BTRC (遺伝子)

BTRC
PDBに登録されている構造
PDB	オルソログ検索: RCSB PDBe PDBj
PDBのIDコード一覧
	1P22, 2P64
識別子
記号	BTRC, BETA-TRCP, FBW1A, FBXW1, FBXW1A, FWD1, bTrCP, bTrCP1, betaTrCP, beta-transducin repeat containing E3 ubiquitin protein ligase
外部ID	OMIM: 603482 MGI: 1338871 HomoloGene: 39330 GeneCards: BTRC
遺伝子の位置 (ヒト)
染色体	10番染色体 (ヒト)
終点	101,557,321 bp
遺伝子の位置 (マウス)
染色体	19番染色体 (マウス)
終点	45,518,452 bp
遺伝子オントロジー
分子機能	• 血漿タンパク結合; • ligase activity; • protein phosphorylated amino acid binding; • protein dimerization activity; • beta-catenin binding; • ubiquitin protein ligase activity; • ubiquitin-protein transferase activity; • snoRNA binding;
細胞の構成要素	• 細胞核; • 細胞質; • 核質; • 細胞質基質; • SCF複合体; • small-subunit processome; • Pwp2p-containing subcomplex of 90S preribosome;
生物学的プロセス	• cellular response to organic cyclic compound; • protein destabilization; • regulation of cell cycle; • タンパク質異化プロセス; • G2/M transition of mitotic cell cycle; • negative regulation of DNA-binding transcription factor activity; • regulation of I-kappaB kinase/NF-kappaB signaling; • stress-activated MAPK cascade; • negative regulation of transcription, DNA-templated; • positive regulation of proteolysis; • regulation of proteasomal protein catabolic process; • regulation of circadian rhythm; • mammary gland epithelial cell proliferation; • branching involved in mammary gland duct morphogenesis; • negative regulation of smoothened signaling pathway; • 周期的プロセス; • NIK/NF-kappaB signaling; • シグナル伝達; • ubiquitin-dependent protein catabolic process; • regulation of canonical Wnt signaling pathway; • protein dephosphorylation; • positive regulation of transcription, DNA-templated; • protein ubiquitination; • positive regulation of circadian rhythm; • Wntシグナル経路; • protein polyubiquitination; • viral process; • 翻訳後修飾; • SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; • interleukin-1-mediated signaling pathway; • proteasome-mediated ubiquitin-dependent protein catabolic process; • maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); • regulation of mitotic cell cycle phase transition; • stimulatory C-type lectin receptor signaling pathway; • Fc-epsilon receptor signaling pathway; • T cell receptor signaling pathway;
	出典:Amigo / QuickGO
オルソログ
	8945
	12234
	ENSG00000166167
	ENSMUSG00000025217
	Q9Y297,Q5T1W7
	Q3ULA2
	NM_001256856; NM_003939; NM_033637
NM_001037758; NM_001286465; NM_001286466; NM_009771; NM_001360120;
	NM_001360122; NM_001360124; NM_001360126; NM_001360127
	NP_001243785; NP_003930; NP_378663
NP_001032847; NP_001273394; NP_001273395; NP_033901; NP_001347049;
	NP_001347051; NP_001347053; NP_001347055; NP_001347056
	ウィキデータ
閲覧/編集ヒト	閲覧/編集マウス

BTRC（β-transducin repeat containing）は、βTrCP1、FBXW1A（F-box/WD repeat-containing protein 1A）、FBXW1、pIκBα-E3 receptor subunitといった名称で知られるタンパク質をコードするヒトの遺伝子である^[5]^[6]。

この遺伝子はF-boxタンパク質ファミリーのメンバーをコードする。F-boxタンパク質はF-boxと呼ばれる約40残基の構造モチーフによって特徴づけられる。F-boxタンパク質はSCF複合体と呼ばれるユビキチンリガーゼ複合体の4つのサブユニットのうちの1つを構成し、常にではないものの多くの場合、リン酸化依存的に基質を認識する。F-boxタンパク質は3つのクラスに分類される。

Fbxw: WD40リピートを含む
Fbxl: ロイシンリッチリピートを含む
Fbxo: 他のタンパク質間相互作用モジュールを含む、または明確なモチーフが存在しない

