RNA-binding protein that regulates the translation of specific target mRNA species downstream of the mTORC1 complex, in function of growth signals and nutrient availability (   ). Interacts on the one hand with the 3' poly-A tails that are present in all mRNA molecules, and on the other hand with the 7-methylguanosine cap structure of mRNAs containing a 5' terminal oligopyrimidine (5'TOP) motif, which is present in mRNAs encoding ribosomal proteins and several components of the translation machinery (  , ). The interaction with the 5' end of mRNAs containing a 5'TOP motif leads to translational repression by preventing the binding of EIF4G1 ( , ). When mTORC1 is activated, LARP1 is phosphorylated and dissociates from the 5' untranslated region (UTR) of mRNA (, ). Does not prevent binding of EIF4G1 to mRNAs that lack a 5'TOP motif . Interacts with the free 40S ribosome subunit and with ribosomes, both monosomes and polysomes ( , ). Under normal nutrient availability, interacts primarily with the 3' untranslated region (UTR) of mRNAs encoding ribosomal proteins and increases protein synthesis (, ). Associates with actively translating ribosomes and stimulates translation of mRNAs containing a 5'TOP motif, thereby regulating protein synthesis, and as a consequence, cell growth and proliferation (, ). Stabilizes mRNAs species with a 5'TOP motif, which is required to prevent apoptosis ( , ).
(Microbial infection) Positively regulates the replication of dengue virus (DENV).
Subcellular locations: Cytoplasm, Cytoplasmic granule
Colocalizes with RPTOR and PABPC1 in cytoplasmic granules that resemble stress granules.