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'''La-related protein 1''' is a [[protein]] that in humans is encoded by the ''LARP1'' [[gene]].<ref name="pmid9872452">{{cite journal |vauthors=Nagase T, Ishikawa K, Suyama M, Kikuno R, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O | title = Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro | journal = DNA Res | volume = 5 | issue = 5 | pages = 277–86 |date=Apr 1999 | pmid = 9872452 | pmc =  | doi =10.1093/dnares/5.5.277 }}</ref><ref name="pmid10878606">{{cite journal |vauthors=Chauvet S, Maurel-Zaffran C, Miassod R, Jullien N, Pradel J, Aragnol D | title = dlarp, a new candidate Hox target in Drosophila whose orthologue in mouse is expressed at sites of epithelium/mesenchymal interactions | journal = Dev Dyn | volume = 218 | issue = 3 | pages = 401–13 |date=Aug 2000 | pmid = 10878606 | pmc =  | doi = 10.1002/1097-0177(200007)218:3<401::AID-DVDY1009>3.0.CO;2-6 }}</ref><ref name="pmid9872452" /><ref name="entrez">{{cite web | title = Entrez Gene: LARP1 La ribonucleoprotein domain family, member 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23367| accessdate = }}</ref><ref name="pmid10878606" />
'''La-related protein 1 (LARP1)''' is a 150 kDa [[protein]] that in humans is encoded by the ''LARP1'' [[gene]].<ref name="pmid9872452">{{cite journal | vauthors = Nagase T, Ishikawa K, Suyama M, Kikuno R, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O | title = Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro | journal = DNA Research | volume = 5 | issue = 5 | pages = 277–86 | date = October 1998 | pmid = 9872452 | pmc =  | doi = 10.1093/dnares/5.5.277 }}</ref><ref name="pmid10878606">{{cite journal | vauthors = Chauvet S, Maurel-Zaffran C, Miassod R, Jullien N, Pradel J, Aragnol D | title = dlarp, a new candidate Hox target in Drosophila whose orthologue in mouse is expressed at sites of epithelium/mesenchymal interactions | journal = Developmental Dynamics | volume = 218 | issue = 3 | pages = 401–13 | date = July 2000 | pmid = 10878606 | pmc =  | doi = 10.1002/1097-0177(200007)218:3<401::AID-DVDY1009>3.0.CO;2-6 }}</ref><ref name="pmid9872452" /><ref name="entrez">{{cite web | title = Entrez Gene: LARP1 La ribonucleoprotein domain family, member 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23367| access-date = }}</ref><ref name="pmid10878606" /> LARP1 is a novel target of the mammalian target of rapamycin complex 1 (mTORC1) signaling pathway, a circuitry often hyperactivated in cancer which regulates cell growth and proliferation primarily through the regulation of protein synthesis.