この遺伝子にコードされるタンパク質はFbxwに属し、F-boxに加えて複数のWD40リピートを含む。このタンパク質はツメガエルのβTrCP、酵母のMet30、アカパンカビのScon2、ショウジョウバエのSlimbと相同である。哺乳類ではβTrCP1に加えて、βTrCP2またはFBXW11と呼ばれるパラログタンパク質が存在するが、これまでのところ両者の機能は冗長的であり区別できないようである。

発見

ヒトのβTrCP（βTrCP1とβTrCP2の双方を指す）は、HIV-1のVpuタンパク質が細胞のCD4をタンパク質分解装置と結び付けて除去する際に結合するユビキチンリガーゼとして同定された^[7]。その後、βTrCPはさまざまな標的の分解を媒介することで複数の細胞過程を調節することが示された^[8]。細胞周期の調節因子はβTrCPの基質の主要なグループを構成している。S期の間、βTrCPはホスファターゼCDC25A（英語版）の分解を促進することでCDK1を抑制しているが^[9]、G₂期にはキナーゼWEE1（英語版）を分解の標的とすることでCDK1の活性化に寄与する^[10]。有糸分裂の序盤には、βTrCPはAPC/Cユビキチンリガーゼ複合体の阻害因子であるEMI1（英語版）の分解を媒介する^[11]^[12]。APC/Cは中期から後期への移行（セキュリンの分解の誘導によって）と有糸分裂の終結（CDK1を活性化するサイクリンサブユニットの分解の駆動によって）を担う。さらに、βTrCPはRESTを標的とし、MAD2の転写抑制を解除する。MAD2はすべての染色分体が紡錘体の微小管に接着するまでAPC/Cを不活性化状態に維持する、紡錘体チェックポイントの必須の構成要素であり、βTrCPはこのようにAPC/Cを制御する^[13]。

機能

βTrCPは細胞周期チェックポイントの調節に重要な役割を果たす。βTrCPは遺伝毒性ストレスに応答して、Chk1とともにCDC25Aの分解を媒介することでCDK1活性の低下に寄与し^[9]^[14]、DNA修復が完了するまで細胞周期の進行を防ぐ。DNA複製やDNA損傷からの回復の間、βTrCPはPLK1依存的にクラスピン（英語版）を標的とする^[15]^[16]^[17]。

βTrCPはタンパク質の翻訳、細胞成長や生存過程においてもにおける重要な因子であることが判明している。分裂促進因子に対する応答として、翻訳開始因子eIF4Aの阻害因子であるPDCD4（英語版）はβTrCPとS6K1（英語版）依存的に迅速に分解され、効率的な翻訳と細胞成長が行われる^[18]。タンパク質の翻訳に関与する他の標的としてはeEF2Kがある。eEF2Kは翻訳伸長因子eEF2をリン酸化してリボソームへの親和性を低下させる^[19]。また、βTrCPはmTORやCK1α（英語版）と協働してmTORの阻害因子であるDEPTORの分解を誘導し、mTORの完全な活性化を促進する自己増幅ループを作り出す^[20]^[21]^[22]。同時に、βTrCPはアポトーシス促進タンパク質BimELの分解を媒介し、細胞生存を促進する^[23]。

βTrCPはリン酸化されたIκBα（英語版）とβ-カテニンの分解モチーフと結合し、おそらくNF-κBとWnt経路を調節することで複数の転写プログラムで機能している^[24]^[25]。βTrCPは中心小体のdisengagement（解離）とlicensing（複製ライセンス化）を調節することが示されている。βTrCPは前中期にintercentrosomal linker protein（中心体間リンカータンパク質）CEP68（英語版）を標的とし、中心小体のdisengagementとその後のseparation（分離）に寄与する^[26]。

相互作用

βTrCPは次に挙げる因子と相互作用することが示されている。

臨床的意義

βTrCPは一部の組織ではがんタンパク質としてふるまう。βTrCPの発現レベルの上昇は、大腸がん^[39]、膵臓がん^[40]、肝芽腫^[41]、そして乳がん^[42]でみられる。

