Einzeltreffer — DigiBib

LNX is a RING finger and PDZ domain containing protein that interacts with the cell fate determinant Numb. To investigate the function of LNX, we tested its RING finger domain for ubiquitin ligase activity. The isolated RING finger domain was able to function as an E2-dependent, E3 ubiquitin ligase in vitro and mutation of a conserved cysteine residue within the RING domain abolished its activity, indicating that LNX is the first described PDZ domain-containing member of the E3 ubiquitin ligase family. We have identified Numb as a substrate of LNX E3 activity in vitro and in vivo. In addition to the RING finger, a region of LNX, including the Numb PTB domain-binding site and the first PDZ domain, is required for Numb ubiquitylation. Expression of wild-type but not mutant LNX causes proteasome-dependent degradation of Numb and can enhance Notch signalling. These results suggest that the levels of mammalian Numb protein and therefore, by extension, the processes of asymmetric cell division and cell fate determination may be regulated by ubiquitin-dependent proteolysis.

Titel:	LNX functions as a RING type E3 ubiquitin ligase that targets the cell fate determinant Numb for ubiquitin-dependent degradation.
Autor/in / Beteiligte Person:	Nie, J ; McGill, MA ; Dermer, M ; Dho, SE ; Wolting, CD ; McGlade, CJ
Link:	Full Text Finder (Volltext)
Zeitschrift:	The EMBO journal, Jg. 21 (2002-01-15), Heft 1-2, S. 93-102
Veröffentlichung:	2024- : [London] : Nature Publishing Group ; <i>Original Publication</i>: Eynsham, Oxford, England : Published for the European Molecular Biology Organization by IRL Press, [c1982-, 2002
Medientyp:	academicJournal
ISSN:	0261-4189 (print)
DOI:	10.1093/emboj/21.1.93
Schlagwort:	Animals Binding Sites CHO Cells Carrier Proteins chemistry Carrier Proteins genetics Cell Line Cricetinae Dogs Humans Ligases genetics Membrane Proteins genetics Mice Mutagenesis, Site-Directed Nerve Tissue Proteins genetics Protein Structure, Tertiary Recombinant Fusion Proteins chemistry Recombinant Fusion Proteins genetics Recombinant Fusion Proteins metabolism Substrate Specificity Ubiquitin metabolism Ubiquitin-Protein Ligases Carrier Proteins metabolism Ligases metabolism Membrane Proteins metabolism Nerve Tissue Proteins metabolism
Sonstiges:	Nachgewiesen in: MEDLINE Sprachen: English Publication Type: Journal Article; Research Support, Non-U.S. Gov't Language: English [EMBO J] 2002 Jan 15; Vol. 21 (1-2), pp. 93-102. MeSH Terms: Carrier Proteins / metabolism ; Ligases / metabolism ; Membrane Proteins / metabolism ; Nerve Tissue Proteins / metabolism ; Animals ; Binding Sites ; CHO Cells ; Carrier Proteins / chemistry ; Carrier Proteins / genetics ; Cell Line ; Cricetinae ; Dogs ; Humans ; Ligases / genetics ; Membrane Proteins / genetics ; Mice ; Mutagenesis, Site-Directed ; Nerve Tissue Proteins / genetics ; Protein Structure, Tertiary ; Recombinant Fusion Proteins / chemistry ; Recombinant Fusion Proteins / genetics ; Recombinant Fusion Proteins / metabolism ; Substrate Specificity ; Ubiquitin / metabolism ; Ubiquitin-Protein Ligases References: Proc Natl Acad Sci U S A. 2000 Jun 6;97(12):6844-9. (PMID: 10841580) ; Mol Cell. 1999 Dec;4(6):883-91. (PMID: 10635314) ; Trends Cell Biol. 2000 Oct;10(10):429-39. (PMID: 10998601) ; Cell. 2000 Sep 1;102(5):549-52. (PMID: 11007473) ; J Cell Biol. 2000 Dec 11;151(6):1345-52. (PMID: 11121447) ; Curr Biol. 2001 Feb 20;11(4):R132-5. (PMID: 11250167) ; Annu Rev Neurosci. 