== Function ==
== Function ==


All LARP proteins, including human LARP, contain 2 conserved regions. The first conserved region shares homology with La proteins (called the La motif, see [[Sjogren syndrome antigen B|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.<ref name="pmid10878606" />
LARP1 is the largest of a 7 member family of LARP proteins (others are: LARP1B, LARP3 (aka genuine La or SSB), LARP4A, LARP4B, LARP6 and LARP7).<ref>{{cite journal | vauthors = Bousquet-Antonelli C, Deragon JM | title = A comprehensive analysis of the La-motif protein superfamily | journal = RNA | volume = 15 | issue = 5 | pages = 750–64 | date = May 2009 | pmid = 19299548 | pmc = 2673062 | doi = 10.1261/rna.1478709 }}</ref> All LARP proteins, including human LARPs, contain 2 conserved regions. The first conserved region shares homology with La proteins (called the La motif, see [[Sjogren syndrome antigen B|SSB]]) whereas the second conserved region (called the LA- motif) is restricted to LARP proteins. LARP1 and 1B also contain a conserved "DM15 region" within their C-terminus.<ref>{{cite journal | vauthors = Lahr RM, Mack SM, Héroux A, Blagden SP, Bousquet-Antonelli C, Deragon JM, Berman AJ | title = The La-related protein 1-specific domain repurposes HEAT-like repeats to directly bind a 5'TOP sequence | journal = Nucleic Acids Research | volume = 43 | issue = 16 | pages = 8077–88 | date = September 2015 | pmid = 26206669 | pmc = 4652764 | doi = 10.1093/nar/gkv748 }}</ref> This region is unique and has been shown to be required for RNA-binding. Mouse Larp1 is expressed in [[dorsal root ganglia]] and [[spinal cord]], as well as in developing organs characterized by [[epithelial]]-[[mesenchymal]] interactions.<ref name="pmid10878606" /> Human LARP1 is present at low levels in normal, non-embryonic cells but is highly expressed in epithelial cancers (such as ovarian, colorectal, prostate, non-small cell lung, hepatocellular and cervical cancers).<ref>{{cite journal | vauthors = Stavraka C, Blagden S | title = The La-Related Proteins, a Family with Connections to Cancer | journal = Biomolecules | volume = 5 | issue = 4 | pages = 2701–22 | date = October 2015 | pmid = 26501340 | pmc = 4693254 | doi = 10.3390/biom5042701 }}</ref><ref>{{cite journal | vauthors = Mura M, Hopkins TG, Michael T, Abd-Latip N, Weir J, Aboagye E, Mauri F, Jameson C, Sturge J, Gabra H, Bushell M, Willis AE, Curry E, Blagden SP | title = LARP1 post-transcriptionally regulates mTOR and contributes to cancer progression | journal = Oncogene | volume = 34 | issue = 39 | pages = 5025–36 | date = September 2015 | pmid = 25531318 | pmc = 4430325 | doi = 10.1038/onc.2014.428 }}</ref><ref name = "Hopkins_2016">{{cite journal | vauthors = Hopkins TG, Mura M, Al-Ashtal HA, Lahr RM, Abd-Latip N, Sweeney K, Lu H, Weir J, El-Bahrawy M, Steel JH, Ghaem-Maghami S, Aboagye EO, Berman AJ, Blagden SP | display-authors = 6 | title = The RNA-binding protein LARP1 is a post-transcriptional regulator of survival and tumorigenesis in ovarian cancer | journal = Nucleic Acids Research | volume = 44 | issue = 3 | pages = 1227–46 | date = February 2016 | pmid = 26717985 | pmc = 4756840 | doi = 10.1093/nar/gkv1515 }}</ref><ref>{{cite journal | vauthors = Xie C, Huang L, Xie S, Xie D, Zhang G, Wang P, Peng L, Gao Z | title = LARP1 predict the prognosis for early-stage and AFP-normal hepatocellular carcinoma | journal = Journal of Translational Medicine | volume = 11 | pages = 272 | date = October 2013 | pmid = 24159927 | pmc = 3814951 | doi = 10.1186/1479-5876-11-272 }}</ref> Some studies have shown that high levels of LARP1 protein correlate with worse prognosis in cancer patients.<ref>{{cite journal | vauthors = Ye L, Lin ST, Mi YS, Liu Y, Ma Y, Sun HM, Peng ZH, Fan JW | title = Overexpression of LARP1 predicts poor prognosis of colorectal cancer and is expected to be a potential therapeutic target | journal = Tumour Biology | volume = 37 | issue = 11 | pages = 14585–14594 | date = November 2016 | pmid = 27614686 | pmc = 5126195 | doi = 10.1007/s13277-016-5332-3 }}</ref><ref>{{cite journal | vauthors = Xu Z, Xu J, Lu H, Lin B, Cai S, Guo J, Zang F, Chen R | title = LARP1 is regulated by the XIST/miR-374a axis and functions as an oncogene in non-small cell lung carcinoma | journal = Oncology Reports | volume = 38 | issue = 6 | pages = 3659–3667 | date = December 2017 | pmid = 29039571 | doi = 10.3892/or.2017.6040 }}</ref>