出典

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000166167 - Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000025217 - Ensembl, May 2017
^ Human PubMed Reference:
^ Mouse PubMed Reference:
^ “The BTRC gene, encoding a human F-box/WD40-repeat protein, maps to chromosome 10q24-q25”. Genomics 58 (1): 104–5. (May 1999). doi:10.1006/geno.1999.5792. PMID 10331953.
^ “Entrez Gene: BTRC beta-transducin repeat containing”. 2020年12月20日閲覧。
^ ^a ^b “A novel human WD protein, h-beta TrCp, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif”. Molecular Cell 1 (4): 565–74. (March 1998). doi:10.1016/S1097-2765(00)80056-8. PMID 9660940.
^ “Deregulated proteolysis by the F-box proteins SKP2 and beta-TrCP: tipping the scales of cancer”. Nature Reviews. Cancer 8 (6): 438–49. (June 2008). doi:10.1038/nrc2396. PMC 2711846. PMID 18500245.
^ ^a ^b ^c “Degradation of Cdc25A by beta-TrCP during S phase and in response to DNA damage”. Nature 426 (6962): 87–91. (November 2003). Bibcode: 2003Natur.426...87B. doi:10.1038/nature02082. PMID 14603323.
^ ^a ^b “M-phase kinases induce phospho-dependent ubiquitination of somatic Wee1 by SCFbeta-TrCP”. Proceedings of the National Academy of Sciences of the United States of America 101 (13): 4419–24. (March 2004). Bibcode: 2004PNAS..101.4419W. doi:10.1073/pnas.0307700101. PMC 384762. PMID 15070733.
^ ^a ^b ^c “Control of meiotic and mitotic progression by the F box protein beta-Trcp1 in vivo”. Developmental Cell 4 (6): 799–812. (June 2003). doi:10.1016/S1534-5807(03)00154-0. PMID 12791266.
^ ^a ^b “Prophase destruction of Emi1 by the SCF(betaTrCP/Slimb) ubiquitin ligase activates the anaphase promoting complex to allow progression beyond prometaphase”. Developmental Cell 4 (6): 813–26. (June 2003). doi:10.1016/S1534-5807(03)00153-9. PMID 12791267.
^ “Control of chromosome stability by the beta-TrCP-REST-Mad2 axis”. Nature 452 (7185): 365–9. (March 2008). Bibcode: 2008Natur.452..365G. doi:10.1038/nature06641. PMC 2707768. PMID 18354482.
^ ^a ^b “SCFbeta-TRCP links Chk1 signaling to degradation of the Cdc25A protein phosphatase”. Genes & Development 17 (24): 3062–74. (December 2003). doi:10.1101/gad.1157503. PMC 305258. PMID 14681206.
^ ^a ^b “SCFbetaTrCP-mediated degradation of Claspin regulates recovery from the DNA replication checkpoint response”. Molecular Cell 23 (3): 319–29. (August 2006). doi:10.1016/j.molcel.2006.06.013. PMID 16885022.
^ ^a ^b “Destruction of Claspin by SCFbetaTrCP restrains Chk1 activation and facilitates recovery from genotoxic stress”. Molecular Cell 23 (3): 307–18. (August 2006). doi:10.1016/j.molcel.2006.06.016. PMID 16885021.
^ ^a ^b “Polo-like kinase-1 controls proteasome-dependent degradation of Claspin during checkpoint recovery”. Current Biology 16 (19): 1950–5. (October 2006). doi:10.1016/j.cub.2006.08.026. PMID 16934469.
^ ^a ^b “S6K1- and betaTRCP-mediated degradation of PDCD4 promotes protein translation and cell growth”. Science 314 (5798): 467–71. (October 2006). Bibcode: 2006Sci...314..467D. doi:10.1126/science.1130276. PMID 17053147.
^ Kruiswijk, Flore; Yuniati, Laurensia; Magliozzi, Roberto; Low, Teck Yew; Lim, Ratna; Bolder, Renske; Mohammed, Shabaz; Proud, Christopher G. et al. (2012-06-05). “Coupled activation and degradation of eEF2K regulates protein synthesis in response to genotoxic stress”. Science Signaling 5 (227): ra40. doi:10.1126/scisignal.2002718. ISSN 1937-9145. PMC 3812825. PMID 22669845.
^ ^a ^b “mTOR generates an auto-amplification loop by triggering the βTrCP- and CK1α-dependent degradation of DEPTOR”. Molecular Cell 44 (2): 317–24. (October 2011). doi:10.1016/j.molcel.2011.09.005. PMC 3212871. PMID 22017877.
^ ^a ^b “DEPTOR, an mTOR inhibitor, is a physiological substrate of SCF(βTrCP) E3 ubiquitin ligase and regulates survival and autophagy”. Molecular Cell 44 (2): 304–16. (October 2011). doi:10.1016/j.molcel.2011.08.029. PMC 3216641. PMID 22017876.
^ ^a ^b “mTOR drives its own activation via SCF(βTrCP)-dependent degradation of the mTOR inhibitor DEPTOR”. Molecular Cell 44 (2): 290–303. (October 2011). doi:10.1016/j.molcel.2011.08.030. PMC 3229299. PMID 22017875.
^ ^a ^b “betaTrCP- and Rsk1/2-mediated degradation of BimEL inhibits apoptosis”. Molecular Cell 33 (1): 109–16. (January 2009). doi:10.1016/j.molcel.2008.12.020. PMC 2655121. PMID 19150432.