2001;24:1-29. (PMID: 11283303) ; Curr Biol. 2001 Apr 3;11(7):494-501. (PMID: 11412999) ; Cell. 1989 Jul 28;58(2):349-60. (PMID: 2752427) ; Cell. 1994 Feb 11;76(3):477-91. (PMID: 8313469) ; Trends Biochem Sci. 1995 Sep;20(9):350. (PMID: 7482701) ; Nature. 1995 Oct 19;377(6550):624-7. (PMID: 7566172) ; Development. 1995 Sep;121(9):2923-36. (PMID: 7555719) ; Development. 1995 Nov;121(11):3489-94. (PMID: 8582263) ; Trends Biochem Sci. 1996 Jun;21(6):208-14. (PMID: 8744354) ; Neuron. 1996 Jul;17(1):21-6. (PMID: 8755475) ; Neuron. 1996 Jul;17(1):27-41. (PMID: 8755476) ; Neuron. 1996 Jul;17(1):43-53. (PMID: 8755477) ; Curr Opin Struct Biol. 1996 Jun;6(3):395-401. (PMID: 8804826) ; Curr Biol. 1996 Sep 1;6(9):1134-45. (PMID: 8805372) ; Proc Natl Acad Sci U S A. 1996 Oct 15;93(21):11925-32. (PMID: 8876239) ; Curr Opin Neurobiol. 1997 Feb;7(1):21-8. (PMID: 9039790) ; Development. 1997 May;124(10):1887-97. (PMID: 9169836) ; Proc Natl Acad Sci U S A. 1997 Jul 8;94(14):7204-9. (PMID: 9207069) ; Genes Dev. 1997 Sep 1;11(17):2239-49. (PMID: 9303539) ; Genes Dev. 1997 Oct 15;11(20):2701-14. (PMID: 9334332) ; Development. 1997 Dec;124(23):4857-66. (PMID: 9428422) ; J Biol Chem. 1998 Apr 10;273(15):9179-87. (PMID: 9535908) ; J Biol Chem. 1998 Apr 24;273(17):10381-8. (PMID: 9553095) ; Mol Cell Biol. 1998 Jul;18(7):3974-82. (PMID: 9632782) ; Genes Dev. 1998 Jun 15;12(12):1837-46. (PMID: 9637685) ; Mech Dev. 1998 Jul;75(1-2):117-26. (PMID: 9739121) ; Annu Rev Biochem. 1998;67:425-79. (PMID: 9759494) ; Cell. 1998 Oct 16;95(2):225-35. (PMID: 9790529) ; EMBO J. 1998 Nov 16;17(22):6541-50. (PMID: 9822599) ; Nat Struct Biol. 1998 Dec;5(12):1075-83. (PMID: 9846878) ; Trends Cell Biol. 1999 Mar;9(3):107-12. (PMID: 10201076) ; Science. 1999 Apr 30;284(5415):770-6. (PMID: 10221902) ; Science. 1999 Apr 23;284(5414):601, 603-4. (PMID: 10328744) ; Neuron. 1999 May;23(1):71-81. (PMID: 10402194) ; Proc Natl Acad Sci U S A. 1999 Sep 28;96(20):11364-9. (PMID: 10500182) ; Science. 1999 Oct 8;286(5438):309-12. (PMID: 10514377) ; J Biol Chem. 1999 Nov 12;274(46):33097-104. (PMID: 10551880) ; J Membr Biol. 2000 Jul 1;176(1):1-17. (PMID: 10882424) Substance Nomenclature: 0 (Carrier Proteins) ; 0 (Membrane Proteins) ; 0 (Nerve Tissue Proteins) ; 0 (Numb protein, mouse) ; 0 (Recombinant Fusion Proteins) ; 0 (Ubiquitin) ; EC 2.3.2.27 (LNX1 protein, human) ; EC 2.3.2.27 (Lnx1 protein, mouse) ; EC 2.3.2.27 (Ubiquitin-Protein Ligases) ; EC 6.- (Ligases) Entry Date(s): Date Created: 20020110 Date Completed: 20020226 Latest Revision: 20221227 Update Code: 20231215 PubMed Central ID: PMC125803

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LNX functions as a RING type E3 ubiquitin ligase that targets the cell fate determinant Numb for ubiquitin-dependent degradation.