LARP-1 binds a specific type of [[Messenger RNA|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 (protein)|Ras]]-[[Mitogen-activated protein kinase|MAPK]] mRNAs. The cluster of LARP-1 homologs may function to control the expression of key developmental regulators.<ref name="pmid18515547">{{cite journal |vauthors=Nykamp K, Lee MH, Kimble J | title = C. elegans La-related protein, LARP-1, localizes to germline P bodies and attenuates Ras-MAPK signaling during oogenesis | journal = RNA | volume = 14 | issue = 7 | pages = 1378–89 |date=July 2008 | pmid = 18515547 | pmc = 2441978 | doi = 10.1261/rna.1066008 | url =  }}</ref>
LARP1 binds to and regulates the translation of terminal oligopyrimidine motif (TOP [[mRNA]]s) and can directly interact with the [[five-prime cap|5' cap]] of mRNAs.<ref name="Hong_2017">{{cite journal | vauthors = Hong S, Freeberg MA, Han T, Kamath A, Yao Y, Fukuda T, Suzuki T, Kim JK, Inoki K | title = LARP1 functions as a molecular switch for mTORC1-mediated translation of an essential class of mRNAs | journal = eLife | volume = 6 | date = June 2017 | pmid = 28650797 | pmc = 5484620 | doi = 10.7554/elife.25237 }}</ref><ref name="Lahr Fonseca Ciotti Al-Ashtal p. ">{{cite journal | vauthors = Lahr RM, Fonseca BD, Ciotti GE, Al-Ashtal HA, Jia JJ, Niklaus MR, Blagden SP, Alain T, Berman AJ | title = La-related protein 1 (LARP1) binds the mRNA cap, blocking eIF4F assembly on TOP mRNAs | journal = eLife | volume = 6 | date = April 2017 | pmid = 28379136 | pmc = 5419741 | doi = 10.7554/elife.24146 }}</ref> It has also been shown to interact with the 3' end and coding regions (CDS) of other genes.<ref name="Hong_2017" /> LARP1 protein colocalizes with [[P-bodies|stress granules and P-bodies]],<ref name = "Nykamp_2008">{{cite journal | vauthors = Nykamp K, Lee MH, Kimble J | title = C. elegans La-related protein, LARP-1, localizes to germline P bodies and attenuates Ras-MAPK signaling during oogenesis | journal = RNA | volume = 14 | issue = 7 | pages = 1378–89 | date = July 2008 | pmid = 18515547 | pmc = 2441978 | doi = 10.1261/rna.1066008 }}</ref> which function in RNA storage and degradation. It has been suggested that LARP1 functions in [[P-bodies]] to attenuate the abundance of conserved [[Ras (protein)|Ras]]-[[Mitogen-activated protein kinase|MAPK]] mRNAs. The cluster of LARP1 homologs may function to control the expression of key developmental regulators.<ref name = "Nykamp_2008" />


==References==
Several studies have demonstrated that LARP1 deficiency selectively affects the recruitment of TOP mRNAs to polysomes [Reference needed]. In some cancer cells, LARP1 deficiency reduces proliferation and activates apoptotic cell death.<ref name = "Hopkins_2016" /> Even though a decrease abundance of proteins encoded by TOP mRNAs has been reported in LARP1 silenced cells, some researchers believe that this can be explained simply by the reduced number of TOP mRNA transcripts in LARP1-deficient cells.
 