^ “The SCFbeta-TRCP-ubiquitin ligase complex associates specifically with phosphorylated destruction motifs in IkappaBalpha and beta-catenin and stimulates IkappaBalpha ubiquitination in vitro”. Genes & Development 13 (3): 270–83. (February 1999). doi:10.1101/gad.13.3.270. PMC 316433. PMID 9990852.
^ ^a ^b “The human F box protein beta-Trcp associates with the Cul1/Skp1 complex and regulates the stability of beta-catenin”. Oncogene 18 (4): 849–54. (January 1999). doi:10.1038/sj.onc.1202653. PMID 10023660.
^ Pagan, Julia K.; Marzio, Antonio; Jones, Mathew J. K.; Saraf, Anita; Jallepalli, Prasad V.; Florens, Laurence; Washburn, Michael P.; Pagano, Michele (2015-01). “Degradation of Cep68 and PCNT cleavage mediate Cep215 removal from the PCM to allow centriole separation, disengagement and licensing”. Nature Cell Biology 17 (1): 31–43. doi:10.1038/ncb3076. ISSN 1476-4679. PMC 4415623. PMID 25503564.
^ ^a ^b ^c “Identification of a family of human F-box proteins”. Current Biology 9 (20): 1177–9. (October 1999). doi:10.1016/S0960-9822(00)80020-2. PMID 10531035.
^ “CK2-dependent phosphorylation of the E2 ubiquitin conjugating enzyme UBC3B induces its interaction with beta-TrCP and enhances beta-catenin degradation”. Oncogene 21 (25): 3978–87. (June 2002). doi:10.1038/sj.onc.1205574. PMID 12037680.
^ “beta-Trcp couples beta-catenin phosphorylation-degradation and regulates Xenopus axis formation”. Proceedings of the National Academy of Sciences of the United States of America 96 (11): 6273–8. (May 1999). doi:10.1073/pnas.96.11.6273. PMC 26871. PMID 10339577.
^ ^a ^b ^c ^d “Homodimer of two F-box proteins betaTrCP1 or betaTrCP2 binds to IkappaBalpha for signal-dependent ubiquitination”. The Journal of Biological Chemistry 275 (4): 2877–84. (January 2000). doi:10.1074/jbc.275.4.2877. PMID 10644755.
^ ^a ^b “TIP120A associates with cullins and modulates ubiquitin ligase activity”. The Journal of Biological Chemistry 278 (18): 15905–10. (May 2003). doi:10.1074/jbc.M213070200. PMID 12609982.
^ “Regulation of the discs large tumor suppressor by a phosphorylation-dependent interaction with the beta-TrCP ubiquitin ligase receptor”. The Journal of Biological Chemistry 278 (43): 42477–86. (October 2003). doi:10.1074/jbc.M302799200. PMID 12902344.
^ ^a ^b “Signal-induced ubiquitination of IkappaBalpha by the F-box protein Slimb/beta-TrCP”. Genes & Development 13 (3): 284–94. (February 1999). doi:10.1101/gad.13.3.284. PMC 316434. PMID 9990853.
^ “Genetic evidence for the essential role of beta-transducin repeat-containing protein in the inducible processing of NF-kappa B2/p100”. The Journal of Biological Chemistry 277 (25): 22111–4. (June 2002). doi:10.1074/jbc.C200151200. PMID 11994270.
^ “SUMO1 modification of NF-kappaB2/p100 is essential for stimuli-induced p100 phosphorylation and processing”. EMBO Reports 9 (9): 885–90. (September 2008). doi:10.1038/embor.2008.122. PMC 2529344. PMID 18617892.
^ “SCFbeta-TRCP controls oncogenic transformation and neural differentiation through REST degradation”. Nature 452 (7185): 370–4. (March 2008). Bibcode: 2008Natur.452..370W. doi:10.1038/nature06780. PMC 2688689. PMID 18354483.
^ “SCF(beta-TRCP) and phosphorylation dependent ubiquitinationof I kappa B alpha catalyzed by Ubc3 and Ubc4”. Oncogene 19 (31): 3529–36. (July 2000). doi:10.1038/sj.onc.1203647. PMID 10918611.
^ “Molecular Interaction Database”. 2006年5月6日時点のオリジナルよりアーカイブ。2012年5月8日閲覧。
^ “Associations among beta-TrCP, an E3 ubiquitin ligase receptor, beta-catenin, and NF-kappaB in colorectal cancer”. Journal of the National Cancer Institute 96 (15): 1161–70. (August 2004). doi:10.1093/jnci/djh219. PMID 15292388.
^ “Increased expression of the E3-ubiquitin ligase receptor subunit betaTRCP1 relates to constitutive nuclear factor-kappaB activation and chemoresistance in pancreatic carcinoma cells”. Cancer Research 65 (4): 1316–24. (February 2005). doi:10.1158/0008-5472.CAN-04-1626. PMID 15735017.
^ “Elevated expression of Wnt antagonists is a common event in hepatoblastomas”. Clinical Cancer Research 11 (12): 4295–304. (June 2005). doi:10.1158/1078-0432.CCR-04-1162. PMID 15958610.
^ “Induction of homologue of Slimb ubiquitin ligase receptor by mitogen signaling”. The Journal of Biological Chemistry 277 (39): 36624–30. (September 2002). doi:10.1074/jbc.M204524200. PMID 12151397.

