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InterPro: IPR002344 Lupus La protein
Protein matches
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UniProtKB Matches: 292 proteins |
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Accession
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IPR002344 Lupus_La |
Type
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Family |
Signatures
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InterPro Relationships
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Contains
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IPR000504 RNA recognition motif, RNP-1
IPR006630 RNA-binding protein Lupus La
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GO Term annotation
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Process
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GO:0006396 RNA processing
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Function
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GO:0003723 RNA binding
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Component
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GO:0005634 nucleus
GO:0030529 ribonucleoprotein complex
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InterPro annotation
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Entry Details in BioMart
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Abstract
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The La protein is a 47 kDa polypeptide that often acts as an autoantigen in systemic lupus erythematosus and Sjogren's syndrome patients [1]. It occurs in both the nucleus and the cytoplasm, where it takes on different roles [2]. In the nucleus, La facilitates the production of tRNAs, acting as a RNA polymerase III (RNAP III) transcription factor by binding to the U-rich 3'UTR of nascent transcripts, assisting in their folding and maturation [3]. In the cytoplasm, La facilitates the translation of specific mRNAs, acting as a translation factor. As a RNA binding protein (RBP), La associates with subsets of mRNAs that contain a 5'-terminal oligopyrimidine (5'TOP) motif known to control protein synthesis. The binding of La to specific classes of RNA molecules regulates their downstream processing, protects them from endonuclease digestion, and organises their export from the nucleus [4, 5, 6, 7].
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Structural links
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Database links
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Publications
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1.
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Izumi RE, Das S, Barat B, Raychaudhuri S, Dasgupta A.
A peptide from autoantigen La blocks poliovirus and hepatitis C virus cap-independent translation and reveals a single tyrosine critical for La RNA binding and translation stimulation.
J. Virol. 78 3763-76 2004
[PubMed: 15016896]
http://dx.doi.org/10.1128/JVI.78.7.3763-3776.2004
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2.
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Intine RV, Tenenbaum SA, Sakulich AL, Keene JD, Maraia RJ.
Differential phosphorylation and subcellular localization of La RNPs associated with precursor tRNAs and translation-related mRNAs.
Mol. Cell 12 1301-7 2003
[PubMed: 14636586]
http://dx.doi.org/10.1016/S1097-2765(03)00429-5
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3.
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Alfano C, Sanfelice D, Babon J, Kelly G, Jacks A, Curry S, Conte MR.
Structural analysis of cooperative RNA binding by the La motif and central RRM domain of human La protein.
Nat. Struct. Mol. Biol. 11 323-9 2004
[PubMed: 15004549]
http://dx.doi.org/10.1038/nsmb747
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4.
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Keene JD.
Posttranscriptional generation of macromolecular complexes.
Mol. Cell 12 1347-9 2003
[PubMed: 14690589]
http://dx.doi.org/10.1016/S1097-2765(03)00496-9
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5.
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Keene JD, Tenenbaum SA.
Eukaryotic mRNPs may represent posttranscriptional operons.
Mol. Cell 9 1161-7 2002
[PubMed: 12086614]
http://dx.doi.org/10.1016/S1097-2765(02)00559-2
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6.
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Keene JD.
Organizing mRNA export.
Nat. Genet. 33 111-2 2003
[PubMed: 12560814]
http://dx.doi.org/10.1038/ng0203-111
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7.
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Keene JD.
Ribonucleoprotein infrastructure regulating the flow of genetic information between the genome and the proteome.
Proc. Natl. Acad. Sci. U.S.A. 98 7018-24 2001
[PubMed: 11416181]
http://dx.doi.org/10.1073/pnas.111145598
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Additional Reading
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Pruijn GJ, Slobbe RL, Van Venrooij WJ.
Structure and function of La and Ro RNPs.
Mol. Biol. Rep. 14 1990 43-8
[PubMed: 2194109]
http://dx.doi.org/10.1007/BF00360410
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Jacks A, Babon J, Kelly G, Manolaridis I, Cary PD, Curry S, Conte MR.
Structure of the C-terminal domain of human La protein reveals a novel RNA recognition motif coupled to a helical nuclear retention element.
Structure 11 2003 833-43
[PubMed: 12842046]
http://dx.doi.org/10.1016/S0969-2126(03)00121-7
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Kotik-Kogan O, Valentine ER, Sanfelice D, Conte MR, Curry S.
Structural analysis reveals conformational plasticity in the recognition of RNA 3' ends by the human La protein.
Structure 16 2008 852-62
[PubMed: 18547518]
http://dx.doi.org/10.1016/j.str.2008.02.021
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Dong G, Chakshusmathi G, Wolin SL, Reinisch KM.
Structure of the La motif: a winged helix domain mediates RNA binding via a conserved aromatic patch.
EMBO J. 23 2004 1000-7
[PubMed: 14976553]
http://dx.doi.org/10.1038/sj.emboj.7600115
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Teplova M, Yuan YR, Phan AT, Malinina L, Ilin S, Teplov A, Patel DJ.
Structural basis for recognition and sequestration of UUU(OH) 3' temini of nascent RNA polymerase III transcripts by La, a rheumatic disease autoantigen.
Mol. Cell 21 2006 75-85
[PubMed: 16387655]
http://dx.doi.org/10.1016/j.molcel.2005.10.027
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InterPro 23.1
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