== References ==
{{reflist}}
{{reflist}}


==Further reading==
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Horke S, Reumann K, Schweizer M, Will H, Heise T | title = Nuclear trafficking of La protein depends on a newly identified nucleolar localization signal and the ability to bind RNA | journal = The Journal of Biological Chemistry | volume = 279 | issue = 25 | pages = 26563–70 | date = June 2004 | pmid = 15060081 | doi = 10.1074/jbc.M401017200 }}
| citations =
* {{cite journal | vauthors = Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP | title = Large-scale characterization of HeLa cell nuclear phosphoproteins | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 101 | issue = 33 | pages = 12130–5 | date = August 2004 | pmid = 15302935 | pmc = 514446 | doi = 10.1073/pnas.0404720101 }}
*{{cite journal | author=Strausberg RL |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241  |name-list-format=vanc| author2=Feingold EA  | author3=Grouse LH  | display-authors=3  | last4=Derge  | first4=JG  | last5=Klausner  | first5=RD  | last6=Collins  | first6=FS  | last7=Wagner  | first7=L  | last8=Shenmen  | first8=CM  | last9=Schuler  | first9=GD }}
* {{cite journal | vauthors = Jin J, Smith FD, Stark C, Wells CD, Fawcett JP, Kulkarni S, Metalnikov P, O'Donnell P, Taylor P, Taylor L, Zougman A, Woodgett JR, Langeberg LK, Scott JD, Pawson T | title = Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization | journal = Current Biology | volume = 14 | issue = 16 | pages = 1436–50 | date = August 2004 | pmid = 15324660 | doi = 10.1016/j.cub.2004.07.051 }}
*{{cite journal  | author=Ota T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285  |name-list-format=vanc| author2=Suzuki Y  | author3=Nishikawa T | display-authors=3  | last4=Otsuki  | first4=Tetsuji  | last5=Sugiyama  | first5=Tomoyasu  | last6=Irie  | first6=Ryotaro  | last7=Wakamatsu  | first7=Ai  | last8=Hayashi  | first8=Koji  | last9=Sato  | first9=Hiroyuki }}
* {{cite journal | vauthors = Beausoleil SA, Villén J, Gerber SA, Rush J, Gygi SP | title = A probability-based approach for high-throughput protein phosphorylation analysis and site localization | journal = Nature Biotechnology | volume = 24 | issue = 10 | pages = 1285–92 | date = October 2006 | pmid = 16964243 | doi = 10.1038/nbt1240 }}
*{{cite journal  | author=Horke S |title=Nuclear trafficking of La protein depends on a newly identified nucleolar localization signal and the ability to bind RNA |journal=J. Biol. Chem. |volume=279 |issue= 25 |pages= 26563–70 |year= 2004 |pmid= 15060081 |doi= 10.1074/jbc.M401017200 |name-list-format=vanc| author2=Reumann K  | author3=Schweizer M  | display-authors=3  | last4=Will  | first4=H  | last5=Heise  | first5=T }}
* {{cite journal | vauthors = Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M | title = Global, in vivo, and site-specific phosphorylation dynamics in signaling networks | journal = Cell | volume = 127 | issue = 3 | pages = 635–48 | date = November 2006 | pmid = 17081983 | doi = 10.1016/j.cell.2006.09.026 }}
*{{cite journal | author=Beausoleil SA |title=Large-scale characterization of HeLa cell nuclear phosphoproteins |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 33 |pages= 12130–5 |year= 2004 |pmid= 15302935 |doi= 10.1073/pnas.0404720101 | pmc=514446  |name-list-format=vanc| author2=Jedrychowski M  | author3=Schwartz D  | display-authors=3  | last4=Elias  | first4=JE  | last5=Villén  | first5=J  | last6=Li  | first6=J  | last7=Cohn  | first7=MA  | last8=Cantley  | first8=LC  | last9=Gygi  | first9=SP }}
*{{cite journal | author=Jin J |title=Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization |journal=Curr. Biol. |volume=14 |issue= 16 |pages= 1436–50 |year= 2004 |pmid= 15324660 |doi= 10.1016/j.cub.2004.07.051 |name-list-format=vanc| author2=Smith FD  | author3=Stark C  | display-authors=3  | last4=Wells  | first4=Clark D.  | last5=Fawcett  | first5=James P.  | last6=Kulkarni  | first6=Sarang  | last7=Metalnikov  | first7=Pavel  | last8=O'Donnell  | first8=Paul  | last9=Taylor  | first9=Paul }}
*{{cite journal | author=Gerhard DS |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928  |name-list-format=vanc| author2=Wagner L  | author3=Feingold EA  | display-authors=3  | last4=Shenmen  | first4=CM  | last5=Grouse  | first5=LH  | last6=Schuler  | first6=G  | last7=Klein  | first7=SL  | last8=Old  | first8=S  | last9=Rasooly  | first9=R }}
*{{cite journal  | author=Beausoleil SA |title=A probability-based approach for high-throughput protein phosphorylation analysis and site localization |journal=Nat. Biotechnol. |volume=24 |issue= 10 |pages= 1285–92 |year= 2006 |pmid= 16964243 |doi= 10.1038/nbt1240 |name-list-format=vanc| author2=Villén J  | author3=Gerber SA  | display-authors=3  | last4=Rush  | first4=John  | last5=Gygi  | first5=Steven P }}
*{{cite journal | author=Olsen JV |title=Global, in vivo, and site-specific phosphorylation dynamics in signaling networks |journal=Cell |volume=127 |issue= 3 |pages= 635–48 |year= 2006 |pmid= 17081983 |doi= 10.1016/j.cell.2006.09.026 |name-list-format=vanc| author2=Blagoev B  | author3=Gnad F  | display-authors=3  | last4=Macek  | first4=Boris  | last5=Kumar  | first5=Chanchal  | last6=Mortensen  | first6=Peter  | last7=Mann  | first7=Matthias }}
*{{cite journal  | author=Ewing RM |title=Large-scale mapping of human protein–protein interactions by mass spectrometry |journal=Mol. Syst. Biol. |volume=3 |issue=  1|pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134  | pmc=1847948  |name-list-format=vanc| author2=Chu P  | author3=Elisma F  | display-authors=3  | last4=Li  | first4=Hongyan  | last5=Taylor  | first5=Paul  | last6=Climie  | first6=Shane  | last7=McBroom-Cerajewski  | first7=Linda  | last8=Robinson  | first8=Mark D  | last9=O'Connor  | first9=Liam }}
}}
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Latest revision as of 01:16, 28 November 2018