外部リンク

Human BTRC genome location and BTRC gene details page in the UCSC Genome Browser.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000166167 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000025217 - Ensembl, May 2017

[3] Human PubMed Reference:

[4] Mouse PubMed Reference:

[pmid10331953-5] “The BTRC gene, encoding a human F-box/WD40-repeat protein, maps to chromosome 10q24-q25”. Genomics 58 (1): 104–5. (May 1999). doi:10.1006/geno.1999.5792. PMID 10331953.

[entrez-6] “Entrez Gene: BTRC beta-transducin repeat containing”. 2020年12月20日閲覧。

[Margottin,_F._et_al.-7] “A novel human WD protein, h-beta TrCp, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif”. Molecular Cell 1 (4): 565–74. (March 1998). doi:10.1016/S1097-2765(00)80056-8. PMID 9660940.

[Frescas,_D._&_Pagano,_M.-8] “Deregulated proteolysis by the F-box proteins SKP2 and beta-TrCP: tipping the scales of cancer”. Nature Reviews. Cancer 8 (6): 438–49. (June 2008). doi:10.1038/nrc2396. PMC 2711846. PMID 18500245.

[Busino,_L._et_al.-9] “Degradation of Cdc25A by beta-TrCP during S phase and in response to DNA damage”. Nature 426 (6962): 87–91. (November 2003). Bibcode: 2003Natur.426...87B. doi:10.1038/nature02082. PMID 14603323.

[Watanabe,_N._et_al.-10] “M-phase kinases induce phospho-dependent ubiquitination of somatic Wee1 by SCFbeta-TrCP”. Proceedings of the National Academy of Sciences of the United States of America 101 (13): 4419–24. (March 2004). Bibcode: 2004PNAS..101.4419W. doi:10.1073/pnas.0307700101. PMC 384762. PMID 15070733.

[Guardavaccaro,_D._et_al.-11] “Control of meiotic and mitotic progression by the F box protein beta-Trcp1 in vivo”. Developmental Cell 4 (6): 799–812. (June 2003). doi:10.1016/S1534-5807(03)00154-0. PMID 12791266.

[Margottin-Goguet,_F._et_al.-12] “Prophase destruction of Emi1 by the SCF(betaTrCP/Slimb) ubiquitin ligase activates the anaphase promoting complex to allow progression beyond prometaphase”. Developmental Cell 4 (6): 813–26. (June 2003). doi:10.1016/S1534-5807(03)00153-9. PMID 12791267.

[Guardavaccaro,_D.,_Frescas,_D._et_al.-13] “Control of chromosome stability by the beta-TrCP-REST-Mad2 axis”. Nature 452 (7185): 365–9. (March 2008). Bibcode: 2008Natur.452..365G. doi:10.1038/nature06641. PMC 2707768. PMID 18354482.

[Jin,_J._et_al.-14] “SCFbeta-TRCP links Chk1 signaling to degradation of the Cdc25A protein phosphatase”. Genes & Development 17 (24): 3062–74. (December 2003). doi:10.1101/gad.1157503. PMC 305258. PMID 14681206.

