL3 protein is also involved in a related feedback loop that regulates the transcription of the Bmal1 gene. Bmal1 expression is regulated by the binding of REV-ERBα and RORα proteins to retinoic acid-related orphan receptor response elements (ROREs) in the Bmal1 promoter region. The binding of the REV-ERBα protein to the promoter represses expression, while RORα binding activates expression.[5] FBXL3 decreases the repression of Bmal1 transcription by inactivating the REV-ERBα and HDAC3 repressor complex.[13]

The FBXL3 protein has also been found to cooperatively degrade c-MYC when bound to CRY2. The c-MYC protein is a transcription factor important in regulating cell proliferation. The CRY2 protein can function as a co-factor for the FBXL3 ligase complex and interacts with phosphorylated c-MYC. This interaction promotes the ubiquitination and degradation of the c-MYC protein. [14]

Interactions

FBXL3 has been shown to interact with:

References

  1. ↑ Cenciarelli C, Chiaur DS, Guardavaccaro D, Parks W, Vidal M, Pagano M (October 1999). "Identification of a family of human F-box proteins". Current Biology. 9 (20): 1177–9. doi:10.1016/S0960-9822(00)80020-2. PMID 10531035.
  2. ↑ Chiaur DS, Murthy S, Cenciarelli C, Parks W, Loda M, Inghirami G, Demetrick D, Pagano M (Jun 2000). "Five human genes encoding F-box proteins: chromosome mapping and analysis in human tumors". Cytogenetics and Cell Genetics. 88 (3–4): 255–8. doi:10.1159/000015532. PMID 10828603.
  3. ↑ 3.0 3.1 "FBXL3 F-box and leucine rich repeat protein 3 [ Homo sapiens (human)". Entrez Gene. Retrieved 27 April 2017.
  4. ↑ 4.0 4.1 4.2 4.3 4.4 4.5 4.6 Virshup DM, Forger DB (June 2007). "After hours keeps clock researchers CRYing Overtime". Cell. 129 (5): 857–9. doi:10.1016/j.cell.2007.05.015. PMID 17540165.
  5. ↑ 5.0 5.1 Ko CH, Takahashi JS (October 2006). "Molecular components of the mammalian circadian clock". Human Molecular Genetics. 15 Spec No 2 (Review Issue 2): R271–7. doi:10.1093/hmg/ddl207. PMID 16987893.
  6. ↑ Busino L, Bassermann F, Maiolica A, Lee C, Nolan PM, Godinho SI, Draetta GF, Pagano M (May 2007). "SCFFbxl3 controls the oscillation of the circadian clock by directing the degradation of cryptochrome proteins". Science. 316 (5826): 900–4. doi:10.1126/science.1141194. PMID 17463251.
  7. ↑ 7.0 7.1 Siepka SM, Yoo SH, Park J, Lee C, Takahashi JS (2007). "Genetics and neurobiology of circadian clocks in mammals". Cold Spring Harbor Symposia on Quantitative Biology. 72 (1): 251–9. doi:10.1101/sqb.2007.72.052. PMID 18419282.
  8. ↑ Godinho SI, Maywood ES, Shaw L, Tucci V, Barnard AR, Busino L, Pagano M, Kendall R, Quwailid MM, Romero MR, O'neill J, Chesham JE, Brooker D, Lalanne Z, Hastings MH, Nolan PM (May 2007). "The after-hours mutant reveals a role for Fbxl3 in determining mammalian circadian period". Science. 316 (5826): 897–900. doi:10.1126/science.1141138. PMID 17463252.
  9. ↑ Hirano A, Yumimoto K, Tsunematsu R, Matsumoto M, Oyama M, Kozuka-Hata H, Nakagawa T, Lanjakornsiripan D, Nakayama KI, Fukada Y (February 2013). "FBXL21 regulates oscillation of the circadian clock through ubiquitination and stabilization of cryptochromes". Cell. 152 (5): 1106–18. doi:10.1016/j.cell.2013.01.054. PMID 23452856.
  10. ↑ Toh KL (August 2008). "Basic science review on circadian rhythm biology and circadian sleep disorders" (PDF). Annals of the Academy of Medicine, Singapore. 37 (8): 662–8. PMID 18797559.
  11. ↑ Sato K, Yoshida K (November 2010). "Augmentation of the ubiquitin-mediated proteolytic system by F-box and additional motif-containing proteins (Review)". International Journal of Oncology. 37 (5): 1071–6. doi:10.3892/ijo_00000758. PMID 20878054.
  12. ↑ 12.0 12.1 Xing W, Busino L, Hinds TR, Marionni ST, Saifee NH, Bush MF, Pagano M, Zheng N (April 2013). "SCF(FBXL3) ubiquitin ligase targets cryptochromes at their cofactor pocket". Nature. 496 (7443): 64–8. doi:10.1038/nature11964. PMID 23503662.
  13. ↑ 13.0 13.1 13.2 Shi G, Xing L, Liu Z, Qu Z, Wu X, Dong Z, Wang X, Gao X, Huang M, Yan J, Yang L, Liu Y, Ptácek LJ, Xu Y (March 2013). "Dual roles of FBXL3 in the mammalian circadian feedback loops are important for period determination and robustness of the clock". Proceedings of the National Academy of Sciences of the United States of America. 110 (12): 4750–5. doi:10.1073/pnas.1302560110. PMID 23471982.
  14. ↑ 14.0 14.1 14.2 Huber AL, Papp SJ, Chan AB, Henriksson E, Jordan SD, Kriebs A, Nguyen M, Wallace M, Li Z, Metallo CM, Lamia KA (November 2016). "CRY2 and FBXL3 Cooperatively Degrade c-MYC". Molecular Cell. 64 (4): 774–789. doi:10.1016/j.molcel.2016.10.012. PMID 27840026.
  15. ↑ Cenciarelli C, Chiaur DS, Guardavaccaro D, Parks W, Vidal M, Pagano M (October 1999). "Identification of a family of human F-box proteins". Current Biology. 9 (20): 1177–9. doi:10.1016/S0960-9822(00)80020-2. PMID 10531035.
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