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Identifiers
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Orthologs
SpeciesHumanMouse
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La-related protein 1 (LARP1) is a 150 kDa protein that in humans is encoded by the LARP1 gene.[1][2][1][3][2] LARP1 is a novel target of the mammalian target of rapamycin complex 1 (mTORC1) signaling pathway, a circuitry often hyperactivated in cancer which regulates cell growth and proliferation primarily through the regulation of protein synthesis.

Function

LARP1 is the largest of a 7 member family of LARP proteins (others are: LARP1B, LARP3 (aka genuine La or SSB), LARP4A, LARP4B, LARP6 and LARP7).[4] All LARP proteins, including human LARPs, 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. LARP1 and 1B also contain a conserved "DM15 region" within their C-terminus.[5] This region is unique and has been shown to be required for RNA-binding. Mouse Larp1 is expressed in dorsal root ganglia and spinal cord, as well as in developing organs characterized by epithelial-mesenchymal interactions.[2] Human LARP1 is present at low levels in normal, non-embryonic cells but is highly expressed in epithelial cancers (such as ovarian, colorectal, prostate, non-small cell lung, hepatocellular and cervical cancers).[6][7][8][9] Some studies have shown that high levels of LARP1 protein correlate with worse prognosis in cancer patients.[10][11]

LARP1 binds to and regulates the translation of terminal oligopyrimidine motif (TOP mRNAs) and can directly interact with the 5' cap of mRNAs.[12][13] It has also been shown to interact with the 3' end and coding regions (CDS) of other genes.[12] LARP1 protein colocalizes with stress granules and P-bodies,[14] which function in RNA storage and degradation. It has been suggested that LARP1 functions in P-bodies to attenuate the abundance of conserved Ras-MAPK mRNAs. The cluster of LARP1 homologs may function to control the expression of key developmental regulators.[14]

Several studies have demonstrated that LARP1 deficiency selectively affects the recruitment of TOP mRNAs to polysomes [Reference needed]. In some cancer cells, LARP1 deficiency reduces proliferation and activates apoptotic cell death.[8] Even though a decrease abundance of proteins encoded by TOP mRNAs has been reported in LARP1 silenced cells, some researchers believe that this can be explained simply by the reduced number of TOP mRNA transcripts in LARP1-deficient cells.