[Peschiaroli,_A._et_al.-15] “SCFbetaTrCP-mediated degradation of Claspin regulates recovery from the DNA replication checkpoint response”. Molecular Cell 23 (3): 319–29. (August 2006). doi:10.1016/j.molcel.2006.06.013. PMID 16885022.

[Mailand,_N.,_Bekker-Jensen,_S.,_Bartek,_J._&_Lukas,_J.-16] “Destruction of Claspin by SCFbetaTrCP restrains Chk1 activation and facilitates recovery from genotoxic stress”. Molecular Cell 23 (3): 307–18. (August 2006). doi:10.1016/j.molcel.2006.06.016. PMID 16885021.

[Mamely,_I._et_al.-17] “Polo-like kinase-1 controls proteasome-dependent degradation of Claspin during checkpoint recovery”. Current Biology 16 (19): 1950–5. (October 2006). doi:10.1016/j.cub.2006.08.026. PMID 16934469.

[Dorrello,_N.V._et_al.-18] “S6K1- and betaTRCP-mediated degradation of PDCD4 promotes protein translation and cell growth”. Science 314 (5798): 467–71. (October 2006). Bibcode: 2006Sci...314..467D. doi:10.1126/science.1130276. PMID 17053147.

[:0-19] Kruiswijk, Flore; Yuniati, Laurensia; Magliozzi, Roberto; Low, Teck Yew; Lim, Ratna; Bolder, Renske; Mohammed, Shabaz; Proud, Christopher G. et al. (2012-06-05). “Coupled activation and degradation of eEF2K regulates protein synthesis in response to genotoxic stress”. Science Signaling 5 (227): ra40. doi:10.1126/scisignal.2002718. ISSN 1937-9145. PMC 3812825. PMID 22669845.

[Duan,_S._et_al.-20] “mTOR generates an auto-amplification loop by triggering the βTrCP- and CK1α-dependent degradation of DEPTOR”. Molecular Cell 44 (2): 317–24. (October 2011). doi:10.1016/j.molcel.2011.09.005. PMC 3212871. PMID 22017877.

[Zhao,_Y.,_Xiong,_X._&_Sun,_Y.-21] “DEPTOR, an mTOR inhibitor, is a physiological substrate of SCF(βTrCP) E3 ubiquitin ligase and regulates survival and autophagy”. Molecular Cell 44 (2): 304–16. (October 2011). doi:10.1016/j.molcel.2011.08.029. PMC 3216641. PMID 22017876.

[Gao,_D._et_al.-22] “mTOR drives its own activation via SCF(βTrCP)-dependent degradation of the mTOR inhibitor DEPTOR”. Molecular Cell 44 (2): 290–303. (October 2011). doi:10.1016/j.molcel.2011.08.030. PMC 3229299. PMID 22017875.

[Dehan,_E._et_al.-23] “betaTrCP- and Rsk1/2-mediated degradation of BimEL inhibits apoptosis”. Molecular Cell 33 (1): 109–16. (January 2009). doi:10.1016/j.molcel.2008.12.020. PMC 2655121. PMID 19150432.

[Winston,_J.T._et_al.-24] “The SCFbeta-TRCP-ubiquitin ligase complex associates specifically with phosphorylated destruction motifs in IkappaBalpha and beta-catenin and stimulates IkappaBalpha ubiquitination in vitro”. Genes & Development 13 (3): 270–83. (February 1999). doi:10.1101/gad.13.3.270. PMC 316433. PMID 9990852.

[Latres,_E.,_Chiaur,_D.S._&_Pagano,_M.-25] “The human F box protein beta-Trcp associates with the Cul1/Skp1 complex and regulates the stability of beta-catenin”. Oncogene 18 (4): 849–54. (January 1999). doi:10.1038/sj.onc.1202653. PMID 10023660.

[:1-26] Pagan, Julia K.; Marzio, Antonio; Jones, Mathew J. K.; Saraf, Anita; Jallepalli, Prasad V.; Florens, Laurence; Washburn, Michael P.; Pagano, Michele (2015-01). “Degradation of Cep68 and PCNT cleavage mediate Cep215 removal from the PCM to allow centriole separation, disengagement and licensing”. Nature Cell Biology 17 (1): 31–43. doi:10.1038/ncb3076. ISSN 1476-4679. PMC 4415623. PMID 25503564.

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