All LARP proteins, including human LARP, contain 2 conserved regions. The first conserved region shares homology with La proteins (called the La motif, see SSB) whereas the second conserved region (called the LA- motif) is restricted to LARP proteins. Mouse Larp1 is expressed in dorsal root ganglia and spinal cord, as well as in developing organs characterized by epithelial-mesenchymal interactions.[2]
LARP-1 binds a specific type of mRNA called TOP mRNAs.These TOP mRNAs are so-called because they bear a 5'TOP (Terminal oligopyrimidine) motif.. LARP-1 also appears to down-regulate the Ras-MAPK pathway. LARP-1 protein colocalizes with P bodies, which function in RNA degradation. We suggest that LARP-1 functions in P-bodies to attenuate the abundance of conserved Ras-MAPK mRNAs. The cluster of LARP-1 homologs may function to control the expression of key developmental regulators.[4]
References
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↑ 2.02.12.2Chauvet S, Maurel-Zaffran C, Miassod R, Jullien N, Pradel J, Aragnol D (Aug 2000). "dlarp, a new candidate Hox target in Drosophila whose orthologue in mouse is expressed at sites of epithelium/mesenchymal interactions". Dev Dyn. 218 (3): 401–13. doi:10.1002/1097-0177(200007)218:3<401::AID-DVDY1009>3.0.CO;2-6. PMID10878606.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID14702039.
Horke S, Reumann K, Schweizer M, et al. (2004). "Nuclear trafficking of La protein depends on a newly identified nucleolar localization signal and the ability to bind RNA". J. Biol. Chem. 279 (25): 26563–70. doi:10.1074/jbc.M401017200. PMID15060081.
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