References

  1. ↑ 1.0 1.1 Nagase T, Ishikawa K, Suyama M, Kikuno R, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (October 1998). "Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Research. 5 (5): 277–86. doi:10.1093/dnares/5.5.277. PMID 9872452.
  2. ↑ 2.0 2.1 2.2 Chauvet S, Maurel-Zaffran C, Miassod R, Jullien N, Pradel J, Aragnol D (July 2000). "dlarp, a new candidate Hox target in Drosophila whose orthologue in mouse is expressed at sites of epithelium/mesenchymal interactions". Developmental Dynamics. 218 (3): 401–13. doi:10.1002/1097-0177(200007)218:3<401::AID-DVDY1009>3.0.CO;2-6. PMID 10878606.
  3. ↑ "Entrez Gene: LARP1 La ribonucleoprotein domain family, member 1".
  4. ↑ Bousquet-Antonelli C, Deragon JM (May 2009). "A comprehensive analysis of the La-motif protein superfamily". RNA. 15 (5): 750–64. doi:10.1261/rna.1478709. PMC 2673062. PMID 19299548.
  5. ↑ Lahr RM, Mack SM, Héroux A, Blagden SP, Bousquet-Antonelli C, Deragon JM, Berman AJ (September 2015). "The La-related protein 1-specific domain repurposes HEAT-like repeats to directly bind a 5'TOP sequence". Nucleic Acids Research. 43 (16): 8077–88. doi:10.1093/nar/gkv748. PMC 4652764. PMID 26206669.
  6. ↑ Stavraka C, Blagden S (October 2015). "The La-Related Proteins, a Family with Connections to Cancer". Biomolecules. 5 (4): 2701–22. doi:10.3390/biom5042701. PMC 4693254. PMID 26501340.
  7. ↑ Mura M, Hopkins TG, Michael T, Abd-Latip N, Weir J, Aboagye E, Mauri F, Jameson C, Sturge J, Gabra H, Bushell M, Willis AE, Curry E, Blagden SP (September 2015). "LARP1 post-transcriptionally regulates mTOR and contributes to cancer progression". Oncogene. 34 (39): 5025–36. doi:10.1038/onc.2014.428. PMC 4430325. PMID 25531318.
  8. ↑ 8.0 8.1 Hopkins TG, Mura M, Al-Ashtal HA, Lahr RM, Abd-Latip N, Sweeney K, et al. (February 2016). "The RNA-binding protein LARP1 is a post-transcriptional regulator of survival and tumorigenesis in ovarian cancer". Nucleic Acids Research. 44 (3): 1227–46. doi:10.1093/nar/gkv1515. PMC 4756840. PMID 26717985.
  9. ↑ Xie C, Huang L, Xie S, Xie D, Zhang G, Wang P, Peng L, Gao Z (October 2013). "LARP1 predict the prognosis for early-stage and AFP-normal hepatocellular carcinoma". Journal of Translational Medicine. 11: 272. doi:10.1186/1479-5876-11-272. PMC 3814951. PMID 24159927.
  10. ↑ Ye L, Lin ST, Mi YS, Liu Y, Ma Y, Sun HM, Peng ZH, Fan JW (November 2016). "Overexpression of LARP1 predicts poor prognosis of colorectal cancer and is expected to be a potential therapeutic target". Tumour Biology. 37 (11): 14585–14594. doi:10.1007/s13277-016-5332-3. PMC 5126195. PMID 27614686.
  11. ↑ Xu Z, Xu J, Lu H, Lin B, Cai S, Guo J, Zang F, Chen R (December 2017). "LARP1 is regulated by the XIST/miR-374a axis and functions as an oncogene in non-small cell lung carcinoma". Oncology Reports. 38 (6): 3659–3667. doi:10.3892/or.2017.6040. PMID 29039571.
  12. ↑ 12.0 12.1 Hong S, Freeberg MA, Han T, Kamath A, Yao Y, Fukuda T, Suzuki T, Kim JK, Inoki K (June 2017). "LARP1 functions as a molecular switch for mTORC1-mediated translation of an essential class of mRNAs". eLife. 6. doi:10.7554/elife.25237. PMC 5484620. PMID 28650797.
  13. ↑ Lahr RM, Fonseca BD, Ciotti GE, Al-Ashtal HA, Jia JJ, Niklaus MR, Blagden SP, Alain T, Berman AJ (April 2017). "La-related protein 1 (LARP1) binds the mRNA cap, blocking eIF4F assembly on TOP mRNAs". eLife. 6. doi:10.7554/elife.24146. PMC 5419741. PMID 28379136.
  14. ↑ 14.0 14.1 Nykamp K, Lee MH, Kimble J (July 2008). "C. elegans La-related protein, LARP-1, localizes to germline P bodies and attenuates Ras-MAPK signaling during oogenesis". RNA. 14 (7): 1378–89. doi:10.1261/rna.1066008. PMC 2441978. PMID 18515547.

Further reading

  • Horke S, Reumann K, Schweizer M, Will H, Heise T (June 2004). "Nuclear trafficking of La protein depends on a newly identified nucleolar localization signal and the ability to bind RNA". The Journal of Biological Chemistry. 279 (25): 26563–70. doi:10.1074/jbc.M401017200. PMID 15060081.
  • Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (August 2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proceedings of the National Academy of Sciences of the United States of America. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
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