cd20381

Tudor domain found in Lamin-B receptor (LBR) and similar proteins

CDD entry
Member databaseCDD
CDD typedomain
Short nameTudor_LBR
SetTudor_SF

Description

LBR, also called integral nuclear envelope inner membrane (INM) protein or LMN2R, is a nuclear envelope protein that anchors the lamina and the heterochromatin to the inner nuclear membrane, in cellular senescence induced by excess thymidine. It is also important for cholesterol biosynthesis. LBR can interact with chromodomain proteins and DNA. It contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.
[5, 21, 3, 17, 12, 11, 10, 7, 19, 2, 9, 14, 20, 1, 13, 6, 16, 4, 15, 18, 8]

References

1.Lamin B receptor (LBR) is involved in the induction of cellular senescence in human cells. Arai R, En A, Takauji Y, Maki K, Miki K, Fujii M, Ayusawa D. Mech Ageing Dev 178, 25-32, (2019). PMID: 30615890

2.SRPK1 and LBR protein kinases show identical substrate specificities. Papoutsopoulou S, Nikolakaki E, Giannakouros T. Biochem Biophys Res Commun 255, 602-7, (1999). PMID: 10049757

3.Temporal control of nuclear envelope assembly by phosphorylation of lamin B receptor. Tseng LC, Chen RH. Mol Biol Cell 22, 3306-17, (2011). PMID: 21795390

4.Lamin B Receptor: Interplay between Structure, Function and Localization. Nikolakaki E, Mylonis I, Giannakouros T. Cells 6, E28, (2017). PMID: 28858257

5.An anadysplasia-like, spontaneously remitting spondylometaphyseal dysplasia secondary to lamin B receptor (LBR) gene mutations: further definition of the phenotypic heterogeneity of LBR-bone dysplasias. Sobreira N, Modaff P, Steel G, You J, Nanda S, Hoover-Fong J, Valle D, Pauli RM. Am J Med Genet A 167A, 159-63, (2015). PMID: 25348816

6.Lamin B receptor-related disorder is associated with a spectrum of skeletal dysplasia phenotypes. Thompson E, Abdalla E, Superti-Furga A, McAlister W, Kratz L, Unger S, Royer-Bertrand B, Campos-Xavier B, Mittaz-Crettol L, Amin AK, DeSanto C, Wilson DB, Douglas G, Kozel B, Shinawi M. Bone 120, 354-363, (2019). PMID: 30448303

7.Mutations in the gene encoding the lamin B receptor produce an altered nuclear morphology in granulocytes (Pelger-Huet anomaly). Hoffmann K, Dreger CK, Olins AL, Olins DE, Shultz LD, Lucke B, Karl H, Kaps R, Muller D, Vaya A, Aznar J, Ware RE, Sotelo Cruz N, Lindner TH, Herrmann H, Reis A, Sperling K. Nat Genet 31, 410-4, (2002). PMID: 12118250

8.ELYS regulates the localization of LBR by modulating its phosphorylation state. Mimura Y, Takagi M, Clever M, Imamoto N. J Cell Sci 129, 4200-4212, (2016). PMID: 27802161

9.Domain-specific interactions of human HP1-type chromodomain proteins and inner nuclear membrane protein LBR. Ye Q, Callebaut I, Pezhman A, Courvalin JC, Worman HJ. J Biol Chem 272, 14983-9, (1997). PMID: 9169472

10.Autosomal recessive HEM/Greenberg skeletal dysplasia is caused by 3 beta-hydroxysterol delta 14-reductase deficiency due to mutations in the lamin B receptor gene. Waterham HR, Koster J, Mooyer P, Noort Gv Gv, Kelley RI, Wilcox WR, Wanders RJ, Hennekam RC, Oosterwijk JC. Am J Hum Genet 72, 1013-7, (2003). PMID: 12618959

11.Lamin B-receptor mutations in Pelger-Huet anomaly. Best S, Salvati F, Kallo J, Garner C, Height S, Thein SL, Rees DC. Br J Haematol 123, 542-4, (2003). PMID: 14617022

12.The mammalian heterochromatin protein 1 binds diverse nuclear proteins through a common motif that targets the chromoshadow domain. Lechner MS, Schultz DC, Negorev D, Maul GG, Rauscher FJ 3rd. Biochem Biophys Res Commun 331, 929-37, (2005). PMID: 15882967

13.A novel case of Greenberg dysplasia and genotype-phenotype correlation analysis for LBR pathogenic variants: An instructive example of one gene-multiple phenotypes. Giorgio E, Sirchia F, Bosco M, Sobreira NLM; Baylor-Hopkins Center for Mendelian Genomics, Grosso E, Brussino A, Brusco A. Am J Med Genet A 179, 306-311, (2019). PMID: 30561119

14.Characterization of the human gene encoding LBR, an integral protein of the nuclear envelope inner membrane. Schuler E, Lin F, Worman HJ. J Biol Chem 269, 11312-7, (1994). PMID: 8157663

15.Dynamics and Structure-Function Relationships of the Lamin B Receptor (LBR). Giannios I, Chatzantonaki E, Georgatos S. PLoS One 12, e0169626, (2017). PMID: 28118363

16.The O-β-linked N-acetylglucosaminylation of the Lamin B receptor and its impact on DNA binding and phosphorylation. Smet-Nocca C, Page A, Cantrelle FX, Nikolakaki E, Landrieu I, Giannakouros T. Biochim Biophys Acta Gen Subj 1862, 825-835, (2018). PMID: 29337275

17.LBR mutation and nuclear envelope defects in a patient affected with Reynolds syndrome. Gaudy-Marqueste C, Roll P, Esteves-Vieira V, Weiller PJ, Grob JJ, Cau P, Levy N, De Sandre-Giovannoli A. J Med Genet 47, 361-70, (2010). PMID: 20522425

18.Pelger-Huet anomaly and Greenberg skeletal dysplasia: LBR-associated diseases of cholesterol metabolism. Turner EM, Schlieker C. Rare Dis 4, e1241363, (2016). PMID: 27830109

19.Inner nuclear membrane protein LBR preferentially interacts with DNA secondary structures and nucleosomal linker. Duband-Goulet I, Courvalin JC. Biochemistry 39, 6483-8, (2000). PMID: 10828963

20.Primary structure analysis and lamin B and DNA binding of human LBR, an integral protein of the nuclear envelope inner membrane. Ye Q, Worman HJ. J Biol Chem 269, 11306-11, (1994). PMID: 8157662

21.Pelger-huet anomaly and a mild skeletal phenotype secondary to mutations in LBR. Borovik L, Modaff P, Waterham HR, Krentz AD, Pauli RM. Am J Med Genet A 161A, 2066-73, (2013). PMID: 23824842

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